SitesBLAST
Comparing WP_011970417.1 NCBI__GCF_000017145.1:WP_011970417.1 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)
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
42% identity, 96% coverage: 1:272/283 of query aligns to 14:286/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G7), L21 (= L8), G22 (= G9), I23 (≠ V10), M24 (= M11), N43 (vs. gap), R44 (= R30), T45 (≠ V31), K48 (≠ R34), V77 (≠ L63), S78 (≠ P64), D82 (= D68), Q85 (≠ H71), V133 (= V119), F244 (= F230), K245 (≠ R231), H248 (≠ L234), K251 (= K237)
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)
42% identity, 96% coverage: 1:272/283 of query aligns to 14:283/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G7), L21 (= L8), G22 (= G9), I23 (≠ V10), M24 (= M11), N43 (vs. gap), R44 (= R30), T45 (≠ V31), K48 (≠ R34), M76 (= M62), V77 (≠ L63), S78 (≠ P64), D82 (= D68), Q85 (≠ H71), V133 (= V119), F241 (= F230), K242 (≠ R231), H245 (≠ L234), K248 (= K237)
- binding sulfate ion: T134 (≠ S120), G135 (= G121), K183 (= K169)
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
35% identity, 99% coverage: 3:283/283 of query aligns to 41:329/335 of P29266
- D68 (≠ R30) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K169) mutation K->A,H,N,R: Complete loss of activity.
- N212 (≠ Q173) mutation to Q: Decrease in activity.
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
33% identity, 100% coverage: 1:283/283 of query aligns to 1:291/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), N10 (≠ V10), M11 (= M11), Y29 (= Y29), D30 (≠ R30), V31 (= V31), M63 (= M62), L64 (= L63), P65 (= P64), T95 (≠ S94), V120 (= V119), G122 (= G121), F238 (= F230), K245 (= K237)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
33% identity, 99% coverage: 3:283/283 of query aligns to 42:330/336 of P31937
- LP 103:104 (= LP 63:64) binding NAD(+)
- N108 (≠ D68) binding NAD(+)
- T134 (≠ S94) binding NAD(+)
- K284 (= K237) binding NAD(+)
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
- 40:68 binding NAD(+)
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
38% identity, 99% coverage: 3:281/283 of query aligns to 3:283/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), Q10 (≠ V10), M11 (= M11), F29 (≠ Y29), D30 (≠ R30), V31 (= V31), M63 (= M62), L64 (= L63), V73 (= V72), S94 (= S93), T95 (≠ S94), R122 (≠ G121)
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)
38% identity, 99% coverage: 3:281/283 of query aligns to 4:284/298 of P0A9V8
- QM 11:12 (≠ VM 10:11) binding NAD(+)
- D31 (≠ R30) binding NAD(+)
- L65 (= L63) binding NAD(+)
- T96 (≠ S94) binding NAD(+)
- G122 (≠ S120) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G121) binding 2,3-dihydroxypropane-1-sulfonate; mutation to G: 130-fold decrease in catalytic efficiency with SLA as substrate. 3-fold decrease in catalytic efficiency with NADH as substrate.
- T124 (≠ G122) 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 (≠ ANQIV 171:175) binding 2,3-dihydroxypropane-1-sulfonate
- K240 (= K237) binding NAD(+)
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
38% identity, 99% coverage: 3:281/283 of query aligns to 3:283/294 of 6smyA
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
33% identity, 100% coverage: 2:283/283 of query aligns to 5:289/294 of 5je8B
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
33% identity, 99% coverage: 2:281/283 of query aligns to 3:283/287 of 3pefA
- binding glycerol: D67 (= D65), G123 (= G121), K171 (= K169), N175 (≠ Q173), M178 (≠ V176), L203 (≠ R201), G207 (≠ M205), N213 (≠ S211), A217 (≠ E215), F232 (= F230), H236 (≠ L234), K239 (= K237), R242 (≠ S240), R269 (≠ L267)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G9), I11 (≠ V10), M12 (= M11), N31 (≠ R30), R32 (≠ V31), S33 (≠ K32), K36 (≠ S35), M64 (= M62), L65 (= L63), A66 (≠ P64), A70 (≠ D68), E73 (≠ H71), T96 (≠ S94), V121 (= V119), G123 (= G121), S124 (≠ G122), A231 (≠ G229), F232 (= F230), H236 (≠ L234), K239 (= K237)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
32% identity, 99% coverage: 4:283/283 of query aligns to 5:285/287 of 3pduA
- binding glycerol: R242 (≠ S240), E246 (≠ D244), E246 (≠ D244), R250 (≠ L248)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G7), G10 (= G9), I11 (≠ V10), M12 (= M11), N31 (≠ R30), R32 (≠ V31), N33 (≠ K32), M64 (= M62), L65 (= L63), A66 (≠ P64), A70 (≠ D68), T96 (≠ S94), V121 (= V119), G123 (= G121), T124 (≠ G122), K171 (= K169), S231 (≠ G229), F232 (= F230), P233 (≠ R231), H236 (≠ L234), K239 (= K237)
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)
37% identity, 98% coverage: 2:277/283 of query aligns to 3:286/298 of Q9I5I6
- P66 (= P64) binding NAD(+)
- T96 (≠ S94) binding NAD(+); mutation to A: Almost abolished activity.
- S122 (= S120) mutation to A: Strongly reduced activity.
- K171 (= K169) active site
- N175 (≠ Q173) mutation to A: Strongly reduced activity.
- W214 (≠ R212) mutation to A: Almost abolished activity.
- Y219 (≠ H217) mutation to A: Strongly reduced activity.
- K246 (= K237) binding NAD(+); mutation to A: Almost abolished activity.
- D247 (= D238) mutation to A: Almost abolished activity.
Sites not aligning to the query:
8z9gA Crystal structure of glyoxylate reductase from acetobacter aceti in complex with NADPH
31% identity, 100% coverage: 2:283/283 of query aligns to 9:286/291 of 8z9gA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: F15 (≠ L8), G16 (= G9), A17 (≠ V10), M18 (= M11), T37 (≠ R30), P38 (≠ V31), S39 (≠ K32), C66 (≠ M62), V67 (≠ L63), P68 (= P64), A72 (≠ D68), S76 (≠ V72), S98 (= S94), S126 (≠ G122), K173 (= K169), Q233 (≠ G229), F234 (= F230), K241 (= K237)
8z9fA Crystal structure of glyoxylate reductase from acetobacter aceti in complex with nadh
31% identity, 100% coverage: 2:283/283 of query aligns to 10:287/293 of 8z9fA
- binding 1,4-dihydronicotinamide adenine dinucleotide: F16 (≠ L8), G17 (= G9), A18 (≠ V10), M19 (= M11), P39 (≠ V31), C67 (≠ M62), V68 (≠ L63), P69 (= P64), A73 (≠ D68), S77 (≠ V72), S99 (= S94), G126 (= G121), S127 (≠ G122), Q234 (≠ G229), F235 (= F230)
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
37% identity, 98% coverage: 2:277/283 of query aligns to 2:284/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), H10 (≠ V10), M11 (= M11), F29 (≠ Y29), D30 (≠ R30), L31 (vs. gap), M63 (= M62), L64 (= L63), P65 (= P64), T94 (≠ S94), V119 (= V119), G121 (= G121), F237 (= F230), K244 (= K237)
3obbA Crystal structure of a possible 3-hydroxyisobutyrate dehydrogenase from pseudomonas aeruginosa pao1 (see paper)
36% identity, 98% coverage: 2:277/283 of query aligns to 3:285/295 of 3obbA
2uyyA Structure of the cytokine-like nuclear factor n-pac
26% identity, 99% coverage: 2:282/283 of query aligns to 8:289/292 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 (= G9), L16 (≠ V10), M17 (= M11), N36 (vs. gap), R37 (= R30), T38 (≠ V31), V70 (≠ L63), S71 (≠ P64), A75 (≠ D68), T101 (≠ S94), F237 (= F230), Y238 (≠ R231), Y241 (≠ L234), K244 (= K237)
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)
26% identity, 99% coverage: 2:282/283 of query aligns to 269:550/553 of Q49A26
- 271:285 (vs. 4:18, 47% identical) binding NAD(+)
- T362 (≠ S94) binding NAD(+)
- M437 (≠ K169) mutation to K: Loss of tetramerization and protein stability.; mutation to N: No effect on tetramerization or protein stability.
- P496 (= P228) to L: decreased interaction with GATA4; decreased synergistic activation of GATA4 target genes transcription; detrimental effect on cardiomyocyte differentiation
- K505 (= K237) binding NAD(+)
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.
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
35% identity, 86% coverage: 3:245/283 of query aligns to 3:250/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (≠ K146), E148 (= E150), A151 (≠ G153), K153 (≠ N155)
- binding nicotinamide-adenine-dinucleotide: G7 (= G7), G9 (= G9), N10 (≠ V10), M11 (= M11), F29 (≠ Y29), D30 (≠ R30), P31 (vs. gap), M63 (= M62), L64 (= L63), G120 (= G122), L239 (= L234), K242 (= K237)
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
35% identity, 86% coverage: 3:245/283 of query aligns to 3:250/292 of 5y8iA
Query Sequence
>WP_011970417.1 NCBI__GCF_000017145.1:WP_011970417.1
MRIGFIGLGVMGRPMAQHLIVAGHQLYLYRVKPRSAHLVESGATACTSASEVARSAEVII
LMLPDTPDVEHVLFGEDGVLEGVEPGKLIIDMSSISPLATKDFAARLDARGCEYLDAPVS
GGEVGAKAASLTIMVGGKPEVFGRAKPLFEKMGKNITLIGGVGDGQVAKVANQIVVALNI
QAVSEALRFAARAGADPAVVRQALMGGFAASRVLEVHGERMISESFEPGFRIRLHHKDLS
LALDSAQLLELMLPNTAMVHQLMNGALSKGLGDKDHSALIEAL
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