SitesBLAST
Comparing Echvi_2777 FitnessBrowser__Cola:Echvi_2777 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)
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)
52% identity, 64% coverage: 225:630/630 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)
52% identity, 64% coverage: 227:630/630 of query aligns to 1:406/406 of 1ybaA
- active site: N104 (= N329), R236 (= R461), D260 (= D485), E265 (= E490), H288 (= H513)
- binding 2-oxoglutaric acid: R56 (= R281), S57 (= S282), C79 (= C304), I80 (= I305)
- binding nicotinamide-adenine-dinucleotide: I80 (= I305), F102 (= F327), V108 (= V333), G154 (= G379), G156 (= G381), H157 (≠ N382), I158 (= I383), Y176 (= Y401), D177 (= D402), I178 (= I403), K181 (≠ R406), H206 (= H431), V207 (= V432), P208 (≠ D433), A234 (≠ L459), S235 (= S460), R236 (= R461), H288 (= H513), G290 (= G515)
- binding phosphate ion: G81 (= G306), N83 (= N308)
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
52% identity, 64% coverage: 227:630/630 of query aligns to 1:406/406 of 2p9eA
- active site: N104 (= N329), R236 (= R461), D260 (= D485), E265 (= E490), H288 (= H513)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G381), H157 (≠ N382), I158 (= I383), Y176 (= Y401), D177 (= D402), I178 (= I403), H206 (= H431), V207 (= V432), P208 (≠ D433), S212 (≠ E437), A234 (≠ L459), S235 (= S460), R236 (= R461), H288 (= H513), G290 (= G515)
1psdA The allosteric ligand site in the vmax-type cooperative enzyme phosphoglycerate dehydrogenase (see paper)
52% identity, 64% coverage: 230:630/630 of query aligns to 2:404/404 of 1psdA
- active site: N102 (= N329), R234 (= R461), D258 (= D485), E263 (= E490), H286 (= H513)
- binding nicotinamide-adenine-dinucleotide: N102 (= N329), H155 (≠ N382), I156 (= I383), D175 (= D402), I176 (= I403), K179 (≠ R406), H204 (= H431), V205 (= V432), P206 (≠ D433), A232 (≠ L459), S233 (= S460), R234 (= R461), H286 (= H513)
- binding serine: H338 (= H566), N340 (= N568), R341 (≠ A569), V344 (= V572)
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, 59% coverage: 233:605/630 of query aligns to 56:438/466 of P87228
- S87 (= S264) modified: Phosphoserine
- S258 (≠ R435) modified: Phosphoserine
1sc6D Crystal structure of w139g d-3-phosphoglycerate dehydrogenase complexed with NAD+ (see paper)
48% identity, 64% coverage: 230:630/630 of query aligns to 2:384/384 of 1sc6D
- active site: N102 (= N329), R228 (= R461), D252 (= D485)
- binding nicotinamide-adenine-dinucleotide: P99 (= P326), F100 (= F327), N102 (= N329), T103 (= T330), G146 (= G379), G148 (= G381), H149 (≠ N382), I150 (= I383), Y168 (= Y401), D169 (= D402), I170 (= I403), H198 (= H431), V199 (= V432), P200 (≠ D433), S204 (≠ E437), T205 (≠ N438), S227 (= S460)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
38% identity, 49% coverage: 233:538/630 of query aligns to 1:303/304 of 1wwkA
- active site: S96 (≠ N329), R230 (= R461), D254 (= D485), E259 (= E490), H278 (= H513)
- binding nicotinamide-adenine-dinucleotide: V100 (= V333), G146 (= G379), F147 (≠ Y380), G148 (= G381), R149 (≠ N382), I150 (= I383), Y168 (= Y401), D169 (= D402), P170 (≠ I403), V201 (= V432), P202 (≠ D433), T207 (≠ N438), T228 (≠ L459), S229 (= S460), D254 (= D485), H278 (= H513), G280 (= G515)
2eklA Structure of st1218 protein from sulfolobus tokodaii
35% identity, 47% coverage: 233:528/630 of query aligns to 5:297/312 of 2eklA
- active site: S100 (≠ N329), R232 (= R461), D256 (= D485), E261 (= E490), H282 (= H513)
- binding nicotinamide-adenine-dinucleotide: I76 (= I305), S100 (≠ N329), G148 (= G379), G150 (= G381), R151 (≠ N382), I152 (= I383), Y170 (= Y401), D171 (= D402), I172 (= I403), L173 (≠ V404), H202 (= H431), V203 (= V432), T204 (≠ D433), I212 (= I441), T230 (≠ L459), S231 (= S460), D256 (= D485), G284 (= G515)
7dkmA Phgdh covalently linked to oridonin (see paper)
33% identity, 48% coverage: 235:537/630 of query aligns to 5:303/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ I305), A102 (≠ V333), G148 (= G379), R151 (≠ N382), I152 (= I383), Y170 (= Y401), D171 (= D402), P172 (vs. gap), I173 (vs. gap), H202 (= H431), T203 (≠ V432), P204 (≠ D433), T209 (≠ N438), C230 (≠ L459), A231 (≠ S460), R232 (= R461), H279 (= H513), G281 (= G515)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: C14 (≠ I244), K17 (≠ E247), I18 (= I248), E293 (≠ Q527)
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
33% identity, 48% coverage: 235:537/630 of query aligns to 5:303/305 of 6plfA
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
35% identity, 47% coverage: 235:529/630 of query aligns to 3:298/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N329), A100 (≠ V333), R149 (≠ N382), I150 (= I383), Y168 (= Y401), D169 (= D402), P170 (vs. gap), I171 (vs. gap), H200 (= H431), T201 (≠ V432), P202 (≠ D433), T207 (≠ N438), C228 (≠ L459), A229 (≠ S460), R230 (= R461), H277 (= H513), G279 (= G515)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
35% identity, 47% coverage: 235:529/630 of query aligns to 4:299/301 of 6rj5A
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
33% identity, 48% coverage: 235:537/630 of query aligns to 4:302/303 of 6plgA
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
33% identity, 48% coverage: 235:537/630 of query aligns to 4:302/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ I378), G147 (= G379), L148 (≠ Y380), G149 (= G381), R150 (≠ N382), I151 (= I383), G152 (= G384), D170 (= D402), H201 (= H431), T202 (≠ V432), P203 (≠ D433)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
33% identity, 48% coverage: 235:537/630 of query aligns to 4:302/302 of 6rihA
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, 52% coverage: 235:562/630 of query aligns to 9:339/533 of O43175
- T78 (≠ I305) binding
- R135 (≠ K362) 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 382:383) binding
- D175 (= D402) binding
- T207 (≠ V432) binding
- CAR 234:236 (≠ LSR 459:461) binding
- D260 (= D485) binding
- V261 (= V486) 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 513:516) binding
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
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
33% identity, 48% coverage: 235:537/630 of query aligns to 1:299/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G381), I148 (= I383), Y166 (= Y401), D167 (= D402), P168 (vs. gap), I169 (vs. gap), I170 (= I403), H198 (= H431), T199 (≠ V432), L208 (≠ I441), R228 (= R461)
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
34% identity, 47% coverage: 235:527/630 of query aligns to 3:291/297 of 6rj3A
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
34% identity, 43% coverage: 263:536/630 of query aligns to 34:311/334 of 5aovA
- active site: L100 (≠ N329), R241 (= R461), D265 (= D485), E270 (= E490), H288 (= H513)
- binding glyoxylic acid: M52 (≠ R281), L53 (≠ S282), L53 (≠ S282), Y74 (≠ F303), A75 (≠ C304), V76 (≠ I305), G77 (= G306), R241 (= R461), H288 (= H513)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ I305), T104 (≠ V333), F158 (≠ Y380), G159 (= G381), R160 (≠ N382), I161 (= I383), S180 (≠ D402), R181 (= R406), A211 (≠ H431), V212 (= V432), P213 (≠ D433), T218 (≠ N438), I239 (≠ L459), A240 (≠ S460), R241 (= R461), H288 (= H513), G290 (= G515)
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
34% identity, 47% coverage: 235:529/630 of query aligns to 3:290/292 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 (≠ N382), Y160 (= Y401), D161 (= D402), P162 (vs. gap), I164 (= I403), L179 (= L418), T193 (≠ V432), P194 (≠ D433), S198 (≠ E437), L202 (≠ I441)
Query Sequence
>Echvi_2777 FitnessBrowser__Cola:Echvi_2777
MTTDKKFIIDFDSTFTQVEALDILGEISLRNDPKRDEKLQAIKDITDLGMEGKLNLRESL
ERRIEILQANKSQIAELIDALKQKVSKSFQRNREFFQENAENIYILSNGFKDFITPVVAA
YGLKEENVFANDFIYDEAGNIIDLNKENLLSNNNGKPATIKSLKLEGDVYVIGDGYTDYE
IKASGLANKFYAFTENINRPKVSSKADHIAPSLDEILYVNKMNKKFSYPKSRINVLLLEN
VHPIGVEIMKQEGYNVEVVSSAMSEEELCEKIKNVSIIGIRSKTQITKKVLENANRLMAV
GAFCIGTNQIDLETCQEKGIAVFNAPFSNTRSVVELAISEIIFLMRNLHDKTLKMHQGIW
NKSASGSFEVRGKKLGIIGYGNIGAQLSVLAENMGMNVFYYDIVERLALGNATKIDSLDE
LLETCDIISLHVDGRTENKNILNKEKIFKMKKGAILVNLSRGHVVDVPALRDALESGHLA
GAAVDVFPTEPKNNDEPFESELIGCPNTILTPHIGGSTLEAQENIAQFVPGKIIEYINSG
NTFNSVNFPNIQLPFLKDAHRLIHIHQNAPGVLAKINQVLASYKINIVGQYLKTNEKIGY
VITDIDKRYSNDVIDALKEIEGTIRFRILY
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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