SitesBLAST
Comparing RR42_RS16835 FitnessBrowser__Cup4G11:RR42_RS16835 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
39% identity, 95% coverage: 2:276/289 of query aligns to 12:286/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G10), L21 (= L11), G22 (= G12), I23 (≠ A13), M24 (= M14), N43 (≠ V33), R44 (= R34), T45 (≠ R35), K48 (≠ A38), V77 (= V67), S78 (≠ T68), D82 (= D72), Q85 (≠ A75), V133 (= V123), F244 (≠ I234), K245 (≠ E235), H248 (≠ L238), K251 (= K241)
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)
39% identity, 95% coverage: 2:276/289 of query aligns to 12:283/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G10), L21 (= L11), G22 (= G12), I23 (≠ A13), M24 (= M14), N43 (≠ V33), R44 (= R34), T45 (≠ R35), K48 (≠ A38), M76 (≠ N66), V77 (= V67), S78 (≠ T68), D82 (= D72), Q85 (≠ A75), V133 (= V123), F241 (≠ I234), K242 (≠ E235), H245 (≠ L238), K248 (= K241)
- binding sulfate ion: T134 (≠ S124), G135 (= G125), K183 (= K173)
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
29% identity, 97% coverage: 6:285/289 of query aligns to 6:287/294 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)
37% identity, 98% coverage: 6:288/289 of query aligns to 4:293/298 of Q9I5I6
- P66 (≠ T68) binding
- T96 (= T98) binding ; mutation to A: Almost abolished activity.
- S122 (= S124) mutation to A: Strongly reduced activity.
- K171 (= K173) active site
- N175 (≠ Q177) mutation to A: Strongly reduced activity.
- W214 (≠ R216) mutation to A: Almost abolished activity.
- Y219 (≠ M221) mutation to A: Strongly reduced activity.
- K246 (= K241) binding ; mutation to A: Almost abolished activity.
- D247 (= D242) mutation to A: Almost abolished activity.
Sites not aligning to the query:
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
32% identity, 97% coverage: 6:285/289 of query aligns to 3:283/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), Q10 (≠ A13), M11 (= M14), F29 (≠ Y32), D30 (≠ V33), V31 (≠ R34), M63 (≠ N66), L64 (≠ V67), V73 (= V76), S94 (= S97), T95 (= T98), R122 (≠ G125)
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
32% identity, 97% coverage: 6:285/289 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, 97% coverage: 6:285/289 of query aligns to 4:284/298 of P0A9V8
- QM 11:12 (≠ AM 13:14) binding
- D31 (≠ V33) binding
- L65 (≠ V67) binding
- T96 (= T98) binding
- G122 (≠ S124) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G125) 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 (≠ G126) 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 (≠ NQIAQ 176:180) binding
- K240 (= K241) binding
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
37% identity, 98% coverage: 6:288/289 of query aligns to 3:291/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), H10 (≠ A13), M11 (= M14), F29 (≠ Y32), D30 (≠ V33), L31 (≠ R34), M63 (≠ N66), L64 (≠ V67), P65 (≠ T68), T94 (= T98), V119 (= V123), G121 (= G125), F237 (≠ I234), K244 (= K241)
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
32% identity, 99% coverage: 2:287/289 of query aligns to 37:329/335 of P29266
- D68 (≠ V33) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K173) mutation K->A,H,N,R: Complete loss of activity.
- N212 (≠ Q177) mutation to Q: Decrease in activity.
3obbA Crystal structure of a possible 3-hydroxyisobutyrate dehydrogenase from pseudomonas aeruginosa pao1 (see paper)
36% identity, 98% coverage: 6:288/289 of query aligns to 4:292/295 of 3obbA
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
31% identity, 99% coverage: 2:287/289 of query aligns to 38:330/336 of P31937
- 40:68 (vs. 4:32, 48% identical) binding
- LP 103:104 (≠ VT 67:68) binding
- N108 (≠ D72) binding
- T134 (= T98) binding
- K284 (= K241) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
30% identity, 98% coverage: 6:287/289 of query aligns to 3:291/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), N10 (≠ A13), M11 (= M14), Y29 (= Y32), D30 (≠ V33), V31 (≠ R34), M63 (≠ N66), L64 (≠ V67), P65 (≠ T68), T95 (= T98), V120 (= V123), G122 (= G125), F238 (≠ I234), K245 (= K241)
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
29% identity, 98% coverage: 6:288/289 of query aligns to 4:286/287 of 3pefA
- binding glycerol: D67 (≠ S69), G123 (= G125), K171 (= K173), N175 (≠ Q177), M178 (≠ Q180), L203 (= L205), G207 (≠ A209), N213 (≠ S215), A217 (≠ D219), F232 (≠ I234), H236 (≠ L238), K239 (= K241), R242 (≠ G244), R269 (≠ M271)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G12), I11 (≠ A13), M12 (= M14), N31 (≠ V33), R32 (= R34), S33 (≠ R35), K36 (≠ A38), M64 (≠ N66), L65 (≠ V67), A66 (≠ T68), A70 (≠ D72), E73 (≠ A75), T96 (= T98), V121 (= V123), G123 (= G125), S124 (≠ G126), A231 (≠ G233), F232 (≠ I234), H236 (≠ L238), K239 (= K241)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
28% identity, 99% coverage: 4:288/289 of query aligns to 2:286/287 of 3pduA
- binding glycerol: R242 (≠ G244), E246 (= E248), E246 (= E248), R250 (≠ Q252)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), G10 (= G12), I11 (≠ A13), M12 (= M14), N31 (≠ V33), R32 (= R34), N33 (≠ R35), M64 (≠ N66), L65 (≠ V67), A66 (≠ T68), A70 (≠ D72), T96 (= T98), V121 (= V123), G123 (= G125), T124 (≠ G126), K171 (= K173), S231 (≠ G233), F232 (≠ I234), P233 (≠ E235), H236 (≠ L238), K239 (= K241)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
31% identity, 98% coverage: 6:288/289 of query aligns to 3:280/288 of 1wp4A
- active site: S116 (= S124), K164 (= K173), N167 (= N176), N168 (≠ Q177)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G10), L8 (= L11), G9 (= G12), A10 (= A13), M11 (= M14), N29 (≠ G26), R30 (≠ H27), T31 (≠ A28), K34 (≠ A31), C61 (≠ N66), L62 (≠ V67), P63 (≠ T68), E67 (≠ D72), S90 (≠ T98), V115 (= V123), T225 (≠ G233), F226 (≠ I234), K233 (= K241)
- binding sulfate ion: S116 (= S124), G117 (= G125), G118 (= G126), K164 (= K173)
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
31% identity, 98% coverage: 6:288/289 of query aligns to 4:281/289 of 2cvzC
- active site: S117 (= S124), K165 (= K173), N168 (= N176), N169 (≠ Q177)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), L9 (= L11), G10 (= G12), A11 (= A13), M12 (= M14), N30 (≠ G26), R31 (≠ H27), T32 (≠ A28), C62 (≠ N66), L63 (≠ V67), P64 (≠ T68), E68 (≠ D72), E71 (≠ A75), S91 (≠ T98), V116 (= V123), F227 (≠ I234), K234 (= K241)
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
38% identity, 88% coverage: 4:258/289 of query aligns to 1:259/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (= R150), E148 (≠ A154), A151 (≠ G157), K153 (≠ T159)
- binding nicotinamide-adenine-dinucleotide: G7 (= G10), G9 (= G12), N10 (≠ A13), M11 (= M14), F29 (≠ Y32), D30 (≠ V33), P31 (≠ R34), M63 (≠ N66), L64 (≠ V67), G120 (= G126), L239 (= L238), K242 (= K241)
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
38% identity, 88% coverage: 4:258/289 of query aligns to 2:260/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (≠ S134), E149 (≠ A154), A152 (≠ G157), G153 (≠ K158), G153 (≠ K158), K154 (≠ T159)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S124), G120 (= G125), W211 (vs. gap), F236 (≠ I234)
- binding nicotinamide-adenine-dinucleotide: G8 (= G10), G10 (= G12), N11 (≠ A13), M12 (= M14), F30 (≠ Y32), D31 (≠ V33), P32 (≠ R34), M64 (≠ N66), L65 (≠ V67), T93 (= T98), G121 (= G126), K168 (= K173), L240 (= L238), K243 (= K241)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
38% identity, 88% coverage: 4:258/289 of query aligns to 2:260/290 of 5y8kA
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
38% identity, 88% coverage: 4:258/289 of query aligns to 1:259/292 of 5y8iA
Query Sequence
>RR42_RS16835 FitnessBrowser__Cup4G11:RR42_RS16835
MSKTTIGFIGLGAMGTPMVRHLLAGGHAVRAYVRRPEAADAARALGAVPCTTPAQAARGA
SVVFTNVTSSQDVHAVLLGEHGVIEGAAPGTICIDHSTISPITTREIAARLAERGIEALD
CPVSGGTVGAEAASLTIMVGGKAEMLERVRPLLALLGKTITHIGDHGAGQVAKLCNQIAQ
VVNIEGIAEAMRFAQAQQVDSARVLQAMATGMAGSRMLDMMGPKMVAHDFAPGIEARLHD
KDFGLAAEIARQLGLELPAMQATSRQLGTLMEKGWGKDDTSSLLRVLEG
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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