SitesBLAST
Comparing WP_007512075.1 NCBI__GCF_000230695.2:WP_007512075.1 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 20 (the maximum) hits to proteins with known functional sites (download)
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)
60% identity, 100% coverage: 2:410/410 of query aligns to 3:410/410 of P0A9T0
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1ybaA The active form of phosphoglycerate dehydrogenase (see paper)
60% identity, 99% coverage: 4:410/410 of query aligns to 1:406/406 of 1ybaA
- active site: N104 (= N107), R236 (= R239), D260 (= D263), E265 (= E268), H288 (= H291)
- binding 2-oxoglutaric acid: R56 (= R59), S57 (= S60), C79 (= C82), I80 (= I83)
- binding nicotinamide-adenine-dinucleotide: I80 (= I83), F102 (≠ Y105), V108 (= V111), G154 (= G157), G156 (= G159), H157 (= H160), I158 (= I161), Y176 (≠ H179), D177 (= D180), I178 (= I181), K181 (= K184), H206 (= H209), V207 (= V210), P208 (= P211), A234 (= A237), S235 (= S238), R236 (= R239), H288 (= H291), G290 (= G293)
- binding phosphate ion: G81 (= G84), N83 (= N86)
1psdA The allosteric ligand site in the vmax-type cooperative enzyme phosphoglycerate dehydrogenase (see paper)
60% identity, 99% coverage: 7:410/410 of query aligns to 2:404/404 of 1psdA
- active site: N102 (= N107), R234 (= R239), D258 (= D263), E263 (= E268), H286 (= H291)
- binding nicotinamide-adenine-dinucleotide: N102 (= N107), H155 (= H160), I156 (= I161), D175 (= D180), I176 (= I181), K179 (= K184), H204 (= H209), V205 (= V210), P206 (= P211), A232 (= A237), S233 (= S238), R234 (= R239), H286 (= H291)
- binding serine: H338 (= H344), N340 (= N346), R341 (≠ V347), V344 (≠ T350)
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
60% identity, 99% coverage: 4:410/410 of query aligns to 1:406/406 of 2p9eA
- active site: N104 (= N107), R236 (= R239), D260 (= D263), E265 (= E268), H288 (= H291)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G159), H157 (= H160), I158 (= I161), Y176 (≠ H179), D177 (= D180), I178 (= I181), H206 (= H209), V207 (= V210), P208 (= P211), S212 (≠ A215), A234 (= A237), S235 (= S238), R236 (= R239), H288 (= H291), G290 (= G293)
1sc6D Crystal structure of w139g d-3-phosphoglycerate dehydrogenase complexed with NAD+ (see paper)
57% identity, 99% coverage: 7:410/410 of query aligns to 2:384/384 of 1sc6D
- active site: N102 (= N107), R228 (= R239), D252 (= D263)
- binding nicotinamide-adenine-dinucleotide: P99 (= P104), F100 (≠ Y105), N102 (= N107), T103 (= T108), G146 (= G157), G148 (= G159), H149 (= H160), I150 (= I161), Y168 (≠ H179), D169 (= D180), I170 (= I181), H198 (= H209), V199 (= V210), P200 (= P211), S204 (≠ A215), T205 (= T216), S227 (= S238)
8q2iA Crystal structure of ser33 in complex 2hg (2-hydroxyglutarate) and serine
49% identity, 100% coverage: 1:410/410 of query aligns to 4:419/419 of 8q2iA
- binding (2R)-2-hydroxypentanedioic acid: S62 (= S60), C84 (= C82), I85 (= I83)
- binding nicotinamide-adenine-dinucleotide: V113 (= V111), G161 (= G159), H162 (= H160), I163 (= I161), Y181 (≠ H179), D182 (= D180), I183 (= I181), H211 (= H209), V212 (= V210), P213 (= P211), T218 (= T216), A239 (= A237), R241 (= R239), H301 (= H291)
- binding serine: H354 (= H344), N356 (= N346), V357 (= V347), L361 (= L351), N372 (= N364), I373 (= I365)
8pinC Crystal structure of ser33
48% identity, 99% coverage: 5:410/410 of query aligns to 4:419/419 of 8pinC
- binding nicotinamide-adenine-dinucleotide: F103 (≠ Y105), N105 (= N107), V109 (= V111), G155 (= G157), G157 (= G159), H158 (= H160), I159 (= I161), D178 (= D180), I179 (= I181), H207 (= H209), V208 (= V210), P209 (= P211), T214 (= T216), M217 (= M219), A235 (= A237), R237 (= R239), G299 (= G293)
- binding : W144 (≠ Y146), D228 (≠ A230), G229 (= G231)
8q2iB Crystal structure of ser33 in complex 2hg (2-hydroxyglutarate) and serine
48% identity, 100% coverage: 2:410/410 of query aligns to 22:447/447 of 8q2iB
- binding nicotinamide-adenine-dinucleotide: V137 (= V111), G185 (= G159), H186 (= H160), I187 (= I161), Y205 (≠ H179), D206 (= D180), I207 (= I181), H235 (= H209), V236 (= V210), P237 (= P211), A263 (= A237), R265 (= R239), H325 (= H291)
- binding serine: V385 (= V347), G387 (= G349), V388 (≠ T350), L389 (= L351), N400 (= N364), I401 (= I365)
8pioA Crystal structure of ser33 in complex with php (3- phosphohydroxypyruvate)
49% identity, 98% coverage: 9:410/410 of query aligns to 32:443/443 of 8pioA
- binding 2-oxo-3-(phosphonooxy)propanoic acid: R81 (= R59), S82 (= S60)
- binding nicotinamide-adenine-dinucleotide: F127 (≠ Y105), V133 (= V111), G181 (= G159), H182 (= H160), I183 (= I161), D202 (= D180), I203 (= I181), H231 (= H209), V232 (= V210), P233 (= P211), T238 (= T216), A259 (= A237), S260 (= S238), R261 (= R239), H321 (= H291), G323 (= G293)
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)
50% identity, 99% coverage: 5:410/410 of query aligns to 51:466/466 of P87228
- S87 (≠ P42) modified: Phosphoserine
- S258 (≠ T213) 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)
33% identity, 87% coverage: 11:368/410 of query aligns to 8:359/533 of O43175
- T78 (≠ I83) binding NAD(+)
- R135 (≠ K140) 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 (≠ HI 160:161) binding NAD(+)
- D175 (= D180) binding NAD(+)
- T207 (≠ V210) binding NAD(+)
- CAR 234:236 (≠ ASR 237:239) binding NAD(+)
- D260 (= D263) binding NAD(+)
- V261 (= V264) 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 (≠ HIGG 291:294) 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
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
38% identity, 74% coverage: 10:313/410 of query aligns to 1:300/304 of 1wwkA
- active site: S96 (≠ N107), R230 (= R239), D254 (= D263), E259 (= E268), H278 (= H291)
- binding nicotinamide-adenine-dinucleotide: V100 (= V111), G146 (= G157), F147 (≠ Y158), G148 (= G159), R149 (≠ H160), I150 (= I161), Y168 (≠ H179), D169 (= D180), P170 (≠ I181), V201 (= V210), P202 (= P211), T207 (= T216), T228 (≠ A237), S229 (= S238), D254 (= D263), H278 (= H291), G280 (= G293)
7dkmA Phgdh covalently linked to oridonin (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 4:300/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ I83), A102 (≠ V111), G148 (= G157), R151 (≠ H160), I152 (= I161), Y170 (≠ H179), D171 (= D180), P172 (vs. gap), I173 (vs. gap), H202 (= H209), T203 (≠ V210), P204 (= P211), T209 (= T216), C230 (≠ A237), A231 (≠ S238), R232 (= R239), H279 (= H291), G281 (= G293)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: C14 (≠ S21), K17 (≠ D24), I18 (≠ N25), E293 (≠ I305)
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 2:298/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N107), A100 (≠ V111), R149 (≠ H160), I150 (= I161), Y168 (≠ H179), D169 (= D180), P170 (vs. gap), I171 (vs. gap), H200 (= H209), T201 (≠ V210), P202 (= P211), T207 (= T216), C228 (≠ A237), A229 (≠ S238), R230 (= R239), H277 (= H291), G279 (= G293)
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 3:299/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ V156), G147 (= G157), L148 (≠ Y158), G149 (= G159), R150 (≠ H160), I151 (= I161), G152 (= G162), D170 (= D180), H201 (= H209), T202 (≠ V210), P203 (= P211)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 3:299/302 of 6rihA
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 4:300/305 of 6plfA
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 3:299/301 of 6rj5A
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 3:299/303 of 6plgA
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
35% identity, 73% coverage: 11:311/410 of query aligns to 2:297/297 of 6rj3A
Query Sequence
>WP_007512075.1 NCBI__GCF_000230695.2:WP_007512075.1
MQTSYPRQDIKVLLLEGVSASAVDNFRRAGYSQVELHAKSLPEDELKARIADAHIVGIRS
RTQLTADVLAQAKRLIAVGCFCIGTNQVDLAAARRLGVPVFNAPYSNTRSVAELVIAEAI
MLLRGIPQKNAQCHRGGWAKSASGSYETRDKVLGIVGYGHIGTQVGVLAESLGMRVIFHD
IETKLALGNARAVSSLDELLERADVVTLHVPETPATRLMIRREQLAKMRAGAMLINASRG
SVVDIDALAAVLRAGHLAGAAVDVFPLEPKGNDDPFVSPLIGLDNVILTPHIGGSTLEAQ
DNIGIEVASKLVRYSDNGSTLSAVNFPEVALPEHPHSRRLLHIHRNVPGTLSRINELFSA
GNINIDAQFLQTDSEVGYVVIDVSADEAQASELKAKLAAIPGTLRSRVLY
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