SitesBLAST
Comparing WP_012971279.1 NCBI__GCF_000025485.1:WP_012971279.1 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)
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
31% identity, 87% coverage: 49:387/389 of query aligns to 70:405/406 of 2p9eA
- active site: N104 (= N83), R236 (= R231), D260 (= D255), E265 (vs. gap), H288 (= H272)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G146), H157 (≠ A147), I158 (= I148), Y176 (= Y166), D177 (= D167), I178 (≠ V172), H206 (= H201), V207 (= V202), P208 (= P203), S212 (≠ Q207), A234 (≠ F229), S235 (= S230), R236 (= R231), H288 (= H272), G290 (= G274)
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)
30% identity, 97% coverage: 3:381/389 of query aligns to 57:456/466 of P87228
- S87 (vs. gap) modified: Phosphoserine
- S258 (≠ T205) modified: Phosphoserine
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)
34% identity, 78% coverage: 3:306/389 of query aligns to 21:317/533 of O43175
- T78 (≠ A59) binding NAD(+)
- R135 (≠ K127) 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 147:148) binding NAD(+)
- D175 (= D167) binding NAD(+)
- T207 (≠ V202) binding NAD(+)
- CAR 234:236 (≠ FSR 229:231) binding NAD(+)
- D260 (= D255) binding NAD(+)
- V261 (≠ F256) 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 272:275) 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
1ybaA The active form of phosphoglycerate dehydrogenase (see paper)
31% identity, 87% coverage: 49:387/389 of query aligns to 70:405/406 of 1ybaA
- active site: N104 (= N83), R236 (= R231), D260 (= D255), E265 (vs. gap), H288 (= H272)
- binding 2-oxoglutaric acid: C79 (≠ G58), I80 (≠ A59)
- binding nicotinamide-adenine-dinucleotide: I80 (≠ A59), F102 (≠ G81), V108 (= V87), G154 (= G144), G156 (= G146), H157 (≠ A147), I158 (= I148), Y176 (= Y166), D177 (= D167), I178 (≠ V172), K181 (≠ A175), H206 (= H201), V207 (= V202), P208 (= P203), A234 (≠ F229), S235 (= S230), R236 (= R231), H288 (= H272), G290 (= G274)
- binding phosphate ion: G81 (= G60), N83 (= N62)
Sites not aligning to the query:
1psdA The allosteric ligand site in the vmax-type cooperative enzyme phosphoglycerate dehydrogenase (see paper)
31% identity, 87% coverage: 49:387/389 of query aligns to 68:403/404 of 1psdA
- active site: N102 (= N83), R234 (= R231), D258 (= D255), E263 (vs. gap), H286 (= H272)
- binding nicotinamide-adenine-dinucleotide: N102 (= N83), H155 (≠ A147), I156 (= I148), D175 (= D167), I176 (≠ V172), K179 (≠ A175), H204 (= H201), V205 (= V202), P206 (= P203), A232 (≠ F229), S233 (= S230), R234 (= R231), H286 (= H272)
- binding serine: H338 (≠ N324), N340 (= N326), R341 (≠ V327), V344 (≠ M330)
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, 87% coverage: 49:387/389 of query aligns to 74:409/410 of P0A9T0
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7dkmA Phgdh covalently linked to oridonin (see paper)
34% identity, 76% coverage: 3:297/389 of query aligns to 17:304/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ A59), A102 (≠ V87), G148 (= G144), R151 (≠ A147), I152 (= I148), Y170 (= Y166), D171 (= D167), P172 (= P168), I173 (≠ T169), H202 (= H201), T203 (≠ V202), P204 (= P203), T209 (= T208), C230 (≠ F229), A231 (≠ S230), R232 (= R231), H279 (= H272), G281 (= G274)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: K17 (= K3), I18 (= I4), E293 (≠ I286)
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
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
34% identity, 76% coverage: 3:297/389 of query aligns to 16:303/303 of 6plgA
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
34% identity, 76% coverage: 3:297/389 of query aligns to 17:304/305 of 6plfA
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
34% identity, 76% coverage: 3:296/389 of query aligns to 13:299/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G146), I148 (= I148), Y166 (= Y166), D167 (= D167), P168 (= P168), I169 (≠ T169), I170 (= I170), H198 (= H201), T199 (≠ V202), L208 (≠ M211), R228 (= R231)
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
34% identity, 76% coverage: 3:296/389 of query aligns to 16:302/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ V143), G147 (= G144), L148 (= L145), G149 (= G146), R150 (≠ A147), I151 (= I148), G152 (= G149), D170 (= D167), H201 (= H201), T202 (≠ V202), P203 (= P203)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
34% identity, 76% coverage: 3:296/389 of query aligns to 16:302/302 of 6rihA
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
34% identity, 75% coverage: 3:295/389 of query aligns to 16:301/301 of 6rj5A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
34% identity, 75% coverage: 3:294/389 of query aligns to 15:299/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N83), A100 (≠ V87), R149 (≠ A147), I150 (= I148), Y168 (= Y166), D169 (= D167), P170 (= P168), I171 (≠ T169), H200 (= H201), T201 (≠ V202), P202 (= P203), T207 (= T208), C228 (≠ F229), A229 (≠ S230), R230 (= R231), H277 (= H272), G279 (= G274)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
34% identity, 84% coverage: 21:348/389 of query aligns to 32:365/525 of 3ddnB
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
34% identity, 84% coverage: 21:348/389 of query aligns to 31:364/526 of 3dc2A
Sites not aligning to the query:
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
34% identity, 75% coverage: 3:292/389 of query aligns to 15:297/297 of 6rj3A
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
34% identity, 72% coverage: 14:295/389 of query aligns to 21:292/292 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 (≠ A147), Y160 (= Y166), D161 (= D167), P162 (= P168), I164 (= I170), L179 (≠ I188), T193 (≠ V202), P194 (= P203), S198 (≠ Q207), L202 (≠ M211)
1sc6D Crystal structure of w139g d-3-phosphoglycerate dehydrogenase complexed with NAD+ (see paper)
31% identity, 87% coverage: 49:387/389 of query aligns to 68:383/384 of 1sc6D
- active site: N102 (= N83), R228 (= R231), D252 (= D255)
- binding nicotinamide-adenine-dinucleotide: P99 (= P80), F100 (≠ G81), N102 (= N83), T103 (≠ A84), G146 (= G144), G148 (= G146), H149 (≠ A147), I150 (= I148), Y168 (= Y166), D169 (= D167), I170 (≠ V172), H198 (= H201), V199 (= V202), P200 (= P203), S204 (≠ Q207), T205 (= T208), S227 (= S230)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
38% identity, 68% coverage: 33:297/389 of query aligns to 43:303/304 of 1wwkA
- active site: S96 (≠ N83), R230 (= R231), D254 (= D255), E259 (≠ N259), H278 (= H272)
- binding nicotinamide-adenine-dinucleotide: V100 (= V87), G146 (= G144), F147 (≠ L145), G148 (= G146), R149 (≠ A147), I150 (= I148), Y168 (= Y166), D169 (= D167), P170 (= P168), V201 (= V202), P202 (= P203), T207 (= T208), T228 (≠ F229), S229 (= S230), D254 (= D255), H278 (= H272), G280 (= G274)
Query Sequence
>WP_012971279.1 NCBI__GCF_000025485.1:WP_012971279.1
MFKIQTLNNISVVGLERLPRERYEIASEIAHPDAILVRSAKMHDLPIPESVKAIGRAGAG
TNNVPVAEMTKRGVAVFNAPGANANAVKELVLAGMLMSARNIAQAWQFARELQGDDAAIN
EAVEAGKKRFAGFELPGRTLGVVGLGAIGVKVANAARALGMHVIGYDPTITVQRAWQLAS
DVKQALSIDDLLARSDFVTFHVPLTDQTRHMINAERIRILPKGAVLLNFSRQGILDDEAV
IAALDSGQLYAYCCDFPSNRLKDHPRVVTLPHLGASTREAEDNCAIMVADQIRDYLEDGN
VTNSVNFPDIVLPRTEGQRLAIVNSNVPNMLGQISTDLAAAGLNIIDMLNRSRGDVAVTL
VDVDKPCPEDTLALIRSIDGVLSVRCLGG
Or try a new SitesBLAST search
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