SitesBLAST
Comparing GFF838 FitnessBrowser__Marino:GFF838 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)
3flkA Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex with nadh, oxalate and metal ion (see paper)
42% identity, 99% coverage: 4:384/384 of query aligns to 1:358/359 of 3flkA
- active site: Y137 (= Y147), K188 (= K218), D221 (= D251), D245 (= D275), D249 (= D279)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I15), A73 (= A76), V74 (≠ L77), G75 (= G78), D82 (= D93), L90 (= L100), N190 (= N220), I222 (≠ A252), R226 (≠ K256), I258 (≠ M288), H280 (= H311), G281 (= G312), S282 (= S313), A283 (= A314), I286 (= I317), N293 (≠ D324)
- binding oxalate ion: R94 (= R104), R104 (= R114), R130 (= R140), D245 (= D275)
2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
39% identity, 98% coverage: 5:382/384 of query aligns to 2:337/337 of 2g4oA
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
35% identity, 99% coverage: 4:383/384 of query aligns to 1:346/346 of 2y41A
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
37% identity, 87% coverage: 4:337/384 of query aligns to 1:300/355 of 2y42D
- active site: Y140 (= Y147), K186 (= K218), D218 (= D251), D242 (= D275), D246 (= D279)
- binding manganese (ii) ion: D242 (= D275), D246 (= D279)
- binding nicotinamide-adenine-dinucleotide: I12 (= I15), D79 (= D84), H274 (= H311), G275 (= G312), A277 (= A314), D279 (= D316), I280 (= I317), N287 (≠ D324)
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
35% identity, 98% coverage: 6:383/384 of query aligns to 2:345/345 of 2ztwA
- active site: Y139 (= Y147), K185 (= K218), D217 (= D251), D241 (= D275), D245 (= D279)
- binding magnesium ion: G203 (≠ S237), Y206 (= Y240), V209 (= V243)
- binding nicotinamide-adenine-dinucleotide: I11 (= I15), H273 (= H311), G274 (= G312), A276 (= A314), D278 (= D316), I279 (= I317), A285 (= A323), N286 (≠ D324)
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)
35% identity, 98% coverage: 6:383/384 of query aligns to 2:345/345 of Q5SIY4
- 74:87 (vs. 79:93, 27% identical) binding
- Y139 (= Y147) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 312:324, 77% identical) binding
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
35% identity, 99% coverage: 3:382/384 of query aligns to 2:358/358 of 6xxyA
- active site: Y144 (= Y147), K194 (= K218), D226 (= D251), D250 (= D275)
- binding magnesium ion: D250 (= D275), D254 (= D279)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A76), V75 (≠ L77), G76 (= G78), E90 (≠ D87), L94 (= L100), Y224 (≠ L249), N227 (≠ A252), M230 (= M255), M263 (= M288), G264 (= G289), E280 (= E308), G283 (≠ H311), G284 (= G312), S285 (= S313), A286 (= A314), P287 (= P315), D288 (= D316), I289 (= I317), N296 (≠ D324), D337 (= D360)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (≠ D87), R108 (= R114), R137 (= R140), K194 (= K218), V197 (≠ A221), D226 (= D251), D250 (= D275)
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
33% identity, 99% coverage: 1:382/384 of query aligns to 4:338/338 of 6m3sB
- active site: Y128 (= Y147), K177 (= K218), D210 (= D251), D234 (= D275)
- binding isocitrate calcium complex: T75 (≠ D85), S83 (= S94), N85 (≠ S96), R89 (= R104), R99 (= R114), R121 (= R140), Y128 (= Y147), D234 (= D275), D238 (= D279)
- binding nicotinamide-adenine-dinucleotide: P72 (= P82), L73 (≠ M83), T75 (≠ D85), N85 (≠ S96), H266 (= H311), G267 (= G312), S268 (= S313), A269 (= A314), D271 (= D316), I272 (= I317), N279 (≠ D324)
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
34% identity, 98% coverage: 6:382/384 of query aligns to 3:337/339 of 6lkyA
- active site: Y123 (= Y147), K174 (= K218), D207 (= D251), D231 (= D275)
- binding nicotinamide-adenine-dinucleotide: P68 (= P82), L69 (≠ M83), T71 (≠ D85), N81 (≠ S96), H263 (= H311), G264 (= G312), S265 (= S313), A266 (= A314), D268 (= D316), I269 (= I317), N276 (≠ D324)
4yb4A Crystal structure of homoisocitrate dehydrogenase from thermus thermophilus in complex with homoisocitrate, magnesium ion (ii) and nadh
36% identity, 89% coverage: 6:345/384 of query aligns to 3:293/333 of 4yb4A
- active site: Y124 (= Y147), K170 (= K218), D203 (= D251), D227 (= D275), D231 (= D279)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ D79), R84 (≠ L101), R87 (= R104), R97 (= R114), R117 (= R140), Y124 (= Y147), D227 (= D275)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I15), A69 (≠ L77), T70 (≠ G78), S71 (≠ D79), I201 (≠ L249), N204 (≠ A252), L240 (≠ M288), E256 (= E308), H259 (= H311), G260 (= G312), S261 (= S313), A262 (= A314), D264 (= D316), I265 (= I317), N272 (≠ D324)
Sites not aligning to the query:
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
36% identity, 89% coverage: 6:345/384 of query aligns to 3:293/333 of 3asjB
- active site: Y124 (= Y147), K170 (= K218), D203 (= D251), D227 (= D275), D231 (= D279)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (≠ L101), R97 (= R114), R117 (= R140), Y124 (= Y147), D227 (= D275), D231 (= D279), V258 (≠ T310)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
36% identity, 89% coverage: 6:345/384 of query aligns to 3:293/333 of 3asjA
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)
36% identity, 89% coverage: 6:345/384 of query aligns to 4:294/334 of Q72IW9
- E57 (≠ A64) 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 (≠ LGD 77:79) binding
- S72 (≠ D79) 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 (≠ L101) 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 (≠ D102) 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 (= R104) binding in other chain
- R98 (= R114) binding in other chain
- R118 (= R140) binding in other chain
- Y125 (= Y147) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (= V162) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K218) binding
- N173 (= N220) binding ; binding
- D204 (= D251) binding
- M208 (= M255) 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 (= F264) 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 (= D275) binding
- D232 (= D279) binding
- V238 (≠ S285) 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 312:316) binding
- N273 (≠ D324) binding
Sites not aligning to the query:
- 310 R→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.
P93832 3-isopropylmalate dehydrogenase 2, chloroplastic; 3-IPM-DH 2; AtIMDH2; AtIMDH3; IMDH 2; Beta-IPM dehydrogenase 2; Isopropylmalate dehydrogenase 2; AtIMD2; EC 1.1.1.85 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
33% identity, 95% coverage: 7:370/384 of query aligns to 45:374/405 of P93832
- 114:129 (vs. 77:93, 24% identical) binding
- L132 (= L100) mutation to A: Reduced activity toward 3-isopropylmalate.
- L133 (= L101) Confers substrate specificity; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
- R136 (= R104) binding ; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R146 (= R114) binding ; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- R174 (= R140) binding ; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
- Y181 (= Y147) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
- K232 (= K218) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
- N234 (= N220) binding ; mutation N->A,D: Loss of activity toward 3-isopropylmalate.
- V235 (≠ A221) mutation to A: Reduced activity toward 3-isopropylmalate.
- D264 (= D251) binding ; binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- N265 (≠ A252) binding
- D288 (= D275) binding ; mutation to N: Loss of activity toward 3-isopropylmalate.
- D292 (= D279) binding ; mutation to N: Reduced activity toward 3-isopropylmalate.
- 318:334 (vs. 308:324, 76% identical) binding
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
34% identity, 90% coverage: 4:348/384 of query aligns to 2:319/364 of 3vkzA
5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
33% identity, 95% coverage: 7:370/384 of query aligns to 15:344/369 of 5j32A
5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
33% identity, 95% coverage: 7:370/384 of query aligns to 5:334/360 of 5j33A
- active site: Y141 (= Y147), K192 (= K218), D224 (= D251), D248 (= D275), D252 (= D279)
- binding magnesium ion: D248 (= D275), D252 (= D279)
- binding nicotinamide-adenine-dinucleotide: I74 (≠ L77), E89 (≠ D93), L92 (= L100), I261 (≠ M288), E278 (= E308), H281 (= H311), G282 (= G312), S283 (= S313), A284 (= A314), I287 (= I317), N294 (≠ D324)
Sites not aligning to the query:
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
32% identity, 100% coverage: 1:383/384 of query aligns to 1:360/363 of 1cnzA
P37412 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
32% identity, 100% coverage: 1:383/384 of query aligns to 1:360/363 of P37412
- D227 (= D251) binding
- D251 (= D275) binding
- D255 (= D279) binding
Q9SA14 3-isopropylmalate dehydrogenase 3, chloroplastic; 3-IPM-DH 3; AtIMDH2; AtIMDH3; IMDH 3; Beta-IPM dehydrogenase 3; Isopropylmalate dehydrogenase 3; AtIMD3; EC 1.1.1.85 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 95% coverage: 6:370/384 of query aligns to 45:375/404 of Q9SA14
- L134 (= L101) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
Query Sequence
>GFF838 FitnessBrowser__Marino:GFF838
MAQTTRIAVTPGDGIGPEVVAEAVRCLETLRAKHGLDLEWTRFPWPSHAWHEEHGESMPA
DALAQLQKYDAILLGALGDPGPMDDPDRYLLPDSISLAPLLDMRKGFDQWVCERPARLLP
GARQYLADERAKDIDMLVIRENSEGEYVSQGGRLRKGTPDEVATQMEVFTRKATDRIIRY
GFEQARNRAADRVSEGRTRTFRTLDGRTCESQVCLVTKRNALRYWGDMYTEAFDEISKEY
PDVATHHELVDAACMKFVQSPWAFDVVVASNLQGDILTDLAAVLSGGMGVAPSCNLNPTD
PDMPSMFEPTHGSAPDIAGQGLADPTAMLFTAARMLEWLGRKDPAIAAAGKELFDAVAAD
LAENSGSRRGTHEIGSAICERLSR
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