SitesBLAST
Comparing WP_011734677.1 NCBI__GCF_000015045.1:WP_011734677.1 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)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
35% identity, 77% coverage: 15:313/390 of query aligns to 28:324/525 of 3ddnB
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
35% identity, 77% coverage: 15:313/390 of query aligns to 27:323/526 of 3dc2A
Sites not aligning to the query:
1ybaA The active form of phosphoglycerate dehydrogenase (see paper)
31% identity, 84% coverage: 60:386/390 of query aligns to 81:405/406 of 1ybaA
- active site: N104 (= N83), R236 (= R230), D260 (= D254), E265 (vs. gap), H288 (= H271)
- binding nicotinamide-adenine-dinucleotide: F102 (≠ G81), V108 (= V87), G154 (= G143), G156 (= G145), H157 (≠ A146), I158 (= I147), Y176 (≠ I169), D177 (≠ S170), I178 (≠ V171), K181 (≠ A174), H206 (= H200), V207 (≠ I201), P208 (= P202), A234 (≠ F228), S235 (= S229), R236 (= R230), H288 (= H271), G290 (= G273)
- binding phosphate ion: G81 (= G60), N83 (= N62)
Sites not aligning to the query:
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)
31% identity, 84% coverage: 60:386/390 of query aligns to 85:409/410 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)
31% identity, 84% coverage: 60:386/390 of query aligns to 79:403/404 of 1psdA
- active site: N102 (= N83), R234 (= R230), D258 (= D254), E263 (vs. gap), H286 (= H271)
- binding nicotinamide-adenine-dinucleotide: N102 (= N83), H155 (≠ A146), I156 (= I147), D175 (≠ S170), I176 (≠ V171), K179 (≠ A174), H204 (= H200), V205 (≠ I201), P206 (= P202), A232 (≠ F228), S233 (= S229), R234 (= R230), H286 (= H271)
- binding serine: H338 (≠ N323), N340 (= N325), R341 (≠ V326), V344 (= V329)
P87228 Putative D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 88% coverage: 45:386/390 of query aligns to 114:465/466 of P87228
- S258 (≠ K204) modified: Phosphoserine
Sites not aligning to the query:
- 87 modified: Phosphoserine
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
31% identity, 86% coverage: 51:386/390 of query aligns to 72:405/406 of 2p9eA
- active site: N104 (= N83), R236 (= R230), D260 (= D254), E265 (vs. gap), H288 (= H271)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G145), H157 (≠ A146), I158 (= I147), Y176 (≠ I169), D177 (≠ S170), I178 (≠ V171), H206 (= H200), V207 (≠ I201), P208 (= P202), S212 (≠ D206), A234 (≠ F228), S235 (= S229), R236 (= R230), H288 (= H271), G290 (= G273)
1sc6D Crystal structure of w139g d-3-phosphoglycerate dehydrogenase complexed with NAD+ (see paper)
31% identity, 86% coverage: 51:386/390 of query aligns to 70:383/384 of 1sc6D
- active site: N102 (= N83), R228 (= R230), D252 (= D254)
- binding nicotinamide-adenine-dinucleotide: P99 (= P80), F100 (≠ G81), N102 (= N83), T103 (≠ A84), G146 (= G143), G148 (= G145), H149 (≠ A146), I150 (= I147), Y168 (≠ I169), D169 (≠ S170), I170 (≠ V171), H198 (= H200), V199 (≠ I201), P200 (= P202), S204 (≠ D206), T205 (= T207), S227 (= S229)
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)
32% identity, 72% coverage: 24:305/390 of query aligns to 40:317/533 of O43175
- T78 (≠ A59) binding NAD(+)
- R135 (vs. gap) 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 (≠ AI 146:147) binding NAD(+)
- D175 (= D166) binding NAD(+)
- T207 (≠ I201) binding NAD(+)
- CAR 234:236 (≠ FSR 228:230) binding NAD(+)
- D260 (= D254) binding NAD(+)
- V261 (≠ F255) 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 (= HLGA 271:274) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 373 A → T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- 377 G → S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
- 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
7dkmA Phgdh covalently linked to oridonin (see paper)
33% identity, 69% coverage: 24:291/390 of query aligns to 36:299/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ A59), A102 (≠ V87), G148 (= G143), R151 (≠ A146), I152 (= I147), Y170 (≠ L165), D171 (= D166), P172 (= P167), I173 (≠ F168), H202 (= H200), T203 (≠ I201), P204 (= P202), T209 (= T207), C230 (≠ F228), A231 (≠ S229), R232 (= R230), H279 (= H271), G281 (= G273)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: E293 (≠ I285)
Sites not aligning to the query:
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: 14, 17, 18
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
33% identity, 69% coverage: 24:291/390 of query aligns to 34:297/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N83), A100 (≠ V87), R149 (≠ A146), I150 (= I147), Y168 (≠ L165), D169 (= D166), P170 (= P167), I171 (≠ F168), H200 (= H200), T201 (≠ I201), P202 (= P202), T207 (= T207), C228 (≠ F228), A229 (≠ S229), R230 (= R230), H277 (= H271), G279 (= G273)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
33% identity, 69% coverage: 24:291/390 of query aligns to 35:298/301 of 6rj5A
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
33% identity, 69% coverage: 24:291/390 of query aligns to 34:297/297 of 6rj3A
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
32% identity, 70% coverage: 24:296/390 of query aligns to 36:304/305 of 6plfA
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
33% identity, 69% coverage: 24:291/390 of query aligns to 35:298/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ I142), G147 (= G143), L148 (= L144), G149 (= G145), R150 (≠ A146), I151 (= I147), G152 (= G148), D170 (= D166), H201 (= H200), T202 (≠ I201), P203 (= P202)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
33% identity, 69% coverage: 24:291/390 of query aligns to 35:298/302 of 6rihA
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
33% identity, 69% coverage: 24:291/390 of query aligns to 35:298/303 of 6plgA
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
33% identity, 69% coverage: 24:291/390 of query aligns to 32:295/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G145), I148 (= I147), Y166 (≠ L165), D167 (= D166), P168 (= P167), I169 (≠ F168), I170 (= I169), H198 (= H200), T199 (≠ I201), L208 (= L210), R228 (= R230)
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
33% identity, 68% coverage: 28:291/390 of query aligns to 34:289/292 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 (≠ A146), Y160 (≠ L165), D161 (= D166), P162 (= P167), I164 (= I169), L179 (= L187), T193 (≠ I201), P194 (= P202), S198 (≠ D206), L202 (= L210)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
36% identity, 68% coverage: 33:296/390 of query aligns to 43:303/304 of 1wwkA
- active site: S96 (≠ N83), R230 (= R230), D254 (= D254), E259 (= E259), H278 (= H271)
- binding nicotinamide-adenine-dinucleotide: V100 (= V87), G146 (= G143), F147 (≠ L144), G148 (= G145), R149 (≠ A146), I150 (= I147), Y168 (≠ L165), D169 (= D166), P170 (= P167), V201 (≠ I201), P202 (= P202), T207 (= T207), T228 (≠ F228), S229 (= S229), D254 (= D254), H278 (= H271), G280 (= G273)
Query Sequence
>WP_011734677.1 NCBI__GCF_000015045.1:WP_011734677.1
MYKIQTLNKIARCGLDQLSRDTYEAATEILNPDAILVRSADMHSMELPPSVLAIARAGAG
VNNIPIPACTQRGIVVFNTPGANANGVKELVIASLFLSSRNLYEGISWANSLAGTENIPE
QIEKGKSRFVGPEIQGKTLGVIGLGAIGVMVANSAANLGMRVLGLDPFISVEAAWKLSHE
VIKAPNLDMLLAESDYITIHIPLKDDTKGLFNAERISRMKKGARLLNFSRSGLVDNTAVK
TAIAEGQLGGYVIDFPEAELLGVDKVLCIPHLGASTPESEDNCAIMAAEQLREYLERGNI
KNSVNYPNCEMAPTGKTRITLLNSNVPKVISRITSTLGEYGLNIDEMLNKNRGEVAYNII
DVSDSVPDELIEKLRQVDGVVAVRLIPDCQ
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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