SitesBLAST
Comparing GFF1289 Psest_1322 3-hydroxyisobutyrate dehydrogenase and related beta-hydroxyacid dehydrogenases 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)
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
35% identity, 90% coverage: 7:271/295 of query aligns to 16:278/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G11), L21 (≠ I12), G22 (= G13), I23 (≠ L14), M24 (= M15), N43 (= N34), R44 (= R35), T45 (≠ S36), K48 (= K39), V77 (≠ L68), S78 (≠ A69), D82 (≠ A73), Q85 (≠ E76), V133 (= V125), F244 (≠ W237), K245 (≠ H238), H248 (≠ T241), K251 (= K244)
3ws7A The 1.18 a resolution structure of l-serine 3-dehydrogenase complexed with NADP+ and sulfate ion from the hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
35% identity, 90% coverage: 7:271/295 of query aligns to 16:275/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G11), L21 (≠ I12), G22 (= G13), I23 (≠ L14), M24 (= M15), N43 (= N34), R44 (= R35), T45 (≠ S36), K48 (= K39), M76 (≠ C67), V77 (≠ L68), S78 (≠ A69), D82 (≠ A73), Q85 (≠ E76), V133 (= V125), F241 (≠ W237), K242 (≠ H238), H245 (≠ T241), K248 (= K244)
- binding sulfate ion: T134 (≠ S126), G135 (= G127), K183 (= K175)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
39% identity, 89% coverage: 4:266/295 of query aligns to 1:259/287 of 3pduA
- binding glycerol: R242 (≠ D247), E246 (≠ K251), E246 (≠ K251), R250 (≠ E255)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), G10 (= G13), I11 (≠ L14), M12 (= M15), N31 (= N34), R32 (= R35), N33 (≠ S36), M64 (≠ C67), L65 (= L68), A66 (= A69), A70 (= A73), T96 (≠ S99), V121 (= V125), G123 (= G127), T124 (≠ G128), K171 (= K175), S231 (≠ K236), F232 (≠ W237), P233 (≠ H238), H236 (≠ T241), K239 (= K244)
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
31% identity, 98% coverage: 7:294/295 of query aligns to 3:295/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), N10 (≠ L14), M11 (= M15), Y29 (≠ W33), D30 (≠ N34), V31 (≠ R35), M63 (≠ C67), L64 (= L68), P65 (≠ A69), T95 (≠ S99), V120 (= V125), G122 (= G127), F238 (vs. gap), K245 (= K244)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
31% identity, 98% coverage: 7:294/295 of query aligns to 42:334/336 of P31937
- LP 103:104 (≠ LA 68:69) binding
- N108 (≠ A73) binding
- T134 (≠ S99) binding
- K284 (= K244) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
- 40:68 binding
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
32% identity, 96% coverage: 7:290/295 of query aligns to 4:285/287 of 3pefA
- binding glycerol: D67 (= D70), G123 (= G127), K171 (= K175), N175 (≠ Q179), M178 (≠ V182), L203 (≠ A207), G207 (≠ A211), N213 (≠ S217), A217 (≠ Q221), F232 (≠ W237), H236 (≠ T241), K239 (= K244), R242 (≠ D247), R269 (≠ G274)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G13), I11 (≠ L14), M12 (= M15), N31 (= N34), R32 (= R35), S33 (= S36), K36 (= K39), M64 (≠ C67), L65 (= L68), A66 (= A69), A70 (= A73), E73 (= E76), T96 (≠ S99), V121 (= V125), G123 (= G127), S124 (≠ G128), A231 (≠ V235), F232 (≠ W237), H236 (≠ T241), K239 (= K244)
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
30% identity, 100% coverage: 1:294/295 of query aligns to 35:333/335 of P29266
- D68 (≠ N34) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K175) mutation K->A,H,N,R: Complete loss of activity.
- N212 (≠ Q179) mutation to Q: Decrease in activity.
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
35% identity, 91% coverage: 4:272/295 of query aligns to 1:262/289 of 2cvzC
- active site: S117 (= S126), K165 (= K175), N168 (= N178), N169 (≠ Q179)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), L9 (≠ I12), G10 (= G13), A11 (≠ L14), M12 (= M15), N30 (= N34), R31 (= R35), T32 (≠ S36), C62 (= C67), L63 (= L68), P64 (≠ A69), E68 (≠ A73), E71 (= E76), S91 (= S99), V116 (= V125), F227 (≠ W237), K234 (= K244)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
35% identity, 90% coverage: 7:272/295 of query aligns to 3:261/288 of 1wp4A
- active site: S116 (= S126), K164 (= K175), N167 (= N178), N168 (≠ Q179)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G11), L8 (≠ I12), G9 (= G13), A10 (≠ L14), M11 (= M15), N29 (= N34), R30 (= R35), T31 (≠ S36), K34 (= K39), C61 (= C67), L62 (= L68), P63 (≠ A69), E67 (≠ A73), S90 (= S99), V115 (= V125), T225 (≠ K236), F226 (≠ W237), K233 (= K244)
- binding sulfate ion: S116 (= S126), G117 (= G127), G118 (= G128), K164 (= K175)
2uyyA Structure of the cytokine-like nuclear factor n-pac
29% identity, 96% coverage: 7:290/295 of query aligns to 9:290/292 of 2uyyA
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: G15 (= G13), L16 (= L14), M17 (= M15), N36 (= N34), R37 (= R35), T38 (≠ S36), V70 (≠ L68), S71 (≠ A69), A75 (= A73), T101 (≠ S99), F237 (≠ W237), Y238 (≠ H238), Y241 (≠ T241), K244 (= K244)
Q49A26 Cytokine-like nuclear factor N-PAC; NPAC; 3-hydroxyisobutyrate dehydrogenase-like protein; Glyoxylate reductase 1 homolog; Nuclear protein NP60; Nuclear protein of 60 kDa; Nucleosome-destabilizing factor; hNDF; Putative oxidoreductase GLYR1 from Homo sapiens (Human) (see 3 papers)
29% identity, 96% coverage: 7:290/295 of query aligns to 270:551/553 of Q49A26
- 271:285 (vs. 8:22, 40% identical) binding
- T362 (≠ S99) binding
- M437 (≠ K175) mutation to K: Loss of tetramerization and protein stability.; mutation to N: No effect on tetramerization or protein stability.
- P496 (= P234) to L: decreased interaction with GATA4; decreased synergistic activation of GATA4 target genes transcription; detrimental effect on cardiomyocyte differentiation
- K505 (= K244) binding
Sites not aligning to the query:
- 214 D→A: Slightly reduced stimulation of KDM1B demethylase activity, but normal KDM1B-binding.
- 214:217 Interaction with histone H3
- 216 H→A: Slightly reduced stimulation of KDM1B demethylase activity, but normal KDM1B-binding.
- 216:225 Interaction with KDM1B
- 217 Required to promote KDM1B demethylase activity toward histone H3K4me1 and H3K4me2; F→A: Abolished stimulation of KDM1B demethylase activity, reduced affinity for histone H3 of the dimer with KDM1B, but normal KDM1B-binding.
- 219 H→A: Impaired KDM1B-binding and abolished stimulation of KDM1B demethylase activity; when associated with A-223.
- 220:222 FLL→AAA: Impaired KDM1B-binding and abolished stimulation of KDM1B demethylase activity.
- 223 S→A: Impaired KDM1B-binding and abolished stimulation of KDM1B demethylase activity; when associated with A-219.
P0A9V8 3-sulfolactaldehyde reductase; SLA reductase; 4-hydroxybutyrate dehydrogenase; Gamma-hydroxybutyrate dehydrogenase; GHBDH; Succinic semialdehyde reductase; SSA reductase; EC 1.1.1.373; EC 1.1.1.61 from Escherichia coli (strain K12)
32% identity, 87% coverage: 7:262/295 of query aligns to 4:258/298 of P0A9V8
- QM 11:12 (≠ LM 14:15) binding
- D31 (≠ N34) binding
- L65 (= L68) binding
- T96 (≠ S99) binding
- G122 (≠ S126) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G127) binding ; mutation to G: 130-fold decrease in catalytic efficiency with SLA as substrate. 3-fold decrease in catalytic efficiency with NADH as substrate.
- T124 (≠ G128) mutation to G: 230-fold decrease in catalytic efficiency with SLA as substrate. 12-fold decrease in catalytic efficiency with NADH as substrate.
- NNYMS 174:178 (≠ CNQMI 177:181) binding
- K240 (= K244) binding
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
32% identity, 87% coverage: 7:262/295 of query aligns to 3:257/294 of 6smyA
Sites not aligning to the query:
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
32% identity, 87% coverage: 7:262/295 of query aligns to 3:257/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), Q10 (≠ L14), M11 (= M15), F29 (≠ W33), D30 (≠ N34), V31 (≠ R35), M63 (≠ C67), L64 (= L68), V73 (= V77), S94 (= S98), T95 (≠ S99), R122 (≠ G127)
Q8T079 Cytokine-like nuclear factor N-PAC; NPAC; Glyoxylate reductase 1 homolog; Nuclear protein NP60 homolog; Nucleosome-destabilizing factor; Putative oxidoreductase GLYR1 homolog from Drosophila melanogaster (Fruit fly) (see paper)
23% identity, 96% coverage: 6:287/295 of query aligns to 317:597/602 of Q8T079
Sites not aligning to the query:
- 8 modified: Phosphoserine
- 10 modified: Phosphoserine
- 224 modified: Phosphoserine
- 228 modified: Phosphoserine
- 243 modified: Phosphoserine
Q922P9 Cytokine-like nuclear factor N-PAC; NPAC; Glyoxylate reductase 1 homolog; Nuclear protein NP60; Putative oxidoreductase GLYR1 from Mus musculus (Mouse) (see paper)
28% identity, 96% coverage: 7:290/295 of query aligns to 269:544/546 of Q922P9
- P489 (= P234) mutation to L: Mutant animals are born at expected Mendelian ratios. 54% mutants display postnatal lethality between days 0 and 1. They show centricular septal defects.
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
29% identity, 97% coverage: 4:288/295 of query aligns to 3:287/294 of 5je8B
Q9I5I6 NAD-dependent L-serine dehydrogenase; L-serine 3-dehydrogenase (NAD(+)); EC 1.1.1.387 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
33% identity, 97% coverage: 4:290/295 of query aligns to 1:292/298 of Q9I5I6
- 2:31 (vs. 5:34, 50% identical) binding
- P66 (≠ A69) binding
- T96 (≠ S99) binding ; mutation to A: Almost abolished activity.
- S122 (= S126) mutation to A: Strongly reduced activity.
- K171 (= K175) active site
- N175 (≠ Q179) mutation to A: Strongly reduced activity.
- W214 (≠ R218) mutation to A: Almost abolished activity.
- Y219 (≠ L223) mutation to A: Strongly reduced activity.
- K246 (= K244) binding ; mutation to A: Almost abolished activity.
- D247 (= D245) mutation to A: Almost abolished activity.
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
32% identity, 90% coverage: 4:269/295 of query aligns to 1:268/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (≠ S136), E149 (≠ M156), A152 (≠ G159), G153 (≠ Q160), G153 (≠ Q160), K154 (≠ R161)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S126), G120 (= G127), W211 (≠ R218), F236 (≠ W237)
- binding nicotinamide-adenine-dinucleotide: G8 (= G11), G10 (= G13), N11 (≠ L14), M12 (= M15), F30 (≠ W33), D31 (≠ N34), P32 (≠ R35), M64 (≠ C67), L65 (= L68), T93 (≠ S99), G121 (= G128), K168 (= K175), L240 (≠ T241), K243 (= K244)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
32% identity, 90% coverage: 4:269/295 of query aligns to 1:268/290 of 5y8kA
Query Sequence
>GFF1289 Psest_1322 3-hydroxyisobutyrate dehydrogenase and related beta-hydroxyacid dehydrogenases
MSDLPTLAFAGIGLMGLPMCRRLLAAGYRLVVWNRSPEKCEPLVALGARAVATPAELCAE
ADIVLLCLADTAAVREVLFGKGGIAEGGKAGKLLVDHSSLEPAATRDMAAELEFRSGMRW
VDAPVSGGTPGAEAGSLVIMAGGRVEDVERVRPVLMNLGQRLTHMGEVGAGQVTKVCNQM
IVACNALVIAEVVALAERAGVDASLLAPALAGGFADSRPLQILAPQMAASEFEPVKWHVR
TLLKDLDTAVKLSREQGSATPLSGLAAQLMRLHGSQGNLERDPATLVQMYWEDEQ
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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