SitesBLAST
Comparing WP_157196862.1 NCBI__GCF_000017185.1:WP_157196862.1 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)
Q72IW9 Isocitrate/homoisocitrate dehydrogenase; Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.286 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see 4 papers)
48% identity, 98% coverage: 6:343/344 of query aligns to 4:334/334 of Q72IW9
- E57 (≠ K58) mutation to V: Confers enzyme activity with 3-isopropylmalate; when associated with I-72; M-85; A-86; T-208; Y-217; M-238 and M-310.
- ATS 70:72 (≠ VST 71:73) binding NADH
- S72 (≠ T73) binding in other chain; mutation to I: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; M-85; A-86; T-208; Y-217; M-238 and M-310.
- R85 (≠ L89) binding in other chain; mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; A-86; T-208; Y-217; M-238 and M-310.; mutation to V: Confers low enzyme activity with 3-isopropylmalate. Reduces activity with homoisocitrate. Abolishes activity with isocitrate.
- Y86 (≠ T90) mutation to A: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; T-208; Y-217; M-238 and M-310.
- R88 (= R92) binding in other chain
- R98 (= R102) binding in other chain
- R118 (= R122) binding in other chain
- Y125 (= Y129) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (≠ L141) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K177) binding (2R,3S)-homoisocitrate
- N173 (= N179) binding (2R,3S)-homoisocitrate; binding NADH
- D204 (= D213) binding Mg(2+)
- M208 (= M217) mutation to T: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; M-238 and M-310.
- F217 (= F226) mutation to Y: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; M-238 and M-310.
- D228 (= D237) binding Mg(2+)
- D232 (= D241) binding Mg(2+)
- V238 (≠ L247) mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; and M-310.
- GSAPD 261:265 (= GSAPD 270:274) binding NADH
- N273 (= N282) binding NADH
- R310 (≠ I319) mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; and M-238.
4yb4A Crystal structure of homoisocitrate dehydrogenase from thermus thermophilus in complex with homoisocitrate, magnesium ion (ii) and nadh
48% identity, 98% coverage: 6:343/344 of query aligns to 3:333/333 of 4yb4A
- active site: Y124 (= Y129), K170 (= K177), D203 (= D213), D227 (= D237), D231 (= D241)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ T73), R84 (≠ L89), R87 (= R92), R97 (= R102), R117 (= R122), Y124 (= Y129), D227 (= D237)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I15), A69 (≠ V71), T70 (≠ S72), S71 (≠ T73), I201 (≠ L211), N204 (≠ A214), L240 (= L250), E256 (= E266), H259 (= H269), G260 (= G270), S261 (= S271), A262 (= A272), D264 (= D274), I265 (= I275), N272 (= N282), D312 (= D322)
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
48% identity, 98% coverage: 6:343/344 of query aligns to 3:333/333 of 3asjB
- active site: Y124 (= Y129), K170 (= K177), D203 (= D213), D227 (= D237), D231 (= D241)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (≠ L89), R97 (= R102), R117 (= R122), Y124 (= Y129), D227 (= D237), D231 (= D241), V258 (= V268)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
48% identity, 98% coverage: 6:343/344 of query aligns to 3:333/333 of 3asjA
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
42% identity, 98% coverage: 6:342/344 of query aligns to 3:339/339 of 6lkyA
- active site: Y123 (= Y129), K174 (= K177), D207 (= D213), D231 (= D237)
- binding nicotinamide-adenine-dinucleotide: P68 (≠ A70), L69 (≠ V71), T71 (= T73), N81 (≠ I88), H263 (= H269), G264 (= G270), S265 (= S271), A266 (= A272), D268 (= D274), I269 (= I275), N276 (= N282)
P40495 Homoisocitrate dehydrogenase, mitochondrial; HIcDH; EC 1.1.1.87 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
42% identity, 97% coverage: 7:340/344 of query aligns to 26:371/371 of P40495
- Y150 (= Y129) mutation to F: Strongly reduced enzyme activity.
- K206 (= K177) mutation to M: Strongly reduced enzyme activity.
O14104 Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.87 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
41% identity, 97% coverage: 9:340/344 of query aligns to 11:360/362 of O14104
- S81 (≠ T73) modified: Phosphoserine
- S91 (= S86) modified: Phosphoserine
3ty3A Crystal structure of homoisocitrate dehydrogenase from schizosaccharomyces pombe bound to glycyl-glycyl-glycine (see paper)
41% identity, 97% coverage: 9:340/344 of query aligns to 7:356/358 of 3ty3A
- active site: Y129 (= Y129), K192 (= K177), D228 (= D213), D252 (= D237), D256 (= D241)
- binding glycylglycylglycine: A74 (= A70), V75 (= V71), S77 (≠ T73), R93 (= R92), E281 (= E266), P282 (= P267), H284 (= H269)
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
41% identity, 97% coverage: 7:340/344 of query aligns to 8:338/338 of 6m3sB
- active site: Y128 (= Y129), K177 (= K177), D210 (= D213), D234 (= D237)
- binding isocitrate calcium complex: T75 (= T73), S83 (= S86), N85 (≠ I88), R89 (= R92), R99 (= R102), R121 (= R122), Y128 (= Y129), D234 (= D237), D238 (= D241)
- binding nicotinamide-adenine-dinucleotide: P72 (≠ A70), L73 (≠ V71), T75 (= T73), N85 (≠ I88), H266 (= H269), G267 (= G270), S268 (= S271), A269 (= A272), D271 (= D274), I272 (= I275), N279 (= N282)
5hn6A Crystal structure of beta-decarboxylating dehydrogenase (tk0280) from thermococcus kodakarensis complexed with mn and 3-isopropylmalate (see paper)
42% identity, 97% coverage: 6:340/344 of query aligns to 3:319/329 of 5hn6A
5hn4A Crystal structure of beta-decarboxylating dehydrogenase (tk0280) from thermococcus kodakarensis complexed with mn and homoisocitrate (see paper)
42% identity, 97% coverage: 6:340/344 of query aligns to 3:319/329 of 5hn4A
- active site: Y118 (= Y129), K163 (= K177), D194 (= D213), D218 (= D237), D222 (= D241)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: T71 (= T73), S80 (= S86), R86 (= R92), R96 (= R102), R111 (= R122), Y118 (= Y129), D218 (= D237)
2d1cA Crystal structure of tt0538 protein from thermus thermophilus hb8
41% identity, 98% coverage: 7:342/344 of query aligns to 21:356/495 of 2d1cA
- active site: Y143 (= Y129), K190 (= K177), D223 (= D213), D247 (= D237), D251 (= D241)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P86 (≠ A70), L87 (≠ V71), E88 (≠ S72), T89 (= T73), N99 (≠ I88), I221 (≠ L211), N224 (≠ A214), Q228 (≠ Y218), L260 (= L250), G261 (= G251), H279 (= H269), G280 (= G270), S281 (= S271), A282 (= A272), K284 (≠ D274), Y285 (≠ I275), I291 (≠ A281), N292 (= N282), D333 (= D322)
4y1pB Crystal structure of 3-isopropylmalate dehydrogenase (saci_0600) from sulfolobus acidocaldarius complex with 3-isopropylmalate and mg2+ (see paper)
40% identity, 96% coverage: 7:336/344 of query aligns to 4:331/336 of 4y1pB
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
39% identity, 97% coverage: 6:340/344 of query aligns to 2:344/345 of 2ztwA
- active site: Y139 (= Y129), K185 (= K177), D217 (= D213), D241 (= D237), D245 (= D241)
- binding magnesium ion: G203 (≠ K196), Y206 (= Y199), V209 (≠ I205)
- binding nicotinamide-adenine-dinucleotide: I11 (= I15), H273 (= H269), G274 (= G270), A276 (= A272), D278 (= D274), I279 (= I275), A285 (= A281), N286 (= N282)
Q5SIY4 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 2 papers)
39% identity, 97% coverage: 6:340/344 of query aligns to 2:344/345 of Q5SIY4
- 74:87 (vs. 73:85, 36% identical) binding NAD(+)
- Y139 (= Y129) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 270:282, 92% identical) binding NAD(+)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
39% identity, 97% coverage: 6:340/344 of query aligns to 3:345/346 of 2y41A
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
40% identity, 97% coverage: 6:337/344 of query aligns to 3:342/355 of 2y42D
- active site: Y140 (= Y129), K186 (= K177), D218 (= D213), D242 (= D237), D246 (= D241)
- binding manganese (ii) ion: D242 (= D237), D246 (= D241)
- binding nicotinamide-adenine-dinucleotide: I12 (= I15), D79 (= D77), H274 (= H269), G275 (= G270), A277 (= A272), D279 (= D274), I280 (= I275), N287 (= N282)
2iv0A Thermal stability of isocitrate dehydrogenase from archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers (see paper)
34% identity, 99% coverage: 5:343/344 of query aligns to 28:412/412 of 2iv0A
3flkA Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex with nadh, oxalate and metal ion (see paper)
36% identity, 98% coverage: 6:343/344 of query aligns to 3:359/359 of 3flkA
- active site: Y137 (= Y129), K188 (= K177), D221 (= D213), D245 (= D237), D249 (= D241)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I15), A73 (= A70), V74 (= V71), G75 (≠ S72), D82 (≠ T79), L90 (≠ I88), N190 (= N179), I222 (≠ A214), R226 (≠ Y218), I258 (≠ L250), H280 (= H269), G281 (= G270), S282 (= S271), A283 (= A272), I286 (= I275), N293 (= N282)
- binding oxalate ion: R94 (= R92), R104 (= R102), R130 (= R122), D245 (= D237)
8grdA Crystal structure of a constitutively active mutant of the alpha beta heterodimer of human idh3 in complex with adp and mg (see paper)
38% identity, 98% coverage: 4:341/344 of query aligns to 1:324/325 of 8grdA
Query Sequence
>WP_157196862.1 NCBI__GCF_000017185.1:WP_157196862.1
MLKIPKICVIEGDGIGKEVIPETVRILKEIGDFEFIYEHAGYECFKRCGDAIPEKTLKTA
KECDAILFGAVSTPKLDETERKPYKSPILTLRKELDLYANVRPIHKLDNSDSSNNIDFII
IRENTEGLYSGVEYYDEEKELAISERHISKKGSKRIIKFAFEYAVKHHRKKVSCIHKSNI
LRITDGLFLNIFNEFKEKYKNEYNIEGNDYLVDATAMYILKSPQMFDVIVTTNLFGDILS
DEASGLLGGLGLAPSANIGDNYGLFEPVHGSAPDIAGKGVANPIAAVLSASMMLYYLDMK
EKSRLLKDAVKQVLAHKDITPDLGGNLKTKEVSDKIIEELRKIS
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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