SitesBLAST
Comparing Ac3H11_1088 FitnessBrowser__acidovorax_3H11:Ac3H11_1088 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)
41% identity, 84% coverage: 24:295/322 of query aligns to 14:284/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G30), L21 (= L31), G22 (= G32), I23 (= I33), M24 (= M34), N43 (≠ V51), R44 (≠ H52), T45 (= T53), K48 (≠ R56), V77 (≠ L86), S78 (≠ P87), D82 (= D91), Q85 (≠ K94), V133 (= V144), F244 (= F255), K245 (≠ R256), H248 (≠ L259), K251 (= K262)
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)
41% identity, 84% coverage: 24:295/322 of query aligns to 14:281/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G30), L21 (= L31), G22 (= G32), I23 (= I33), M24 (= M34), N43 (≠ V51), R44 (≠ H52), T45 (= T53), K48 (≠ R56), M76 (= M85), V77 (≠ L86), S78 (≠ P87), D82 (= D91), Q85 (≠ K94), V133 (= V144), F241 (= F255), K242 (≠ R256), H245 (≠ L259), K248 (= K262)
- binding sulfate ion: T134 (≠ S145), G135 (= G146), K183 (= K194)
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
31% identity, 92% coverage: 20:314/322 of query aligns to 37:335/335 of P29266
- D68 (vs. gap) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K194) mutation K->A,H,N,R: Complete loss of activity.
- N212 (≠ Q198) mutation to Q: Decrease in activity.
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
31% identity, 89% coverage: 25:310/322 of query aligns to 5:291/294 of 5je8B
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
31% identity, 92% coverage: 20:314/322 of query aligns to 38:336/336 of P31937
- 40:68 (vs. 22:52, 48% identical) binding
- LP 103:104 (= LP 86:87) binding
- N108 (≠ D91) binding
- T134 (≠ S119) binding
- K284 (= K262) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
31% identity, 89% coverage: 24:310/322 of query aligns to 1:293/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G32), N10 (≠ I33), M11 (= M34), Y29 (≠ H52), D30 (≠ T53), V31 (≠ R54), M63 (= M85), L64 (= L86), P65 (= P87), T95 (≠ S119), V120 (= V144), G122 (= G146), F238 (= F255), K245 (= K262)
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
31% identity, 89% coverage: 25:310/322 of query aligns to 3:287/287 of 3pefA
- binding glycerol: D67 (= D88), G123 (= G146), K171 (= K194), N175 (≠ Q198), M178 (≠ V201), L203 (≠ R226), G207 (≠ L230), N213 (≠ S236), A217 (≠ E240), F232 (= F255), H236 (≠ L259), K239 (= K262), R242 (≠ N265), R269 (≠ V292)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G32), I11 (= I33), M12 (= M34), N31 (≠ T53), R32 (= R54), S33 (≠ G55), K36 (≠ V57), M64 (= M85), L65 (= L86), A66 (≠ P87), A70 (≠ D91), E73 (≠ K94), T96 (≠ S119), V121 (= V144), G123 (= G146), S124 (≠ G147), A231 (≠ G254), F232 (= F255), H236 (≠ L259), K239 (= K262)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
33% identity, 91% coverage: 25:316/322 of query aligns to 2:287/288 of 1wp4A
- active site: S116 (= S145), K164 (= K194), N167 (= N197), N168 (≠ Q198)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G30), L8 (= L31), G9 (= G32), A10 (≠ I33), M11 (= M34), N29 (≠ H52), R30 (≠ T53), T31 (≠ R54), K34 (≠ V57), C61 (≠ M85), L62 (= L86), P63 (= P87), E67 (≠ D91), S90 (= S119), V115 (= V144), T225 (≠ G254), F226 (= F255), K233 (= K262)
- binding sulfate ion: S116 (= S145), G117 (= G146), G118 (= G147), K164 (= K194)
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
33% identity, 91% coverage: 25:316/322 of query aligns to 3:288/289 of 2cvzC
- active site: S117 (= S145), K165 (= K194), N168 (= N197), N169 (≠ Q198)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G30), L9 (= L31), G10 (= G32), A11 (≠ I33), M12 (= M34), N30 (≠ H52), R31 (≠ T53), T32 (≠ R54), C62 (≠ M85), L63 (= L86), P64 (= P87), E68 (≠ D91), E71 (≠ K94), S91 (= S119), V116 (= V144), F227 (= F255), K234 (= K262)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
32% identity, 88% coverage: 27:309/322 of query aligns to 5:286/287 of 3pduA
- binding glycerol: R242 (≠ N265), E246 (≠ S269), E246 (≠ S269), R250 (≠ A273)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G30), G10 (= G32), I11 (= I33), M12 (= M34), N31 (≠ T53), R32 (= R54), N33 (vs. gap), M64 (= M85), L65 (= L86), A66 (≠ P87), A70 (≠ D91), T96 (≠ S119), V121 (= V144), G123 (= G146), T124 (≠ G147), K171 (= K194), S231 (≠ G254), F232 (= F255), P233 (≠ R256), H236 (≠ L259), K239 (= K262)
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
32% identity, 87% coverage: 26:306/322 of query aligns to 3:283/294 of 6smyA
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: 26:306/322 of query aligns to 4:284/298 of P0A9V8
- QM 11:12 (≠ IM 33:34) binding
- D31 (vs. gap) binding
- L65 (= L86) binding
- T96 (≠ S119) binding
- G122 (≠ S145) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G146) 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 (≠ G147) 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 (≠ NQII- 197:200) binding
- K240 (= K262) binding
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
32% identity, 87% coverage: 26:306/322 of query aligns to 3:283/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G32), Q10 (≠ I33), M11 (= M34), F29 (≠ H52), D30 (vs. gap), V31 (≠ T53), M63 (= M85), L64 (= L86), V73 (= V95), S94 (= S118), T95 (≠ S119), R122 (≠ G146)
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)
28% identity, 91% coverage: 16:308/322 of query aligns to 260:551/553 of Q49A26
- 271:285 (vs. 27:41, 47% identical) binding
- T362 (≠ S119) binding
- M437 (≠ K194) mutation to K: Loss of tetramerization and protein stability.; mutation to N: No effect on tetramerization or protein stability.
- P496 (= P253) to L: decreased interaction with GATA4; decreased synergistic activation of GATA4 target genes transcription; detrimental effect on cardiomyocyte differentiation
- K505 (= K262) 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.
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)
29% identity, 90% coverage: 16:304/322 of query aligns to 308:596/602 of Q8T079
Sites not aligning to the query:
- 8 modified: Phosphoserine
- 10 modified: Phosphoserine
- 224 modified: Phosphoserine
- 228 modified: Phosphoserine
- 243 modified: Phosphoserine
2uyyA Structure of the cytokine-like nuclear factor n-pac
28% identity, 90% coverage: 18:307/322 of query aligns to 1:289/292 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 (= G32), L16 (≠ I33), M17 (= M34), N36 (≠ T53), R37 (= R54), T38 (vs. gap), V70 (≠ L86), S71 (≠ P87), A75 (≠ D91), T101 (≠ S119), F237 (= F255), Y238 (≠ R256), Y241 (≠ L259), K244 (= K262)
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, 91% coverage: 16:308/322 of query aligns to 259:544/546 of Q922P9
- P489 (= P253) 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.
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
32% identity, 90% coverage: 25:313/322 of query aligns to 2:292/292 of 5y8iA
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
32% identity, 89% coverage: 25:312/322 of query aligns to 2:291/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (= R171), E148 (= E175), A151 (≠ G178), K153 (≠ N180)
- binding nicotinamide-adenine-dinucleotide: G7 (= G30), G9 (= G32), N10 (≠ I33), M11 (= M34), F29 (≠ Y50), D30 (≠ V51), P31 (≠ H52), M63 (= M85), L64 (= L86), G120 (= G147), L239 (= L259), K242 (= K262)
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
32% identity, 89% coverage: 25:309/322 of query aligns to 3:289/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (= T155), E149 (= E175), A152 (≠ G178), G153 (≠ K179), G153 (≠ K179), K154 (≠ N180)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S145), G120 (= G146), W211 (≠ L239), F236 (= F255)
- binding nicotinamide-adenine-dinucleotide: G8 (= G30), G10 (= G32), N11 (≠ I33), M12 (= M34), F30 (≠ Y50), D31 (≠ V51), P32 (≠ H52), M64 (= M85), L65 (= L86), T93 (≠ S119), G121 (= G147), K168 (= K194), L240 (= L259), K243 (= K262)
Query Sequence
>Ac3H11_1088 FitnessBrowser__acidovorax_3H11:Ac3H11_1088
MSQDPRIDESPPHKENKNMTDTPLKLGFIGLGIMGAPMCGHLIAAGHQLYVHTRGRVAPQ
IAQSSATQCTTARGVAERADIVFLMLPDTPDVEKVLFGADGVAQGLKGSVGKVVVDMSSI
SPVATKDFAARIEAVGAQYLDAPVSGGELGAKNATLSIMVGGPEAVFERIRPLFERLGKN
ITLVGGNGDGQTAKVANQIIVALNIEAVAEALLFAARAGADPARVRQALLGGFASSKILE
VHAERMIKRTFDPGFRIGLHQKDLNLALSSARALGVPLPNTAMAQELFNACVAHGGQGWD
HSAMVRALEKMANFEMGQAAAA
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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