blastp_kegg |
lcl|pop:POPTR_0001s24380g
|
1 |
169 |
+ |
169 |
Gaps:35 |
62.01 |
329 |
60.78 |
5e-68 |
POPTRDRAFT_706198 UDP-GLUCURONIC ACID DECARBOXYLASE family protein
|
blastp_kegg |
lcl|atr:s00092p00147500
|
15 |
182 |
+ |
168 |
Gaps:28 |
66.43 |
286 |
51.58 |
1e-48 |
AMTR_s00092p00147500 hypothetical protein
|
blastp_kegg |
lcl|pvu:PHAVU_011G065700g
|
1 |
169 |
+ |
169 |
none |
34.50 |
342 |
95.76 |
5e-47 |
hypothetical protein
|
blastp_kegg |
lcl|vvi:100245048
|
1 |
169 |
+ |
169 |
none |
34.10 |
346 |
98.31 |
5e-47 |
UDP-glucuronic acid decarboxylase 1-like
|
blastp_kegg |
lcl|gmx:100819843
|
1 |
169 |
+ |
169 |
none |
34.50 |
342 |
96.61 |
5e-47 |
UDP-glucuronic acid decarboxylase 1-like
|
blastp_kegg |
lcl|gmx:100816443
|
1 |
169 |
+ |
169 |
none |
34.50 |
342 |
96.61 |
6e-47 |
UDP-glucuronic acid decarboxylase 6-like
|
blastp_kegg |
lcl|tcc:TCM_041878
|
1 |
169 |
+ |
169 |
none |
34.10 |
346 |
96.61 |
7e-47 |
UDP-XYL synthase 5 isoform 5
|
blastp_kegg |
lcl|mtr:MTR_2g096660
|
1 |
169 |
+ |
169 |
none |
33.62 |
351 |
96.61 |
7e-47 |
UDP-glucuronic acid decarboxylase
|
blastp_kegg |
lcl|mus:103987002
|
1 |
169 |
+ |
169 |
none |
34.10 |
346 |
95.76 |
7e-47 |
UDP-glucuronic acid decarboxylase 6-like
|
blastp_kegg |
lcl|tcc:TCM_042808
|
1 |
169 |
+ |
169 |
none |
34.40 |
343 |
94.92 |
1e-46 |
UDP-XYL synthase 6
|
blastp_pdb |
4ef7_B
|
89 |
167 |
+ |
79 |
none |
23.44 |
337 |
64.56 |
6e-30 |
mol:protein length:337 UDP-glucuronic acid decarboxylase 1
|
blastp_pdb |
4ef7_A
|
89 |
167 |
+ |
79 |
none |
23.44 |
337 |
64.56 |
6e-30 |
mol:protein length:337 UDP-glucuronic acid decarboxylase 1
|
blastp_pdb |
2b69_A
|
89 |
167 |
+ |
79 |
none |
23.03 |
343 |
64.56 |
7e-30 |
mol:protein length:343 UDP-glucuronate decarboxylase 1
|
blastp_pdb |
3slg_F
|
69 |
167 |
+ |
99 |
Gaps:18 |
28.76 |
372 |
33.64 |
2e-07 |
mol:protein length:372 PbgP3 protein
|
blastp_pdb |
3slg_E
|
69 |
167 |
+ |
99 |
Gaps:18 |
28.76 |
372 |
33.64 |
2e-07 |
mol:protein length:372 PbgP3 protein
|
blastp_pdb |
3slg_D
|
69 |
167 |
+ |
99 |
Gaps:18 |
28.76 |
372 |
33.64 |
2e-07 |
mol:protein length:372 PbgP3 protein
|
blastp_pdb |
3slg_C
|
69 |
167 |
+ |
99 |
Gaps:18 |
28.76 |
372 |
33.64 |
2e-07 |
mol:protein length:372 PbgP3 protein
|
blastp_pdb |
3slg_B
|
69 |
167 |
+ |
99 |
Gaps:18 |
28.76 |
372 |
33.64 |
2e-07 |
mol:protein length:372 PbgP3 protein
|
blastp_pdb |
3slg_A
|
69 |
167 |
+ |
99 |
Gaps:18 |
28.76 |
372 |
33.64 |
2e-07 |
mol:protein length:372 PbgP3 protein
|
blastp_uniprot_sprot |
sp|Q9FIE8|UXS3_ARATH
|
1 |
169 |
+ |
169 |
none |
34.50 |
342 |
94.07 |
9e-46 |
UDP-glucuronic acid decarboxylase 3 OS Arabidopsis thaliana GN UXS3 PE 1 SV 1
|
blastp_uniprot_sprot |
sp|Q9SN95|UXS5_ARATH
|
1 |
169 |
+ |
169 |
none |
34.60 |
341 |
94.92 |
1e-45 |
UDP-glucuronic acid decarboxylase 5 OS Arabidopsis thaliana GN UXS5 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q9ZV36|UXS6_ARATH
|
1 |
169 |
+ |
169 |
none |
34.40 |
343 |
93.22 |
7e-45 |
UDP-glucuronic acid decarboxylase 6 OS Arabidopsis thaliana GN UXS6 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q8S8T4|UXS4_ARATH
|
64 |
169 |
+ |
106 |
Gaps:2 |
24.38 |
443 |
59.26 |
2e-33 |
UDP-glucuronic acid decarboxylase 4 OS Arabidopsis thaliana GN UXS4 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q9LZI2|UXS2_ARATH
|
64 |
169 |
+ |
106 |
Gaps:2 |
24.27 |
445 |
59.26 |
3e-33 |
UDP-glucuronic acid decarboxylase 2 OS Arabidopsis thaliana GN UXS2 PE 1 SV 1
|
blastp_uniprot_sprot |
sp|Q8VZC0|UXS1_ARATH
|
6 |
169 |
+ |
164 |
none |
25.52 |
435 |
66.67 |
2e-30 |
UDP-glucuronic acid decarboxylase 1 OS Arabidopsis thaliana GN UXS1 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q8NBZ7|UXS1_HUMAN
|
89 |
167 |
+ |
79 |
none |
18.81 |
420 |
64.56 |
3e-29 |
UDP-glucuronic acid decarboxylase 1 OS Homo sapiens GN UXS1 PE 1 SV 1
|
blastp_uniprot_sprot |
sp|Q5R885|UXS1_PONAB
|
89 |
167 |
+ |
79 |
none |
18.81 |
420 |
64.56 |
3e-29 |
UDP-glucuronic acid decarboxylase 1 OS Pongo abelii GN UXS1 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q91XL3|UXS1_MOUSE
|
89 |
167 |
+ |
79 |
none |
18.81 |
420 |
64.56 |
3e-29 |
UDP-glucuronic acid decarboxylase 1 OS Mus musculus GN Uxs1 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q5PQX0|UXS1_RAT
|
89 |
167 |
+ |
79 |
none |
18.81 |
420 |
64.56 |
3e-29 |
UDP-glucuronic acid decarboxylase 1 OS Rattus norvegicus GN Uxs1 PE 1 SV 1
|
rpsblast_cdd |
gnl|CDD|187541
|
3 |
169 |
+ |
167 |
Gaps:1 |
38.36 |
305 |
66.67 |
3e-42 |
cd05230 UGD_SDR_e UDP-glucuronate decarboxylase (UGD) and related proteins extended (e) SDRs. UGD catalyzes the formation of UDP-xylose from UDP-glucuronate it is an extended-SDR and has the characteristic glycine-rich NAD-binding pattern TGXXGXXG and active site tetrad. 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.
|