SitesBLAST
Comparing WP_011385541.1 NCBI__GCF_000009985.1:WP_011385541.1 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)
3flkA Crystal structure of tartrate dehydrogenase from pseudomonas putida in complex with nadh, oxalate and metal ion (see paper)
50% identity, 97% coverage: 4:349/358 of query aligns to 2:352/359 of 3flkA
- active site: Y137 (= Y138), K188 (= K189), D221 (= D222), D245 (= D246), D249 (= D250)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I14), A73 (= A75), V74 (= V76), G75 (= G77), D82 (= D83), L90 (≠ R91), N190 (= N191), I222 (≠ A223), R226 (= R227), I258 (≠ L259), H280 (= H281), G281 (= G282), S282 (= S283), A283 (= A284), I286 (= I287), N293 (= N294)
- binding oxalate ion: R94 (≠ C95), R104 (= R105), R130 (= R131), D245 (= D246)
2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
42% identity, 89% coverage: 5:323/358 of query aligns to 3:313/337 of 2g4oA
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)
39% identity, 98% coverage: 4:355/358 of query aligns to 3:333/334 of Q72IW9
- E57 (= E63) 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 (≠ VGA 76:78) binding
- S72 (≠ A78) 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 (≠ L92) 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 (≠ N93) 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 (≠ C95) binding in other chain
- R98 (= R105) binding in other chain
- R118 (= R131) binding in other chain
- Y125 (= Y138) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
- V135 (= V153) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
- K171 (= K189) binding
- N173 (= N191) binding ; binding
- D204 (= D222) binding
- M208 (= M226) 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 (≠ L235) 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 (= D246) binding
- D232 (= D250) binding
- V238 (≠ A256) 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 (≠ GSAFD 282:286) binding
- N273 (= N294) binding
- R310 (≠ H332) 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
39% identity, 98% coverage: 4:355/358 of query aligns to 2:332/333 of 4yb4A
- active site: Y124 (= Y138), K170 (= K189), D203 (= D222), D227 (= D246), D231 (= D250)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: S71 (≠ A78), R84 (≠ L92), R87 (≠ C95), R97 (= R105), R117 (= R131), Y124 (= Y138), D227 (= D246)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I12 (= I14), A69 (≠ V76), T70 (≠ G77), S71 (≠ A78), I201 (≠ L220), N204 (≠ A223), L240 (= L259), E256 (= E278), H259 (= H281), G260 (= G282), S261 (= S283), A262 (= A284), D264 (= D286), I265 (= I287), N272 (= N294), D312 (= D335)
3asjB Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
39% identity, 98% coverage: 4:355/358 of query aligns to 2:332/333 of 3asjB
- active site: Y124 (= Y138), K170 (= K189), D203 (= D222), D227 (= D246), D231 (= D250)
- binding (2Z)-3-[(carboxymethyl)sulfanyl]-2-hydroxyprop-2-enoic acid: R84 (≠ L92), R97 (= R105), R117 (= R131), Y124 (= Y138), D227 (= D246), D231 (= D250), V258 (≠ I280)
3asjA Crystal structure of homoisocitrate dehydrogenase in complex with a designed inhibitor (see paper)
39% identity, 98% coverage: 4:355/358 of query aligns to 2:332/333 of 3asjA
2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
38% identity, 97% coverage: 4:350/358 of query aligns to 2:342/355 of 2y42D
- active site: Y140 (= Y138), K186 (= K189), D218 (= D222), D242 (= D246), D246 (= D250)
- binding manganese (ii) ion: D242 (= D246), D246 (= D250)
- binding nicotinamide-adenine-dinucleotide: I12 (= I14), D79 (vs. gap), H274 (= H281), G275 (= G282), A277 (= A284), D279 (= D286), I280 (= I287), N287 (= N294)
2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
38% identity, 97% coverage: 4:350/358 of query aligns to 2:342/346 of 2y41A
2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
38% identity, 97% coverage: 4:350/358 of query aligns to 1:341/345 of 2ztwA
- active site: Y139 (= Y138), K185 (= K189), D217 (= D222), D241 (= D246), D245 (= D250)
- binding magnesium ion: G203 (≠ A208), Y206 (≠ F211), V209 (= V214)
- binding nicotinamide-adenine-dinucleotide: I11 (= I14), H273 (= H281), G274 (= G282), A276 (= A284), D278 (= D286), I279 (= I287), A285 (= A293), N286 (= N294)
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)
38% identity, 97% coverage: 4:350/358 of query aligns to 1:341/345 of Q5SIY4
- 74:87 (vs. 78:88, 14% identical) binding
- Y139 (= Y138) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
- 274:286 (vs. 282:294, 85% identical) binding
6m3sB Dimeric isocitrate dehydrogenase from xanthomonas campestris pv. Campestris 8004
38% identity, 94% coverage: 6:342/358 of query aligns to 8:327/338 of 6m3sB
- active site: Y128 (= Y138), K177 (= K189), D210 (= D222), D234 (= D246)
- binding isocitrate calcium complex: T75 (≠ V81), S83 (≠ G89), N85 (≠ R91), R89 (≠ C95), R99 (= R105), R121 (= R131), Y128 (= Y138), D234 (= D246), D238 (= D250)
- binding nicotinamide-adenine-dinucleotide: P72 (= P79), L73 (vs. gap), T75 (≠ V81), N85 (≠ R91), H266 (= H281), G267 (= G282), S268 (= S283), A269 (= A284), D271 (= D286), I272 (= I287), N279 (= N294)
6lkyA Crystal structure of isocitrate dehydrogenase from methylococcus capsulatus
36% identity, 93% coverage: 5:336/358 of query aligns to 3:318/339 of 6lkyA
- active site: Y123 (= Y138), K174 (= K189), D207 (= D222), D231 (= D246)
- binding nicotinamide-adenine-dinucleotide: P68 (≠ A75), L69 (≠ V76), T71 (≠ A78), N81 (≠ R91), H263 (= H281), G264 (= G282), S265 (= S283), A266 (= A284), D268 (= D286), I269 (= I287), N276 (= N294)
3ty3A Crystal structure of homoisocitrate dehydrogenase from schizosaccharomyces pombe bound to glycyl-glycyl-glycine (see paper)
35% identity, 98% coverage: 2:353/358 of query aligns to 1:356/358 of 3ty3A
- active site: Y129 (= Y138), K192 (= K189), D228 (= D222), D252 (= D246), D256 (= D250)
- binding glycylglycylglycine: A74 (= A75), V75 (= V76), S77 (≠ A78), R93 (= R91), E281 (= E278), P282 (= P279), H284 (= H281)
O14104 Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.87 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 98% coverage: 2:353/358 of query aligns to 5:360/362 of O14104
- S81 (≠ A78) modified: Phosphoserine
- S91 (≠ T86) modified: Phosphoserine
P40495 Homoisocitrate dehydrogenase, mitochondrial; HIcDH; EC 1.1.1.87 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
36% identity, 98% coverage: 2:351/358 of query aligns to 22:369/371 of P40495
- Y150 (= Y138) mutation to F: Strongly reduced enzyme activity.
- K206 (= K189) mutation to M: Strongly reduced enzyme activity.
5hn6A Crystal structure of beta-decarboxylating dehydrogenase (tk0280) from thermococcus kodakarensis complexed with mn and 3-isopropylmalate (see paper)
37% identity, 98% coverage: 4:354/358 of query aligns to 2:320/329 of 5hn6A
5hn4A Crystal structure of beta-decarboxylating dehydrogenase (tk0280) from thermococcus kodakarensis complexed with mn and homoisocitrate (see paper)
37% identity, 98% coverage: 4:354/358 of query aligns to 2:320/329 of 5hn4A
- active site: Y118 (= Y138), K163 (= K189), D194 (= D222), D218 (= D246), D222 (= D250)
- binding (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylic acid: T71 (≠ A78), S80 (≠ T86), R86 (≠ C95), R96 (= R105), R111 (= R131), Y118 (= Y138), D218 (= D246)
6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
35% identity, 92% coverage: 1:328/358 of query aligns to 1:331/358 of 6xxyA
- active site: Y144 (= Y138), K194 (= K189), D226 (= D222), D250 (= D246)
- binding magnesium ion: D250 (= D246), D254 (= D250)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A75), V75 (= V76), G76 (= G77), E90 (≠ L87), L94 (≠ R91), Y224 (≠ L220), N227 (≠ A223), M230 (= M226), M263 (≠ L259), G264 (= G260), E280 (= E278), G283 (≠ H281), G284 (= G282), S285 (= S283), A286 (= A284), P287 (≠ F285), D288 (= D286), I289 (= I287), N296 (= N294)
- binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (≠ L87), R108 (= R105), R137 (= R131), K194 (= K189), V197 (≠ A192), D226 (= D222), D250 (= D246)
Sites not aligning to the query:
3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
35% identity, 98% coverage: 4:353/358 of query aligns to 3:364/364 of 3vkzA
1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
35% identity, 90% coverage: 2:324/358 of query aligns to 3:328/363 of 1cnzA
Query Sequence
>WP_011385541.1 NCBI__GCF_000009985.1:WP_011385541.1
MREFKIAAIPADGIGKEVVAAGLEVLDVLAKRDGGFRLNIETFDWGSDYYKKHGTMMPEN
GRETLKQFDAIYFGAVGAPDVPDHVTLWGLRLNICQPFDQYANVRPTRILPGIKSPLAGV
GPRLLNWVIVRENSEGEYAGQGGRSHRGFPEEVATEVAIFTRAGVTRIMRFAFKLAQSRP
RKLLTVVTKSNAQRHGMVMWDEIAAEVAGEFPDVTWDKMLVDAMTMRMTLKPETLDTIVA
TNLHADILSDLAAALAGSLGIAPTANLNPERKFPSMFEPIHGSAFDITGKGIANPIGTFW
TACMMLDHLGETAASARLMRAIERVTANPLLHTPDLGGKATTRIVTDAVIAAIEADNE
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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