SitesBLAST
Comparing CA265_RS12240 FitnessBrowser__Pedo557:CA265_RS12240 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)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
36% identity, 83% coverage: 42:299/311 of query aligns to 45:317/334 of 5aovA
- active site: L100 (≠ N97), R241 (= R222), D265 (= D246), E270 (= E251), H288 (= H270)
- binding glyoxylic acid: M52 (≠ R49), L53 (≠ G50), L53 (≠ G50), Y74 (≠ C71), A75 (≠ G72), V76 (= V73), G77 (= G74), R241 (= R222), H288 (= H270)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V73), T104 (≠ I101), F158 (≠ L149), G159 (= G150), R160 (≠ N151), I161 (= I152), S180 (= S171), R181 (= R172), A211 (≠ H192), V212 (≠ L193), P213 (= P194), T218 (= T199), I239 (≠ T220), A240 (= A221), R241 (= R222), H288 (= H270), G290 (≠ A272)
2eklA Structure of st1218 protein from sulfolobus tokodaii
33% identity, 80% coverage: 46:294/311 of query aligns to 49:306/312 of 2eklA
- active site: S100 (≠ N97), R232 (= R222), D256 (= D246), E261 (= E251), H282 (= H270)
- binding nicotinamide-adenine-dinucleotide: I76 (≠ V73), S100 (≠ N97), G148 (= G148), G150 (= G150), R151 (≠ N151), I152 (= I152), Y170 (≠ W170), D171 (vs. gap), I172 (vs. gap), L173 (vs. gap), H202 (= H192), V203 (≠ L193), T204 (≠ P194), I212 (= I202), T230 (= T220), S231 (≠ A221), D256 (= D246), G284 (≠ A272)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
31% identity, 94% coverage: 6:296/311 of query aligns to 3:320/334 of 3kb6B
- active site: S97 (≠ N97), R231 (= R222), D255 (= D246), E260 (= E251), H294 (= H270)
- binding lactic acid: F49 (≠ I47), S72 (≠ G72), V73 (= V73), G74 (= G74), Y96 (≠ S96), R231 (= R222), H294 (= H270)
- binding nicotinamide-adenine-dinucleotide: V73 (= V73), Y96 (≠ S96), V101 (≠ I101), G150 (= G150), R151 (≠ N151), I152 (= I152), D171 (≠ S171), V172 (vs. gap), P203 (= P194), T229 (= T220), A230 (= A221), R231 (= R222), H294 (= H270), A296 (= A272), Y297 (≠ S273)
7dkmA Phgdh covalently linked to oridonin (see paper)
37% identity, 77% coverage: 42:280/311 of query aligns to 43:286/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ V73), A102 (≠ I101), G148 (= G148), R151 (≠ N151), I152 (= I152), Y170 (≠ W170), D171 (vs. gap), P172 (vs. gap), I173 (vs. gap), H202 (= H192), T203 (≠ L193), P204 (= P194), T209 (= T199), C230 (≠ T220), A231 (= A221), R232 (= R222), H279 (= H270), G281 (≠ T275)
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, 293
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
37% identity, 77% coverage: 42:280/311 of query aligns to 42:285/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (= L147), G147 (= G148), L148 (= L149), G149 (= G150), R150 (≠ N151), I151 (= I152), G152 (= G153), D170 (vs. gap), H201 (= H192), T202 (≠ L193), P203 (= P194)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
37% identity, 77% coverage: 42:280/311 of query aligns to 42:285/302 of 6rihA
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
37% identity, 77% coverage: 42:280/311 of query aligns to 41:284/297 of 6rj3A
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
37% identity, 77% coverage: 42:280/311 of query aligns to 42:285/303 of 6plgA
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
37% identity, 77% coverage: 42:280/311 of query aligns to 42:285/301 of 6rj5A
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
37% identity, 77% coverage: 42:280/311 of query aligns to 43:286/305 of 6plfA
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
37% identity, 77% coverage: 42:280/311 of query aligns to 41:284/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N97), A100 (≠ I101), R149 (≠ N151), I150 (= I152), Y168 (≠ W170), D169 (vs. gap), P170 (vs. gap), I171 (vs. gap), H200 (= H192), T201 (≠ L193), P202 (= P194), T207 (= T199), C228 (≠ T220), A229 (= A221), R230 (= R222), H277 (= H270), G279 (≠ T275)
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
37% identity, 77% coverage: 42:280/311 of query aligns to 39:282/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G150), I148 (= I152), Y166 (≠ W170), D167 (vs. gap), P168 (vs. gap), I169 (vs. gap), I170 (vs. gap), H198 (= H192), T199 (≠ L193), L208 (≠ I202), R228 (= R222)
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)
37% identity, 77% coverage: 42:280/311 of query aligns to 47:290/533 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 (vs. gap) binding NAD(+)
- T207 (≠ L193) binding NAD(+)
- CAR 234:236 (≠ TAR 220:222) binding NAD(+)
- D260 (= D246) binding NAD(+)
- V261 (= V247) 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
- H---LGA 283:286 (≠ HAASLTA 270:276) 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
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
33% identity, 96% coverage: 2:299/311 of query aligns to 1:316/332 of 6biiA
- active site: L99 (≠ N97), R240 (= R222), D264 (= D246), E269 (= E251), H287 (= H270)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (= V73), T103 (≠ I101), G156 (= G148), F157 (≠ L149), G158 (= G150), R159 (≠ N151), I160 (= I152), A179 (≠ S171), R180 (= R172), S181 (= S173), K183 (vs. gap), V211 (≠ L193), P212 (= P194), E216 (= E198), T217 (= T199), V238 (≠ T220), A239 (= A221), R240 (= R222), D264 (= D246), H287 (= H270), G289 (≠ A272)
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
38% identity, 72% coverage: 58:280/311 of query aligns to 49:276/292 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 (≠ W170), D161 (vs. gap), P162 (vs. gap), I164 (vs. gap), L179 (= L179), T193 (≠ L193), P194 (= P194), S198 (≠ E198), L202 (≠ I202)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
34% identity, 94% coverage: 4:296/311 of query aligns to 2:304/304 of 1wwkA
- active site: S96 (≠ N97), R230 (= R222), D254 (= D246), E259 (= E251), H278 (= H270)
- binding nicotinamide-adenine-dinucleotide: V100 (≠ I101), G146 (= G148), F147 (≠ L149), G148 (= G150), R149 (≠ N151), I150 (= I152), Y168 (≠ W170), D169 (vs. gap), P170 (vs. gap), V201 (≠ L193), P202 (= P194), T207 (= T199), T228 (= T220), S229 (≠ A221), D254 (= D246), H278 (= H270), G280 (≠ A272)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
37% identity, 94% coverage: 5:297/311 of query aligns to 5:305/525 of 3ddnB
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
37% identity, 94% coverage: 5:297/311 of query aligns to 4:304/526 of 3dc2A
Sites not aligning to the query:
8wpiA Anabaena mcyi with prebound NAD and soaked NADP
35% identity, 83% coverage: 42:299/311 of query aligns to 40:309/318 of 8wpiA
- binding nicotinamide-adenine-dinucleotide: V99 (≠ I101), G146 (= G148), G148 (= G150), R149 (≠ N151), I150 (= I152), Y169 (≠ W170), D170 (vs. gap), P171 (vs. gap), Y172 (vs. gap), H202 (= H192), P203 (≠ L193), E204 (≠ P194), E208 (= E198), T209 (= T199), T230 (= T220), S231 (≠ A221), R232 (= R222), H280 (= H270)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: Y48 (≠ G50), S69 (≠ C71), G70 (= G72), F71 (≠ V73), G72 (= G74), L110 (= L112), K113 (≠ D115), F116 (≠ R118), F226 (= F216), R232 (= R222), D273 (≠ P263), N274 (= N264), V284 (≠ L274), T285 (= T275), G289 (≠ Y279)
Sites not aligning to the query:
8wprA Anabaena mcyi r166a with prebound NAD and malate
35% identity, 83% coverage: 42:299/311 of query aligns to 42:311/320 of 8wprA
- binding nicotinamide-adenine-dinucleotide: S97 (≠ N97), V101 (≠ I101), G150 (= G150), A151 (≠ N151), I152 (= I152), Y171 (≠ W170), D172 (vs. gap), P173 (vs. gap), Y174 (vs. gap), P205 (≠ L193), E206 (≠ P194), E210 (= E198), T211 (= T199), T232 (= T220), S233 (≠ A221), R234 (= R222), H282 (= H270), G285 (≠ S273)
Query Sequence
>CA265_RS12240 FitnessBrowser__Pedo557:CA265_RS12240
MRKNVLLLETIAEEALALLQENVNVFTGYDEAGLKDTLNNVEVHAIITRGKKHIDKTLMD
ACPHLEVAARCGVGLDNVDVDEASARKIRVINAPGSNAATIAEHTLALMLMLMRDMHRSV
NHVKQNNWNWRNQYAGDELNGKTLGILGLGNIGKRVAKLGDAFGMKVLCWSRSVQDLPLD
EVLQQSDVVSLHLPLSNETNEIIGASQLALMKPKAFLINTARGALIDHAALLDALNAGTI
AGFAADVLPDEPPLQSLAVVQHPNALVTPHAASLTASTYKQMCLLTVRNVLSVLAGQQPE
LNSIYNRNAFI
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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