SitesBLAST
Comparing Ac3H11_2395 FitnessBrowser__acidovorax_3H11:Ac3H11_2395 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)
33% identity, 89% coverage: 39:335/335 of query aligns to 38:330/334 of 5aovA
- active site: L100 (vs. gap), R241 (= R246), D265 (= D270), E270 (= E275), H288 (= H294)
- binding glyoxylic acid: M52 (≠ L52), L53 (≠ V53), L53 (≠ V53), Y74 (≠ T76), A75 (≠ G77), V76 (≠ K78), G77 (≠ I79), R241 (= R246), H288 (= H294)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ K78), T104 (≠ P105), F158 (≠ Y162), G159 (= G163), R160 (= R164), I161 (= I165), S180 (≠ G184), R181 (= R185), A211 (≠ H216), V212 (≠ L217), P213 (≠ R218), T218 (= T223), I239 (≠ T244), A240 (≠ S245), R241 (= R246), H288 (= H294), G290 (= G296)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
33% identity, 93% coverage: 9:320/335 of query aligns to 16:320/334 of 3kb6B
- active site: S97 (= S101), R231 (= R246), D255 (= D270), E260 (= E275), H294 (= H294)
- binding lactic acid: F49 (≠ L52), S72 (≠ K78), V73 (≠ I79), G74 (= G80), Y96 (≠ G100), R231 (= R246), H294 (= H294)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ I79), Y96 (≠ G100), V101 (≠ P105), G150 (= G163), R151 (= R164), I152 (= I165), D171 (≠ E186), V172 (≠ G187), P203 (≠ R218), T229 (= T244), A230 (≠ S245), R231 (= R246), H294 (= H294), A296 (≠ G296), Y297 (= Y297)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
34% identity, 83% coverage: 44:320/335 of query aligns to 39:304/304 of 1wwkA
- active site: S96 (≠ P105), R230 (= R246), D254 (= D270), E259 (= E275), H278 (= H294)
- binding nicotinamide-adenine-dinucleotide: V100 (vs. gap), G146 (= G161), F147 (≠ Y162), G148 (= G163), R149 (= R164), I150 (= I165), Y168 (≠ W183), D169 (≠ G184), P170 (≠ R185), V201 (≠ L217), P202 (≠ R218), T207 (= T223), T228 (= T244), S229 (= S245), D254 (= D270), H278 (= H294), G280 (= G296)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
33% identity, 87% coverage: 43:335/335 of query aligns to 41:329/332 of 6biiA
- active site: L99 (= L108), R240 (= R246), D264 (= D270), E269 (= E275), H287 (= H294)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ K78), T103 (vs. gap), G156 (= G161), F157 (≠ Y162), G158 (= G163), R159 (= R164), I160 (= I165), A179 (≠ G184), R180 (= R185), S181 (≠ G187), K183 (≠ R189), V211 (≠ L217), P212 (≠ R218), E216 (= E222), T217 (= T223), V238 (≠ T244), A239 (≠ S245), R240 (= R246), D264 (= D270), H287 (= H294), G289 (= G296)
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)
30% identity, 87% coverage: 39:331/335 of query aligns to 40:321/533 of O43175
- T78 (≠ K78) binding
- R135 (≠ Q134) 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 (= RI 164:165) binding
- D175 (≠ G184) binding
- T207 (≠ L217) binding
- CAR 234:236 (≠ TSR 244:246) binding
- D260 (= D270) binding
- V261 (= V271) 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 (≠ HIGY 294:297) 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
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
30% identity, 84% coverage: 39:320/335 of query aligns to 36:305/305 of 6plfA
2eklA Structure of st1218 protein from sulfolobus tokodaii
31% identity, 81% coverage: 50:319/335 of query aligns to 48:307/312 of 2eklA
- active site: S100 (≠ P102), R232 (= R246), D256 (= D270), E261 (= E275), H282 (= H294)
- binding nicotinamide-adenine-dinucleotide: I76 (≠ K78), S100 (≠ P102), G148 (= G161), G150 (= G163), R151 (= R164), I152 (= I165), Y170 (≠ W183), D171 (≠ G184), I172 (≠ R185), L173 (≠ E186), H202 (= H216), V203 (≠ L217), T204 (≠ R218), I212 (≠ L226), T230 (= T244), S231 (= S245), D256 (= D270), G284 (= G296)
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
31% identity, 79% coverage: 39:302/335 of query aligns to 35:286/303 of 6plgA
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
31% identity, 79% coverage: 39:302/335 of query aligns to 35:286/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ W160), G147 (= G161), L148 (≠ Y162), G149 (= G163), R150 (= R164), I151 (= I165), G152 (= G166), D170 (≠ G184), H201 (= H216), T202 (≠ L217), P203 (≠ R218)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
31% identity, 79% coverage: 39:302/335 of query aligns to 35:286/302 of 6rihA
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
31% identity, 79% coverage: 39:302/335 of query aligns to 32:283/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G163), I148 (= I165), Y166 (≠ W183), D167 (≠ G184), P168 (≠ R185), I169 (≠ E186), I170 (≠ G187), H198 (= H216), T199 (≠ L217), L208 (= L226), R228 (= R246)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
31% identity, 79% coverage: 39:302/335 of query aligns to 35:286/301 of 6rj5A
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
31% identity, 79% coverage: 39:302/335 of query aligns to 34:285/297 of 6rj3A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
31% identity, 79% coverage: 39:302/335 of query aligns to 34:285/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (≠ S101), A100 (≠ P105), R149 (= R164), I150 (= I165), Y168 (≠ W183), D169 (≠ G184), P170 (≠ R185), I171 (≠ E186), H200 (= H216), T201 (≠ L217), P202 (≠ R218), T207 (= T223), C228 (≠ T244), A229 (≠ S245), R230 (= R246), H277 (= H294), G279 (= G296)
7dkmA Phgdh covalently linked to oridonin (see paper)
31% identity, 79% coverage: 39:302/335 of query aligns to 36:287/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ K78), A102 (≠ P105), G148 (= G161), R151 (= R164), I152 (= I165), Y170 (≠ W183), D171 (≠ G184), P172 (≠ R185), I173 (≠ E186), H202 (= H216), T203 (≠ L217), P204 (≠ R218), T209 (= T223), C230 (≠ T244), A231 (≠ S245), R232 (= R246), H279 (= H294), G281 (= G296)
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
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
33% identity, 81% coverage: 59:331/335 of query aligns to 56:331/332 of 6v89A
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
33% identity, 81% coverage: 59:331/335 of query aligns to 56:331/331 of 1hl3A
- active site: S99 (≠ P102), R241 (= R246), D265 (= D270), E270 (= E275), H290 (= H294)
- binding nicotinamide-adenine-dinucleotide: T103 (vs. gap), G158 (= G163), R159 (= R164), V160 (≠ I165), D179 (≠ G184), Y181 (≠ E186), H211 (= H216), C212 (≠ L217), G213 (≠ R218), N218 (≠ T223), T239 (= T244), A240 (≠ S245), R241 (= R246), D265 (= D270), H290 (= H294)
- binding : L331 (= L331)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
33% identity, 81% coverage: 59:331/335 of query aligns to 56:331/331 of 1hkuA
- active site: S99 (≠ P102), R241 (= R246), D265 (= D270), E270 (= E275), H290 (= H294)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ K78), T103 (vs. gap), G156 (= G161), G158 (= G163), R159 (= R164), V160 (≠ I165), Y178 (≠ W183), D179 (≠ G184), P180 (≠ R185), Y181 (≠ E186), C212 (≠ L217), N218 (≠ T223), T239 (= T244), A240 (≠ S245), R241 (= R246), H290 (= H294), W293 (vs. gap), L331 (= L331)
6cdfA Human ctbp1 (28-378) (see paper)
33% identity, 81% coverage: 59:331/335 of query aligns to 57:332/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (vs. gap), G157 (= G161), R160 (= R164), V161 (≠ I165), Y179 (≠ W183), D180 (≠ G184), P181 (≠ R185), Y182 (≠ E186), H212 (= H216), C213 (≠ L217), N219 (≠ T223), T240 (= T244), A241 (≠ S245), R242 (= R246), H291 (= H294), W294 (vs. gap)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
32% identity, 80% coverage: 28:296/335 of query aligns to 9:279/526 of 3dc2A
Sites not aligning to the query:
Query Sequence
>Ac3H11_2395 FitnessBrowser__acidovorax_3H11:Ac3H11_2395
MNIVILDDYQDAVRKLHCATRLDAYTAKVYTNTIKGLGQLSVRLKDADIIVLVRERTQIT
RQLVEKLPRLKLIAQTGKIGSHIDVAACTERGIAVAEGVGSPVAPAELTWALVMASMRRL
PQYISNLKHGAWQQSGLKTASMPANFGLGNVLRGKTLGIWGYGRIGQLVAGYGRAFGMNV
RVWGREGSRAQALTDGYQAATTREEFFSQCDVISLHLRLNDETRGLISLEDLSCMKPTSL
LVNTSRAELIEPDALIAALNRGRPGMAAVDVFESEPILQGHALLRLENCICTPHIGYVEQ
DSYELYFGAAFDNVVNFIKGTPTNIVNPGSLQVRR
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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