Protein : Qrob_P0531870.2 Q. robur
Protein Identifier  ? Qrob_P0531870.2 Organism . Name  Quercus robur
Score  93.5 Score Type  egn
Protein Description  (M=1) 1.3.99.6 - 3-oxo-5-beta-steroid 4-dehydrogenase. Code Enzyme  EC:1.3.99.6, EC:1.3.1.3
Gene Prediction Quality  validated Protein length 

Sequence

Length: 408  
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0 Synonyms

2 GO Terms

Identifier Name Description
GO:0003824 catalytic activity Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0050662 coenzyme binding Interacting selectively and non-covalently with a coenzyme, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed.

19 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|mdm:103420085 30 407 + 378 Gaps:3 96.93 391 73.09 0.0 3-oxo-Delta(4 5)-steroid 5-beta-reductase-like
blastp_kegg lcl|sly:101055557 30 407 + 378 Gaps:2 97.16 387 71.01 0.0 putative steroid 5beta-reductase (EC:1.3.1.3)
blastp_kegg lcl|tcc:TCM_007184 19 407 + 389 Gaps:2 95.58 407 71.47 0.0 Progesterone 5-beta-reductase putative isoform 1
blastp_kegg lcl|sot:102581216 30 407 + 378 Gaps:2 96.91 388 70.74 0.0 3-oxo-Delta(4 5)-steroid 5-beta-reductase-like
blastp_kegg lcl|vvi:100264565 30 407 + 378 Gaps:2 96.66 389 71.54 0.0 uncharacterized LOC100264565
blastp_kegg lcl|pmum:103335185 30 407 + 378 Gaps:7 96.96 395 70.50 0.0 3-oxo-Delta(4 5)-steroid 5-beta-reductase-like
blastp_kegg lcl|pper:PRUPE_ppa006872mg 30 407 + 378 Gaps:6 96.94 392 70.53 0.0 hypothetical protein
blastp_kegg lcl|fve:101293643 30 407 + 378 Gaps:5 96.92 389 68.44 0.0 3-oxo-Delta(4 5)-steroid 5-beta-reductase-like isoform 1
blastp_kegg lcl|vvi:100247199 30 407 + 378 Gaps:2 96.92 390 69.84 0.0 uncharacterized LOC100247199
blastp_kegg lcl|mtr:MTR_133s1006 30 407 + 378 Gaps:2 96.92 390 68.52 0.0 Progesterone 5-beta-reductase
blastp_pdb 2v6g_A 44 407 + 364 Gaps:1 99.73 364 72.18 0.0 mol:protein length:364 PROGESTERONE 5-BETA-REDUCTASE
blastp_pdb 2v6f_A 44 407 + 364 Gaps:1 99.73 364 72.18 0.0 mol:protein length:364 PROGESTERONE 5-BETA-REDUCTASE
blastp_uniprot_sprot sp|Q6PQJ9|5BPOR_DIGLA 30 407 + 378 Gaps:1 96.92 389 70.56 0.0 3-oxo-Delta(4 5)-steroid 5-beta-reductase OS Digitalis lanata PE 1 SV 1
blastp_uniprot_sprot sp|Q9STX2|VEP1_ARATH 31 407 + 377 Gaps:3 96.91 388 66.76 0.0 3-oxo-Delta(4 5)-steroid 5-beta-reductase OS Arabidopsis thaliana GN VEP1 PE 1 SV 1
blastp_uniprot_sprot sp|K7WDL7|IRIS_CATRO 42 407 + 366 Gaps:7 93.04 388 61.22 2e-161 Iridoid synthase OS Catharanthus roseus PE 1 SV 1
blastp_uniprot_sprot sp|O74913|YJ72_SCHPO 45 407 + 363 Gaps:72 98.02 405 25.44 3e-31 Uncharacterized protein C757.02c OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN SPCC757.02c PE 4 SV 1
rpsblast_cdd gnl|CDD|187652 45 347 + 303 Gaps:15 100.00 308 46.75 1e-108 cd08948 5beta-POR_like_SDR_a progesterone 5-beta-reductase-like proteins (5beta-POR) atypical (a) SDRs. 5beta-POR catalyzes the reduction of progesterone to 5beta-pregnane-3 20-dione in Digitalis plants. This subgroup of atypical-extended SDRs shares the structure of an extended SDR but has a different glycine-rich nucleotide binding motif (GXXGXXG) and lacks the YXXXK active site motif of classical and extended SDRs. Tyr-179 and Lys 147 are present in the active site but not in the usual SDR configuration. Given these differences it has been proposed that this subfamily represents a new SDR class. Other atypical SDRs include biliverdin IX beta reductase (BVR-B aka flavin reductase) NMRa (a negative transcriptional regulator of various fungi) phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases phenylpropene synthases eugenol synthase triphenylmethane reductase isoflavone reductases and others. 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. In addition to the Rossmann fold core region typical of all SDRs extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids and typically have a TGXXGXXG cofactor binding motif. 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|187537 46 293 + 248 Gaps:73 99.43 176 27.43 4e-19 cd05226 SDR_e_a Extended (e) and atypical (a) SDRs. Extended or atypical short-chain dehydrogenases/reductases (SDRs aka tyrosine-dependent oxidoreductases) 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. 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. Atypical SDRs include biliverdin IX beta reductase (BVR-B aka flavin reductase) NMRa (a negative transcriptional regulator of various fungi) progesterone 5-beta-reductase like proteins phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases phenylpropene synthases eugenol synthase triphenylmethane reductase isoflavone reductases and others. 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. 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|30800 47 360 + 314 Gaps:43 97.13 314 21.31 2e-10 COG0451 WcaG Nucleoside-diphosphate-sugar epimerases [Cell envelope biogenesis outer membrane / Carbohydrate transport and metabolism].

5 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 45 407 363 PTHR32487:SF0 none none none
Gene3D 45 315 271 G3DSA:3.40.50.720 none none IPR016040
Pfam 46 270 225 PF01370 none NAD dependent epimerase/dehydratase family IPR001509
SUPERFAMILY 45 333 289 SSF51735 none none none
PANTHER 45 407 363 PTHR32487 none none none

0 Localization

6 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_nEpis_3P Qrob_Chr12 12 s_1AOES6_1466 s_1B0DDG_1094 28,97 28,55 30,1 lod 3.6 8.4
Champenoux_2015_nEpis_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 26,53 25,47 27,72 lod 4.4 8.9
Bourran2_2014_nP_A4 Qrob_Chr11 11 s_1B58GB_1413 s_1A5BYY_1671 11,15 0 42,38 lod 1,8913 4,5
Bourran2_2002_QTL16_peak_Bud_burst_A4 Qrob_Chr11 11 s_A9OIA_166 s_1C6WBF_114 21,23 2,83 42,83 lod 5,1 7,2
Bourran2_2015_nSeqBC_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 26,06 25,47 27,72 lod 3.6 7.1
Champenoux_2015_nSecLBD_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 25,78 25,47 27,72 lod 6.3 16.6

0 Targeting