Protein : Qrob_P0088120.2 Q. robur
Protein Identifier  ? Qrob_P0088120.2 Organism . Name  Quercus robur
Score  90.2 Score Type  egn
Protein Description  (M=3) K07748 - sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating) [EC:1.1.1.170] Code Enzyme  EC:1.1.1.170
Gene Prediction Quality  validated Protein length 

Sequence

Length: 318  
Kegg Orthology  K07748
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0 Synonyms

4 GO Terms

Identifier Name Description
GO:0055114 oxidation-reduction process A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0003854 3-beta-hydroxy-delta5-steroid dehydrogenase activity Catalysis of the reaction: a 3-beta-hydroxy-delta(5)-steroid + NAD+ = a 3-oxo-delta(5)-steroid + NADH + H(+).
GO:0006694 steroid biosynthetic process The chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus; includes de novo formation and steroid interconversion by modification.

32 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pmum:103322301 1 317 + 317 Gaps:39 47.88 589 78.72 7e-146 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3
blastp_kegg lcl|pper:PRUPE_ppa003251mg 1 317 + 317 Gaps:39 47.88 589 78.01 3e-144 hypothetical protein
blastp_kegg lcl|mdm:103419184 1 317 + 317 Gaps:39 47.88 589 76.60 8e-142 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3-like
blastp_kegg lcl|pxb:103933227 1 317 + 317 Gaps:39 47.88 589 75.53 5e-139 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3
blastp_kegg lcl|cmo:103483967 1 317 + 317 Gaps:37 48.11 582 72.14 2e-132 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3
blastp_kegg lcl|csv:101212494 1 317 + 317 Gaps:37 48.11 582 71.79 5e-132 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3-like
blastp_kegg lcl|pop:POPTR_0007s01710g 8 317 + 310 Gaps:43 48.45 580 74.02 2e-131 3-beta hydroxysteroid dehydrogenase/isomerase family protein
blastp_kegg lcl|gmx:100814147 1 317 + 317 Gaps:39 48.35 575 70.14 3e-131 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3-like
blastp_kegg lcl|gmx:100794808 1 317 + 317 Gaps:40 47.61 586 69.18 1e-130 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3-like
blastp_kegg lcl|rcu:RCOM_0454370 1 317 + 317 Gaps:36 48.53 579 70.46 4e-129 hydroxysteroid dehydrogenase putative (EC:1.1.1.170)
blastp_uniprot_sprot sp|A9X4U2|HSDD3_ARATH 11 317 + 307 Gaps:39 47.77 561 67.91 4e-118 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3 OS Arabidopsis thaliana GN 3BETAHSD/D3 PE 2 SV 2
blastp_uniprot_sprot sp|Q9FX01|HSDD1_ARATH 13 317 + 305 Gaps:40 61.73 439 50.55 9e-79 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1 OS Arabidopsis thaliana GN 3BETAHSD/D1 PE 2 SV 1
blastp_uniprot_sprot sp|Q67ZE1|HSDD2_ARATH 1 317 + 317 Gaps:43 50.00 564 49.29 7e-77 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2 OS Arabidopsis thaliana GN 3BETAHSD/D2 PE 2 SV 2
blastp_uniprot_sprot sp|Q9R1J0|NSDHL_MOUSE 11 315 + 305 Gaps:56 69.34 362 45.42 4e-48 Sterol-4-alpha-carboxylate 3-dehydrogenase decarboxylating OS Mus musculus GN Nsdhl PE 2 SV 1
blastp_uniprot_sprot sp|Q15738|NSDHL_HUMAN 3 315 + 313 Gaps:56 69.44 373 42.08 2e-46 Sterol-4-alpha-carboxylate 3-dehydrogenase decarboxylating OS Homo sapiens GN NSDHL PE 1 SV 2
blastp_uniprot_sprot sp|Q5PPL3|NSDHL_RAT 11 315 + 305 Gaps:56 69.34 362 44.22 5e-46 Sterol-4-alpha-carboxylate 3-dehydrogenase decarboxylating OS Rattus norvegicus GN Nsdhl PE 2 SV 1
blastp_uniprot_sprot sp|Q3ZBE9|NSDHL_BOVIN 5 315 + 311 Gaps:58 72.75 356 44.40 8e-46 Sterol-4-alpha-carboxylate 3-dehydrogenase decarboxylating OS Bos taurus GN NSDHL PE 2 SV 1
blastp_uniprot_sprot sp|P53199|ERG26_YEAST 149 315 + 167 Gaps:4 48.42 349 43.79 9e-35 Sterol-4-alpha-carboxylate 3-dehydrogenase decarboxylating OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN ERG26 PE 1 SV 1
blastp_uniprot_sprot sp|A8DZE7|D42E1_DANRE 7 315 + 309 Gaps:62 70.03 387 35.06 2e-30 Short-chain dehydrogenase/reductase family 42E member 1 OS Danio rerio GN sdr42e1 PE 2 SV 1
blastp_uniprot_sprot sp|O43050|ERG26_SCHPO 150 315 + 166 Gaps:2 48.24 340 41.46 4e-29 Sterol-4-alpha-carboxylate 3-dehydrogenase decarboxylating OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN erg26 PE 3 SV 1
rpsblast_cdd gnl|CDD|187673 12 317 + 306 Gaps:56 78.21 335 51.53 6e-87 cd09813 3b-HSD-NSDHL-like_SDR_e human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like extended (e) SDRs. This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects) an X-linked dominant male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana and Saccharomyces cerevisiae ERG26 a 3b-HSD/C-4 decarboxylase involved in the synthesis of ergosterol the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins and include isomerases epimerases oxidoreductases and lyases they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold an NAD(P)(H)-binding region and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range they catalyze a wide range of activities including the metabolism of steroids cofactors carbohydrates lipids aromatic compounds and amino acids and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151 human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys there is often an upstream Ser and/or an Asn contributing to the active site while substrate binding is in the C-terminal region which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys a water molecule stabilized by Asn and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
rpsblast_cdd gnl|CDD|144605 14 317 + 304 Gaps:54 97.14 280 38.24 1e-64 pfam01073 3Beta_HSD 3-beta hydroxysteroid dehydrogenase/isomerase family. The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerisation of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.
rpsblast_cdd gnl|CDD|187552 12 315 + 304 Gaps:58 77.34 331 38.28 2e-45 cd05241 3b-HSD-like_SDR_e 3beta-hydroxysteroid dehydrogenases (3b-HSD)-like extended (e) SDRs. Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids such as pregnenolone to progesterone or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana and Saccharomyces cerevisiae ERG26 a 3b-HSD/C-4 decarboxylase involved in the synthesis of ergosterol the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects) an X-linked dominant male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins and include isomerases epimerases oxidoreductases and lyases they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold an NAD(P)(H)-binding region and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range they catalyze a wide range of activities including the metabolism of steroids cofactors carbohydrates lipids aromatic compounds and amino acids and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151 human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys there is often an upstream Ser and/or an Asn contributing to the active site while substrate binding is in the C-terminal region which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys a water molecule stabilized by Asn and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
rpsblast_cdd gnl|CDD|187672 12 315 + 304 Gaps:60 77.88 339 35.23 6e-28 cd09812 3b-HSD_like_1_SDR_e 3beta-hydroxysteroid dehydrogenase (3b-HSD)-like subgroup1 extended (e) SDRs. An uncharacterized subgroup of the 3b-HSD-like extended-SDR family. Proteins in this subgroup have the characteristic active site tetrad and NAD(P)-binding motif of extended-SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration this activity is essential for the biosynthesis of all classes of hormonal steroids. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins and include isomerases epimerases oxidoreductases and lyases they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold an NAD(P)(H)-binding region and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range they catalyze a wide range of activities including the metabolism of steroids cofactors carbohydrates lipids aromatic compounds and amino acids and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151 human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys there is often an upstream Ser and/or an Asn contributing to the active site while substrate binding is in the C-terminal region which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys a water molecule stabilized by Asn and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
rpsblast_cdd gnl|CDD|187671 13 314 + 302 Gaps:70 76.84 354 32.35 8e-21 cd09811 3b-HSD_HSDB1_like_SDR_e human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like extended (e) SDRs. This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase HSD3B7] and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins and include isomerases epimerases oxidoreductases and lyases they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold an NAD(P)(H)-binding region and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range they catalyze a wide range of activities including the metabolism of steroids cofactors carbohydrates lipids aromatic compounds and amino acids and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151 human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys there is often an upstream Ser and/or an Asn contributing to the active site while substrate binding is in the C-terminal region which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys a water molecule stabilized by Asn and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
rpsblast_cdd gnl|CDD|30800 11 316 + 306 Gaps:65 82.48 314 27.80 8e-17 COG0451 WcaG Nucleoside-diphosphate-sugar epimerases [Cell envelope biogenesis outer membrane / Carbohydrate transport and metabolism].
rpsblast_cdd gnl|CDD|187650 148 276 + 129 Gaps:10 64.50 200 28.68 1e-13 cd08946 SDR_e extended (e) SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins and include isomerases epimerases oxidoreductases and lyases they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold an NAD(P)(H)-binding region and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range they catalyze a wide range of activities including the metabolism of steroids cofactors carbohydrates lipids aromatic compounds and amino acids and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151 human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys there is often an upstream Ser and/or an Asn contributing to the active site while substrate binding is in the C-terminal region which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys a water molecule stabilized by Asn and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
rpsblast_cdd gnl|CDD|201754 14 276 + 263 Gaps:66 93.99 233 27.40 2e-13 pfam01370 Epimerase NAD dependent epimerase/dehydratase family. This family of proteins utilise NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
rpsblast_cdd gnl|CDD|187539 15 278 + 264 Gaps:71 66.98 318 32.39 5e-13 cd05228 AR_FR_like_1_SDR_e uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins extended (e) SDRs. This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins and include isomerases epimerases oxidoreductases and lyases they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold an NAD(P)(H)-binding region and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range they catalyze a wide range of activities including the metabolism of steroids cofactors carbohydrates lipids aromatic compounds and amino acids and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151 human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys there is often an upstream Ser and/or an Asn contributing to the active site while substrate binding is in the C-terminal region which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys a water molecule stabilized by Asn and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
rpsblast_cdd gnl|CDD|187566 13 315 + 303 Gaps:73 84.21 304 31.64 7e-12 cd05256 UDP_AE_SDR_e UDP-N-acetylglucosamine 4-epimerase extended (e) SDRs. This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa WbpP an extended SDR that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins and include isomerases epimerases oxidoreductases and lyases they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold an NAD(P)(H)-binding region and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range they catalyze a wide range of activities including the metabolism of steroids cofactors carbohydrates lipids aromatic compounds and amino acids and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151 human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys there is often an upstream Ser and/or an Asn contributing to the active site while substrate binding is in the C-terminal region which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys a water molecule stabilized by Asn and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

10 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 148 316 169 PF01073 none 3-beta hydroxysteroid dehydrogenase/isomerase family IPR002225
Pfam 14 120 107 PF01073 none 3-beta hydroxysteroid dehydrogenase/isomerase family IPR002225
PANTHER 9 115 107 PTHR10366 none none none
PANTHER 152 317 166 PTHR10366 none none none
PANTHER 152 317 166 PTHR10366:SF242 none none none
SUPERFAMILY 142 316 175 SSF51735 none none none
SUPERFAMILY 8 97 90 SSF51735 none none none
PANTHER 9 115 107 PTHR10366:SF242 none none none
Gene3D 12 114 103 G3DSA:3.40.50.720 none none IPR016040
Gene3D 151 315 165 G3DSA:3.40.50.720 none none IPR016040

0 Localization

1 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2015_nEpiBC_A4 Qrob_Chr07 7 s_1DP9TW_798 v_8128_173 22,61 22,14 22,73 lod 3.1 8.5

0 Targeting