SitesBLAST
Comparing WP_015448446.1 NCBI__GCF_000230695.2:WP_015448446.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 17 hits to proteins with known functional sites (download)
4lhmA Thymidine phosphorylase from e.Coli with 3'-azido-3'-deoxythymidine (see paper)
46% identity, 96% coverage: 6:432/444 of query aligns to 4:432/440 of 4lhmA
- active site: D83 (= D83), K84 (= K84), H85 (= H85), S86 (= S86), T123 (= T123), D164 (= D164), R171 (= R171), S186 (= S186), K190 (= K190), K191 (= K191)
- binding 3'-azido-3'-deoxythymidine: T87 (= T87), Y168 (= Y168), R171 (= R171), V177 (= V177), S186 (= S186), K190 (= K190), F210 (≠ Q210)
- binding sulfate ion: K84 (= K84), S86 (= S86), S95 (= S95), S113 (= S113), T123 (= T123), A175 (= A175), V177 (= V177), D178 (= D178), R234 (≠ D234), R257 (= R257), K288 (≠ G288), H403 (= H403)
Sites not aligning to the query:
4eadA Thymidine phosphorylase from e.Coli with 3'-azido-2'-fluoro- dideoxyuridine
46% identity, 96% coverage: 6:432/444 of query aligns to 4:432/440 of 4eadA
- active site: D83 (= D83), K84 (= K84), H85 (= H85), S86 (= S86), T123 (= T123), D164 (= D164), R171 (= R171), S186 (= S186), K190 (= K190), K191 (= K191)
- binding 2',3'-dideoxy-2'-fluoro-3'-triaza-1,2-dien-2-ium-1-yluridine: T87 (= T87), Y168 (= Y168), R171 (= R171), V177 (= V177), S186 (= S186), K190 (= K190), F210 (≠ Q210)
4yyyB X-ray structure of the thymidine phosphorylase from salmonella typhimurium in complex with uridine (see paper)
47% identity, 90% coverage: 6:405/444 of query aligns to 4:405/440 of 4yyyB
- active site: D83 (= D83), K84 (= K84), H85 (= H85), S86 (= S86), T123 (= T123), D164 (= D164), R171 (= R171), S186 (= S186), K190 (= K190), K191 (= K191)
- binding uridine: T87 (= T87), G118 (= G118), Y168 (= Y168), R171 (= R171), S186 (= S186), I187 (= I187), K190 (= K190), S248 (≠ R248), Q261 (≠ D261), Y267 (≠ G267)
4yekA X-ray structure of the thymidine phosphorylase from salmonella typhimurium in complex with thymidine (see paper)
47% identity, 90% coverage: 6:405/444 of query aligns to 4:405/440 of 4yekA
- active site: D83 (= D83), K84 (= K84), H85 (= H85), S86 (= S86), T123 (= T123), D164 (= D164), R171 (= R171), S186 (= S186), K190 (= K190), K191 (= K191)
- binding thymidine: T87 (= T87), Y168 (= Y168), R171 (= R171), S186 (= S186), F210 (≠ Q210), S248 (≠ R248), Q261 (≠ D261), Y267 (≠ G267), T384 (≠ A384), D385 (≠ E385)
5ey3A X-ray structure of the thymidine phosphorylase from salmonella typhimurium in complex with cytidine and sulphate
47% identity, 90% coverage: 6:405/444 of query aligns to 6:407/442 of 5ey3A
- active site: D85 (= D83), K86 (= K84), H87 (= H85), S88 (= S86), T125 (= T123), D166 (= D164), R173 (= R171), S188 (= S186), K192 (= K190), K193 (= K191)
- binding 4-amino-1-beta-d-ribofuranosyl-2(1h)-pyrimidinone: R117 (= R115), E130 (= E128)
7m7kB Crystal structure of uridine bound to geobacillus thermoglucosidasius pyrimidine nucleoside phosphorylase pynp
38% identity, 97% coverage: 9:437/444 of query aligns to 5:429/432 of 7m7kB
1brwB The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation (see paper)
39% identity, 96% coverage: 5:432/444 of query aligns to 2:425/433 of 1brwB
- active site: D80 (= D83), K81 (= K84), H82 (= H85), S83 (= S86), T120 (= T123), D161 (= D164), R168 (= R171), S183 (= S186), K187 (= K190), K188 (= K191)
- binding calcium ion: G88 (= G91), L243 (= L246), A246 (≠ E249), E255 (≠ A258)
- binding phosphate ion: H82 (= H85), S83 (= S86), T92 (≠ S95), K108 (≠ M111), S110 (= S113), T120 (= T123)
- binding uracil: H82 (= H85), T84 (= T87), L114 (= L117), Y165 (= Y168), I180 (≠ M183), S183 (= S186), I184 (= I187)
1brwA The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation (see paper)
39% identity, 96% coverage: 5:432/444 of query aligns to 2:425/433 of 1brwA
- active site: H82 (= H85), D161 (= D164), R168 (= R171), S183 (= S186), K187 (= K190)
- binding calcium ion: G88 (= G91), T90 (≠ G93), L243 (= L246), A246 (≠ E249), E255 (≠ A258)
- binding phosphate ion: K81 (= K84), H82 (= H85), S83 (= S86), T92 (≠ S95), K108 (≠ M111)
P77836 Pyrimidine-nucleoside phosphorylase; PYNP; Py-NPase; EC 2.4.2.2 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
37% identity, 97% coverage: 5:436/444 of query aligns to 2:429/433 of P77836
- KHS 81:83 (= KHS 84:86) binding phosphate
- G88 (= G91) binding K(+)
- T90 (≠ G93) binding K(+)
- T92 (≠ S95) binding phosphate
- KMS 108:110 (≠ MIS 111:113) binding phosphate
- T120 (= T123) binding phosphate
- R168 (= R171) binding substrate
- K187 (= K190) binding substrate
- L243 (= L246) binding K(+)
- A246 (≠ E249) binding K(+)
- E255 (≠ A258) binding K(+)
2j0fA Structural basis for non-competitive product inhibition in human thymidine phosphorylase: implication for drug design (see paper)
45% identity, 89% coverage: 9:403/444 of query aligns to 6:408/446 of 2j0fA
- active site: D81 (= D83), K82 (= K84), H83 (= H85), S84 (= S86), T121 (= T123), D162 (= D164), R169 (= R171), S184 (= S186), K188 (= K190), K189 (= K191)
- binding thymine: H83 (= H85), S84 (= S86), T85 (= T87), L115 (= L117), Y166 (= Y168), R169 (= R171), I181 (≠ M183), S184 (= S186), K188 (= K190)
2wk6A Structural features of native human thymidine phosphorylase and in complex with 5-iodouracil (see paper)
44% identity, 89% coverage: 9:403/444 of query aligns to 5:407/446 of 2wk6A
- active site: D80 (= D83), K81 (= K84), H82 (= H85), S83 (= S86), T120 (= T123), D161 (= D164), R168 (= R171), S183 (= S186), K187 (= K190), K188 (= K191)
- binding 5-iodouracil: H82 (= H85), T84 (= T87), L114 (= L117), Y165 (= Y168), R168 (= R171), I180 (≠ M183), S183 (= S186), I184 (= I187), K187 (= K190)
P19971 Thymidine phosphorylase; TP; Gliostatin; Platelet-derived endothelial cell growth factor; PD-ECGF; TdRPase; EC 2.4.2.4 from Homo sapiens (Human) (see 3 papers)
44% identity, 89% coverage: 9:403/444 of query aligns to 39:441/482 of P19971
- Y199 (= Y168) mutation to A: Abolishes catalytic activity.; mutation to F: Reduced catalytic activity.; mutation to L: Reduced catalytic activity.
Sites not aligning to the query:
- 471 S → L: in dbSNP:rs11479
5olnB X-ray structure of the complex pyrimidine-nucleoside phosphorylase from bacillus subtilis at 1.88 a (see paper)
36% identity, 95% coverage: 3:426/444 of query aligns to 1:421/434 of 5olnB
1uouA Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor (see paper)
44% identity, 89% coverage: 9:403/444 of query aligns to 7:399/438 of 1uouA
- active site: D82 (= D83), K83 (= K84), H84 (= H85), S85 (= S86), T122 (= T123), D163 (= D164), R170 (= R171), S185 (= S186), K189 (= K190), K190 (= K191)
- binding 5-chloro-6-(1-(2-iminopyrrolidinyl) methyl) uracil: H84 (= H85), S85 (= S86), T86 (= T87), L116 (= L117), Y167 (= Y168), R170 (= R171), I182 (≠ M183), S185 (= S186), K189 (= K190)
4ga4A Crystal structure of amp phosphorylase n-terminal deletion mutant (see paper)
29% identity, 92% coverage: 10:416/444 of query aligns to 7:402/418 of 4ga4A
- active site: D78 (= D83), V79 (≠ K84), H80 (= H85), S81 (= S86), T119 (= T123), D159 (= D164), A165 (vs. gap), S180 (= S186), K184 (= K190), K185 (= K191)
- binding phosphate ion: H80 (= H85), S81 (= S86), N91 (≠ S95)
4ga6A Crystal structure of amp phosphorylasE C-terminal deletion mutant in complex with substrates (see paper)
30% identity, 92% coverage: 10:416/444 of query aligns to 91:486/493 of 4ga6A
- active site: D162 (= D83), V163 (≠ K84), H164 (= H85), S165 (= S86), T203 (= T123), D243 (= D164), A249 (vs. gap), S264 (= S186), K268 (= K190), K269 (= K191)
- binding adenosine monophosphate: H164 (= H85), S165 (= S86), I166 (≠ T87), S194 (≠ G114), A196 (≠ G116), I197 (≠ L117), T198 (≠ G118), S199 (≠ H119), T203 (= T123), D256 (= D178), M261 (= M183), S264 (= S186), K288 (≠ Q210)
Q5JCX3 AMP phosphorylase; AMPpase; Nucleoside monophosphate phosphorylase; NMP phosphorylase; EC 2.4.2.57 from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) (see paper)
30% identity, 92% coverage: 10:416/444 of query aligns to 91:486/503 of Q5JCX3
- G168 (= G89) binding AMP
- SRAITS 194:199 (≠ GRGLGH 114:119) binding AMP
- T203 (= T123) binding AMP
- D256 (= D178) mutation D->N,A: Almost complete loss of activity.
- S264 (= S186) binding AMP
- K288 (≠ Q210) binding AMP; mutation to A: Almost complete loss of activity.
Query Sequence
>WP_015448446.1 NCBI__GCF_000230695.2:WP_015448446.1
MSAQRATGLIRCKRDGGQLDASQLRAVAQGIGSGAWSEGQIAAFAMAVAWRGMSTPECRQ
FTLALRDSGQCLRWDHLPGPTLDKHSTGGVGDGVSLLLAPLLAACGGYVPMISGRGLGHT
GGTLDKLESLAGYDVHPSTARLRQVVEEVGCAIVGQGDELVPADRRLYAVRDVTATVDVA
DLMVASILSKKLAGGARVLVLDIKTGNGAQLPGMAAARALAGRMLAVAEGSGLDLRVVYS
DMDQLLGREAGNALELRAVLDLLCSRGDNPRLLSLTLELAAALLCTGGLADDRNDAERRL
RRALDTGEAAERFARMVVALGGPADLLQRADVHLARAPIQREVRSPGSGYVVAVDVRALG
QAVVELGGGRSRPGQALDHAVGLAEVLGCGSAVEAGQPLAIIHARRADDAEAVQRRVACA
FRITSEMPPSRPLWQWHVPAERVA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory