SitesBLAST
Comparing GFF4636 FitnessBrowser__WCS417:GFF4636 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)
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
51% identity, 99% coverage: 3:293/295 of query aligns to 41:331/335 of P29266
- D68 (= D30) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K170) mutation K->A,H,N,R: Complete loss of activity.
- N212 (= N174) mutation to Q: Decrease in activity.
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
49% identity, 99% coverage: 1:293/295 of query aligns to 1:293/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), N10 (= N10), M11 (= M11), Y29 (≠ F29), D30 (= D30), V31 (≠ L31), M63 (= M63), L64 (= L64), P65 (= P65), T95 (= T95), V120 (= V120), G122 (= G122), F238 (= F238), K245 (= K245)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
49% identity, 99% coverage: 3:293/295 of query aligns to 42:332/336 of P31937
- LP 103:104 (= LP 64:65) binding
- N108 (≠ H69) binding
- T134 (= T95) binding
- K284 (= K245) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
- 40:68 binding
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)
51% identity, 97% coverage: 2:287/295 of query aligns to 3:288/298 of Q9I5I6
- P66 (= P65) binding
- T96 (= T95) binding ; mutation to A: Almost abolished activity.
- S122 (= S121) mutation to A: Strongly reduced activity.
- K171 (= K170) active site
- N175 (= N174) mutation to A: Strongly reduced activity.
- W214 (= W213) mutation to A: Almost abolished activity.
- Y219 (= Y218) mutation to A: Strongly reduced activity.
- K246 (= K245) binding ; mutation to A: Almost abolished activity.
- D247 (= D246) mutation to A: Almost abolished activity.
Sites not aligning to the query:
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
51% identity, 97% coverage: 2:287/295 of query aligns to 2:286/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), H10 (≠ N10), M11 (= M11), F29 (= F29), D30 (= D30), L31 (= L31), M63 (= M63), L64 (= L64), P65 (= P65), T94 (= T95), V119 (= V120), G121 (= G122), F237 (= F238), K244 (= K245)
3obbA Crystal structure of a possible 3-hydroxyisobutyrate dehydrogenase from pseudomonas aeruginosa pao1 (see paper)
51% identity, 97% coverage: 2:287/295 of query aligns to 3:287/295 of 3obbA
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
40% identity, 98% coverage: 3:292/295 of query aligns to 3:288/292 of 5y8iA
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
40% identity, 98% coverage: 3:292/295 of query aligns to 3:288/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (≠ Q147), E148 (≠ A151), A151 (≠ G154), K153 (≠ N156)
- binding nicotinamide-adenine-dinucleotide: G7 (= G7), G9 (= G9), N10 (= N10), M11 (= M11), F29 (= F29), D30 (= D30), P31 (≠ L31), M63 (= M63), L64 (= L64), G120 (= G123), L239 (= L242), K242 (= K245)
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
40% identity, 98% coverage: 3:292/295 of query aligns to 4:289/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (= T131), E149 (≠ A151), A152 (≠ G154), G153 (≠ R155), G153 (≠ R155), K154 (≠ N156)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S121), G120 (= G122), W211 (= W213), F236 (= F238)
- binding nicotinamide-adenine-dinucleotide: G8 (= G7), G10 (= G9), N11 (= N10), M12 (= M11), F30 (= F29), D31 (= D30), P32 (≠ L31), M64 (= M63), L65 (= L64), T93 (= T95), G121 (= G123), K168 (= K170), L240 (= L242), K243 (= K245)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
40% identity, 98% coverage: 3:292/295 of query aligns to 4:289/290 of 5y8kA
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
38% identity, 95% coverage: 1:280/295 of query aligns to 14:286/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G7), L21 (= L8), G22 (= G9), I23 (≠ N10), M24 (= M11), N43 (≠ D30), R44 (≠ L31), T45 (≠ N32), K48 (≠ V35), V77 (≠ L64), S78 (≠ P65), D82 (≠ H69), Q85 (≠ S72), V133 (= V120), F244 (= F238), K245 (≠ G239), H248 (≠ L242), K251 (= K245)
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: 1:280/295 of query aligns to 14:283/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G7), L21 (= L8), G22 (= G9), I23 (≠ N10), M24 (= M11), N43 (≠ D30), R44 (≠ L31), T45 (≠ N32), K48 (≠ V35), M76 (= M63), V77 (≠ L64), S78 (≠ P65), D82 (≠ H69), Q85 (≠ S72), V133 (= V120), F241 (= F238), K242 (≠ G239), H245 (≠ L242), K248 (= K245)
- binding sulfate ion: T134 (≠ S121), G135 (= G122), K183 (= K170)
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
34% identity, 99% coverage: 2:293/295 of query aligns to 5:288/294 of 5je8B
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
35% identity, 98% coverage: 3:292/295 of query aligns to 3:286/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), Q10 (≠ N10), M11 (= M11), F29 (= F29), D30 (= D30), V31 (≠ L31), M63 (= M63), L64 (= L64), V73 (= V73), S94 (= S94), T95 (= T95), R122 (≠ G122)
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
35% identity, 98% coverage: 3:292/295 of query aligns to 3:286/294 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)
35% identity, 98% coverage: 3:292/295 of query aligns to 4:287/298 of P0A9V8
- QM 11:12 (≠ NM 10:11) binding
- D31 (= D30) binding
- L65 (= L64) binding
- T96 (= T95) binding
- G122 (≠ S121) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G122) 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 (≠ G123) mutation to G: 230-fold decrease in catalytic efficiency with SLA as substrate. 12-fold decrease in catalytic efficiency with NADH as substrate.
- NN-YMS 174:178 (≠ NNLLLG 173:178) binding
- K240 (= K245) binding
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
32% identity, 99% coverage: 2:293/295 of query aligns to 3:287/287 of 3pefA
- binding glycerol: D67 (≠ A66), G123 (= G122), K171 (= K170), N175 (= N174), M178 (≠ L177), L203 (≠ A202), G207 (≠ N206), N213 (= N219), A217 (≠ G223), F232 (= F238), H236 (≠ L242), K239 (= K245), R242 (≠ G248), R269 (≠ S275)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G9), I11 (≠ N10), M12 (= M11), N31 (≠ D30), R32 (≠ L31), S33 (≠ N32), K36 (≠ V35), M64 (= M63), L65 (= L64), A66 (≠ P65), A70 (≠ H69), E73 (≠ S72), T96 (= T95), V121 (= V120), G123 (= G122), S124 (≠ G123), A231 (≠ G237), F232 (= F238), H236 (≠ L242), K239 (= K245)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
32% identity, 97% coverage: 5:289/295 of query aligns to 6:283/287 of 3pduA
- binding glycerol: R242 (≠ G248), E246 (= E252), E246 (= E252), R250 (≠ Q256)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G7), G10 (= G9), I11 (≠ N10), M12 (= M11), N31 (≠ D30), R32 (≠ L31), N33 (= N32), M64 (= M63), L65 (= L64), A66 (≠ P65), A70 (≠ H69), T96 (= T95), V121 (= V120), G123 (= G122), T124 (≠ G123), K171 (= K170), S231 (≠ G237), F232 (= F238), P233 (≠ G239), H236 (≠ L242), K239 (= K245)
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
34% identity, 96% coverage: 2:283/295 of query aligns to 3:270/289 of 2cvzC
- active site: S117 (= S121), K165 (= K170), N168 (= N173), N169 (= N174)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G7), L9 (= L8), G10 (= G9), A11 (≠ N10), M12 (= M11), N30 (≠ F29), R31 (≠ D30), T32 (≠ L31), C62 (≠ M63), L63 (= L64), P64 (= P65), E68 (≠ S72), E71 (≠ L75), S91 (≠ T95), V116 (= V120), F227 (= F238), K234 (= K245)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
33% identity, 94% coverage: 2:277/295 of query aligns to 2:264/288 of 1wp4A
- active site: S116 (= S121), K164 (= K170), N167 (= N173), N168 (= N174)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G7), L8 (= L8), G9 (= G9), A10 (≠ N10), M11 (= M11), N29 (≠ F29), R30 (≠ D30), T31 (≠ L31), K34 (≠ T34), C61 (≠ M63), L62 (= L64), P63 (= P65), E67 (≠ S72), S90 (≠ T95), V115 (= V120), T225 (≠ G237), F226 (= F238), K233 (= K245)
- binding sulfate ion: S116 (= S121), G117 (= G122), G118 (= G123), K164 (= K170)
Query Sequence
>GFF4636 FitnessBrowser__WCS417:GFF4636
MKIAFIGLGNMGAPMARNLIKAGHALNLFDLNQTVLKELAELGGTVSESPRDAAKDAELV
ITMLPAAAHVRSVWLNEDGVLAGIGKGVPAVDCSTIDPQTIRDVAAAAAKQDVAVADAPV
SGGTGGAQAGTLTFMVGANPELFATLQPVLAQMGRNIVHCGEVGTGQIAKICNNLLLGIS
MVGVSEAMALGDALGIDTQVLAGIINSSTGRCWSSDTYNPWPGVIETAPSSRGYTGGFGA
DLMLKDLGLATEAARQVKQPVILGAVAQQLYQSMSQRGEGGKDFSAIINSYRKPK
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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