SitesBLAST
Comparing WP_007472804.1 NCBI__GCF_000170735.1:WP_007472804.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
36% identity, 96% coverage: 4:504/522 of query aligns to 5:507/526 of 3dc2A
- active site: N96 (= N97), R230 (= R232), D254 (= D256), E259 (= E261), H277 (= H279)
- binding serine: Y458 (≠ N456), D460 (= D458), R461 (≠ V459), P462 (= P460), G463 (= G461), A464 (≠ V462), L465 (≠ I463), L484 (= L482)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
35% identity, 96% coverage: 4:504/522 of query aligns to 6:506/525 of 3ddnB
O43175 D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; Malate dehydrogenase; EC 1.1.1.95; EC 1.1.1.399; EC 1.1.1.37 from Homo sapiens (Human) (see 3 papers)
35% identity, 75% coverage: 2:395/522 of query aligns to 8:402/533 of O43175
- T78 (≠ V73) binding NAD(+)
- R135 (= R131) to W: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606949
- RI 155:156 (≠ NI 151:152) binding NAD(+)
- D175 (= D171) binding NAD(+)
- T207 (= T203) binding NAD(+)
- CAR 234:236 (= CAR 230:232) binding NAD(+)
- D260 (= D256) binding NAD(+)
- V261 (= V257) to M: in PHGDHD; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs267606947
- HLGA 283:286 (≠ HIGA 279:282) binding NAD(+)
- A373 (≠ F368) to T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- G377 (= G372) to S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 425 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907988
- 490 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907987
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
38% identity, 58% coverage: 2:305/522 of query aligns to 4:305/305 of 6plfA
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
39% identity, 56% coverage: 2:294/522 of query aligns to 3:297/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ I147), G147 (= G148), L148 (≠ F149), G149 (= G150), R150 (≠ N151), I151 (= I152), G152 (= G153), D170 (= D171), H201 (= H202), T202 (= T203), P203 (= P204)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
39% identity, 56% coverage: 2:294/522 of query aligns to 3:297/302 of 6rihA
7dkmA Phgdh covalently linked to oridonin (see paper)
39% identity, 56% coverage: 2:294/522 of query aligns to 4:298/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ V73), A102 (= A101), G148 (= G148), R151 (≠ N151), I152 (= I152), Y170 (= Y170), D171 (= D171), P172 (= P172), I173 (≠ Y173), H202 (= H202), T203 (= T203), P204 (= P204), T209 (= T209), C230 (= C230), A231 (= A231), R232 (= R232), H279 (= H279), G281 (= G281)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: C14 (≠ A12), K17 (≠ E15), I18 (= I16), E293 (vs. gap)
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
39% identity, 56% coverage: 2:294/522 of query aligns to 3:297/303 of 6plgA
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
39% identity, 56% coverage: 2:294/522 of query aligns to 2:296/297 of 6rj3A
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
39% identity, 56% coverage: 2:294/522 of query aligns to 3:297/301 of 6rj5A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
39% identity, 56% coverage: 2:294/522 of query aligns to 2:296/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N97), A100 (= A101), R149 (≠ N151), I150 (= I152), Y168 (= Y170), D169 (= D171), P170 (= P172), I171 (≠ Y173), H200 (= H202), T201 (= T203), P202 (= P204), T207 (= T209), C228 (= C230), A229 (= A231), R230 (= R232), H277 (= H279), G279 (= G281)
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
39% identity, 56% coverage: 4:294/522 of query aligns to 2:294/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G150), I148 (= I152), Y166 (= Y170), D167 (= D171), P168 (= P172), I169 (≠ Y173), I170 (= I174), H198 (= H202), T199 (= T203), L208 (≠ M212), R228 (= R232)
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
38% identity, 56% coverage: 2:294/522 of query aligns to 2:288/292 of 6plfB
- binding 4-{(1S)-1-[(5-chloro-6-{[(5S)-2-oxo-1,3-oxazolidin-5-yl]methoxy}-1H-indole-2-carbonyl)amino]-2-hydroxyethyl}benzoic acid: R141 (≠ N151), Y160 (= Y170), D161 (= D171), P162 (= P172), I164 (= I174), L179 (≠ F190), T193 (= T203), P194 (= P204), S198 (≠ E208), L202 (≠ M212)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
37% identity, 58% coverage: 1:305/522 of query aligns to 1:304/304 of 1wwkA
- active site: S96 (≠ N97), R230 (= R232), D254 (= D256), E259 (= E261), H278 (= H279)
- binding nicotinamide-adenine-dinucleotide: V100 (≠ A101), G146 (= G148), F147 (= F149), G148 (= G150), R149 (≠ N151), I150 (= I152), Y168 (= Y170), D169 (= D171), P170 (= P172), V201 (≠ T203), P202 (= P204), T207 (= T209), T228 (≠ C230), S229 (≠ A231), D254 (= D256), H278 (= H279), G280 (= G281)
2eklA Structure of st1218 protein from sulfolobus tokodaii
38% identity, 58% coverage: 1:304/522 of query aligns to 5:307/312 of 2eklA
- active site: S100 (≠ N97), R232 (= R232), D256 (= D256), E261 (= E261), H282 (= H279)
- binding nicotinamide-adenine-dinucleotide: I76 (≠ V73), S100 (≠ N97), G148 (= G148), G150 (= G150), R151 (≠ N151), I152 (= I152), Y170 (= Y170), D171 (= D171), I172 (≠ P172), L173 (≠ Y173), H202 (= H202), V203 (≠ T203), T204 (≠ P204), I212 (≠ M212), T230 (≠ C230), S231 (≠ A231), D256 (= D256), G284 (= G281)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
34% identity, 54% coverage: 32:313/522 of query aligns to 35:322/334 of 5aovA
- active site: L100 (≠ N97), R241 (= R232), D265 (= D256), E270 (= E261), H288 (= H279)
- binding glyoxylic acid: M52 (≠ R49), L53 (≠ S50), L53 (≠ S50), Y74 (≠ A71), A75 (≠ G72), V76 (= V73), G77 (= G74), R241 (= R232), H288 (= H279)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V73), T104 (≠ A101), F158 (= F149), G159 (= G150), R160 (≠ N151), I161 (= I152), S180 (≠ D171), R181 (≠ P172), A211 (≠ H202), V212 (≠ T203), P213 (= P204), T218 (= T209), I239 (≠ C230), A240 (= A231), R241 (= R232), H288 (= H279), G290 (= G281)
7cvpA The crystal structure of human phgdh from biortus.
38% identity, 41% coverage: 79:294/522 of query aligns to 33:251/254 of 7cvpA
- binding nicotinamide-adenine-dinucleotide: G101 (= G148), G103 (= G150), R104 (≠ N151), I105 (= I152), Y123 (= Y170), D124 (= D171), P125 (= P172), I126 (≠ Y173), H155 (= H202), T156 (= T203), P157 (= P204), T162 (= T209), C183 (= C230), A184 (= A231), R185 (= R232), H232 (= H279), G234 (= G281)
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
34% identity, 60% coverage: 1:315/522 of query aligns to 7:324/406 of 2p9eA
- active site: N104 (= N97), R236 (= R232), D260 (= D256), E265 (= E261), H288 (= H279)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G150), H157 (≠ N151), I158 (= I152), Y176 (= Y170), D177 (= D171), I178 (vs. gap), H206 (= H202), V207 (≠ T203), P208 (= P204), S212 (≠ E208), A234 (≠ C230), S235 (≠ A231), R236 (= R232), H288 (= H279), G290 (= G281)
P0A9T0 D-3-phosphoglycerate dehydrogenase; PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Escherichia coli (strain K12) (see 2 papers)
34% identity, 60% coverage: 1:315/522 of query aligns to 11:328/410 of P0A9T0
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1psdA The allosteric ligand site in the vmax-type cooperative enzyme phosphoglycerate dehydrogenase (see paper)
34% identity, 60% coverage: 1:315/522 of query aligns to 5:322/404 of 1psdA
- active site: N102 (= N97), R234 (= R232), D258 (= D256), E263 (= E261), H286 (= H279)
- binding nicotinamide-adenine-dinucleotide: N102 (= N97), H155 (≠ N151), I156 (= I152), D175 (= D171), I176 (vs. gap), K179 (vs. gap), H204 (= H202), V205 (≠ T203), P206 (= P204), A232 (≠ C230), S233 (≠ A231), R234 (= R232), H286 (= H279)
Sites not aligning to the query:
Query Sequence
>WP_007472804.1 NCBI__GCF_000170735.1:WP_007472804.1
MKAVICDPIHPAGVEILKKAKDIEVVDASKTPKDELLKIIEDADGVITRSPTPVDEKFLS
HAKKLKAIVRAGVGVDNVDIEACSKRGIVVMNIPTANTLAAVELTMAHLLTAARSFTNAV
WNLKKEHEWNREKWLGIELAGKKLGIIGFGNIGSRVGIRAKALEMDVIAYDPYIDPSKAT
DLGCKYTTDFDEILKCDFITIHTPKTPETINMITKKEIEKMKDGVVLINCARGGLYNEND
VYEGLKSGKIRWLGIDVFEKEPVTEHPFFELENTSVTPHIGANTKESQQRIAIQAAEAII
EALRGSSYPNALNLPINTANTPEWVIKYLELAQKMSYLLSQIIKKPIKKVKVSLSGDISN
EEKSVLTFSLVGLLKNITDNVNYVNALVLAEEKGIETEVKKEKNETYKNLVQIKVLTDEG
EYSISGTMLENHPRVVEFKGFDLEFEPKGKMIFFKNTDVPGVIGEVGMTLAKHNINIADF
RLGRNKEGQAMAVIIVDNDVNEEVLNELKKLKAALSVAYAEI
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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