SitesBLAST
Comparing 3608350 FitnessBrowser__Dino:3608350 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)
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
46% identity, 98% coverage: 3:287/291 of query aligns to 3:290/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (= R139), E148 (≠ D143), A151 (≠ G146), K153 (= K148)
- binding nicotinamide-adenine-dinucleotide: G7 (= G7), G9 (= G9), N10 (= N10), M11 (= M11), F29 (= F29), D30 (= D30), P31 (vs. gap), M63 (= M58), L64 (= L59), G120 (= G115), L239 (= L234), K242 (= K237)
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
46% identity, 98% coverage: 3:287/291 of query aligns to 3:290/292 of 5y8iA
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
47% identity, 96% coverage: 3:281/291 of query aligns to 4:285/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (= T123), E149 (≠ D143), A152 (≠ G146), G153 (≠ Q147), G153 (≠ Q147), K154 (= K148)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S113), G120 (= G114), W211 (= W205), F236 (= F230)
- binding nicotinamide-adenine-dinucleotide: G8 (= G7), G10 (= G9), N11 (= N10), M12 (= M11), F30 (= F29), D31 (= D30), P32 (vs. gap), M64 (= M58), L65 (= L59), T93 (= T87), G121 (= G115), K168 (= K162), L240 (= L234), K243 (= K237)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
47% identity, 96% coverage: 3:281/291 of query aligns to 4:285/290 of 5y8kA
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
39% identity, 96% coverage: 3:281/291 of query aligns to 41:326/335 of P29266
- D68 (= D30) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K162) mutation K->A,H,N,R: Complete loss of activity.
- N212 (= N166) mutation to Q: Decrease in activity.
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
39% identity, 97% coverage: 1:281/291 of query aligns to 1:288/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), N10 (= N10), M11 (= M11), Y29 (≠ F29), D30 (= D30), V31 (≠ L31), M63 (= M58), L64 (= L59), P65 (= P60), T95 (= T87), V120 (= V112), G122 (= G114), F238 (= F230), K245 (= K237)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
39% identity, 96% coverage: 3:281/291 of query aligns to 42:327/336 of P31937
- LP 103:104 (= LP 59:60) binding
- N108 (= N61) binding
- T134 (= T87) binding
- K284 (= K237) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
- 40:68 binding
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
45% identity, 97% coverage: 2:284/291 of query aligns to 2:290/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), H10 (≠ N10), M11 (= M11), F29 (= F29), D30 (= D30), L31 (= L31), M63 (= M58), L64 (= L59), P65 (= P60), T94 (= T87), V119 (= V112), G121 (= G114), F237 (= F230), K244 (= 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)
45% identity, 97% coverage: 2:284/291 of query aligns to 3:292/298 of Q9I5I6
- P66 (= P60) binding
- T96 (= T87) binding ; mutation to A: Almost abolished activity.
- S122 (= S113) mutation to A: Strongly reduced activity.
- K171 (= K162) active site
- N175 (= N166) mutation to A: Strongly reduced activity.
- W214 (= W205) mutation to A: Almost abolished activity.
- Y219 (= Y210) mutation to A: Strongly reduced activity.
- K246 (= K237) binding ; mutation to A: Almost abolished activity.
- D247 (= D238) mutation to A: Almost abolished activity.
Sites not aligning to the query:
3obbA Crystal structure of a possible 3-hydroxyisobutyrate dehydrogenase from pseudomonas aeruginosa pao1 (see paper)
44% identity, 97% coverage: 2:284/291 of query aligns to 3:291/295 of 3obbA
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)
36% identity, 92% coverage: 1:268/291 of query aligns to 14:279/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G7), L21 (= L8), G22 (= G9), I23 (≠ N10), M24 (= M11), N43 (≠ D30), R44 (≠ L31), T45 (= T32), K48 (vs. gap), M76 (= M58), V77 (≠ L59), S78 (≠ P60), D82 (≠ I64), Q85 (≠ S67), V133 (= V112), F241 (= F230), K242 (≠ A231), H245 (≠ L234), K248 (= K237)
- binding sulfate ion: T134 (≠ S113), G135 (= G114), K183 (= K162)
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
35% identity, 92% coverage: 1:268/291 of query aligns to 14:282/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G7), L21 (= L8), G22 (= G9), I23 (≠ N10), M24 (= M11), N43 (≠ D30), R44 (≠ L31), T45 (= T32), K48 (vs. gap), V77 (≠ L59), S78 (≠ P60), D82 (≠ I64), Q85 (≠ S67), V133 (= V112), F244 (= F230), K245 (≠ A231), H248 (≠ L234), K251 (= K237)
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
31% identity, 98% coverage: 2:287/291 of query aligns to 5:292/294 of 5je8B
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
34% identity, 90% coverage: 2:264/291 of query aligns to 2:260/288 of 1wp4A
- active site: S116 (= S113), K164 (= K162), N167 (= N165), N168 (= N166)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G7), L8 (= L8), G9 (= G9), A10 (≠ N10), M11 (= M11), N29 (vs. gap), R30 (vs. gap), T31 (vs. gap), K34 (≠ L31), C61 (≠ M58), L62 (= L59), P63 (= P60), E67 (≠ I64), S90 (≠ T87), V115 (= V112), T225 (≠ G229), F226 (= F230), K233 (= K237)
- binding sulfate ion: S116 (= S113), G117 (= G114), G118 (= G115), K164 (= K162)
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
34% identity, 90% coverage: 2:264/291 of query aligns to 3:261/289 of 2cvzC
- active site: S117 (= S113), K165 (= K162), N168 (= N165), N169 (= N166)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G7), L9 (= L8), G10 (= G9), A11 (≠ N10), M12 (= M11), N30 (vs. gap), R31 (vs. gap), T32 (vs. gap), C62 (≠ M58), L63 (= L59), P64 (= P60), E68 (≠ I64), E71 (≠ S67), S91 (≠ T87), V116 (= V112), F227 (= F230), K234 (= K237)
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
33% identity, 97% coverage: 2:284/291 of query aligns to 3:285/287 of 3pefA
- binding glycerol: D67 (≠ N61), G123 (= G114), K171 (= K162), N175 (= N166), M178 (≠ L169), L203 (≠ F194), G207 (≠ S198), N213 (≠ C211), A217 (≠ G215), F232 (= F230), H236 (≠ L234), K239 (= K237), R242 (= R240), R269 (≠ E268)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G9), I11 (≠ N10), M12 (= M11), N31 (≠ D30), R32 (≠ L31), S33 (≠ T32), K36 (≠ V35), M64 (= M58), L65 (= L59), A66 (≠ P60), A70 (≠ I64), E73 (≠ S67), T96 (= T87), V121 (= V112), G123 (= G114), S124 (≠ G115), A231 (≠ G229), F232 (= F230), H236 (≠ L234), K239 (= K237)
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
31% identity, 97% coverage: 3:283/291 of query aligns to 3:284/294 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)
31% identity, 97% coverage: 3:283/291 of query aligns to 4:285/298 of P0A9V8
- QM 11:12 (≠ NM 10:11) binding
- D31 (= D30) binding
- L65 (= L59) binding
- T96 (= T87) binding
- G122 (≠ S113) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G114) 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 (≠ G115) 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 (≠ NNMIL 165:169) binding
- K240 (= K237) binding
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
31% identity, 97% coverage: 3:283/291 of query aligns to 3:284/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), Q10 (≠ N10), M11 (= M11), F29 (= F29), D30 (= D30), V31 (≠ L31), M63 (= M58), L64 (= L59), V73 (= V68), S94 (= S86), T95 (= T87), R122 (≠ G114)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
34% identity, 96% coverage: 4:281/291 of query aligns to 5:282/287 of 3pduA
- binding glycerol: R242 (= R240), E246 (≠ Q244), E246 (≠ Q244), R250 (≠ A248)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G7), G10 (= G9), I11 (≠ N10), M12 (= M11), N31 (≠ D30), R32 (≠ L31), N33 (≠ T32), M64 (= M58), L65 (= L59), A66 (≠ P60), A70 (≠ I64), T96 (= T87), V121 (= V112), G123 (= G114), T124 (≠ G115), K171 (= K162), S231 (≠ G229), F232 (= F230), P233 (≠ A231), H236 (≠ L234), K239 (= K237)
Query Sequence
>3608350 FitnessBrowser__Dino:3608350
MKIGFVGLGNMGAPMARNLAAAGHAVTGFDLTAPVPEGVTGAASAAEAAAGAEVVITMLP
NGAILRSVAAELIPAMAPGAVLLDCSTVDVESARAVAAQAEAAGLGALDAPVSGGTGGAE
AGTLTFMVGGSDAAFATARPLFDIMGQKAVHCGGAGNGQAAKICNNMILGVTMVATCEGF
ALADKLGLDRQALFDVVSTSSGYSWSMNVYCPAPGIGPESPADRDYAPGFAAELMLKDLR
LSQQAAEAVDADTPTGATATALFETFVETEGMGKKDFTAILPRFAAKGRAS
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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