SitesBLAST
Comparing WP_011969870.1 NCBI__GCF_000017145.1:WP_011969870.1 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)
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
56% identity, 97% coverage: 1:290/298 of query aligns to 1:289/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (= T129), E149 (= E149), A152 (≠ G152), G153 (≠ K153), G153 (≠ K153), K154 (= K154)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S119), G120 (= G120), W211 (= W211), F236 (= F236)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G10 (= G10), N11 (= N11), M12 (= M12), F30 (= F30), D31 (= D31), P32 (≠ L32), M64 (= M64), L65 (= L65), T93 (= T93), G121 (= G121), K168 (= K168), L240 (= L240), K243 (= K243)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
56% identity, 97% coverage: 1:290/298 of query aligns to 1:289/290 of 5y8kA
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
55% identity, 98% coverage: 2:294/298 of query aligns to 1:292/292 of 5y8iA
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
55% identity, 98% coverage: 2:292/298 of query aligns to 1:290/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (≠ K145), E148 (= E149), A151 (≠ G152), K153 (= K154)
- binding nicotinamide-adenine-dinucleotide: G7 (= G8), G9 (= G10), N10 (= N11), M11 (= M12), F29 (= F30), D30 (= D31), P31 (≠ L32), M63 (= M64), L64 (= L65), G120 (= G121), L239 (= L240), K242 (= K243)
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
41% identity, 98% coverage: 2:293/298 of query aligns to 39:333/335 of P29266
- D68 (= D31) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K168) mutation K->A,H,N,R: Complete loss of activity.
- N212 (= N172) mutation to Q: Decrease in activity.
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
41% identity, 98% coverage: 2:293/298 of query aligns to 40:334/336 of P31937
- 40:68 (vs. 2:30, 55% identical) binding NAD(+)
- LP 103:104 (= LP 65:66) binding NAD(+)
- N108 (≠ H70) binding NAD(+)
- T134 (= T93) binding NAD(+)
- K284 (= K243) binding NAD(+)
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
41% identity, 97% coverage: 4:293/298 of query aligns to 3:295/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), N10 (= N11), M11 (= M12), Y29 (≠ F30), D30 (= D31), V31 (≠ L32), M63 (= M64), L64 (= L65), P65 (= P66), T95 (= T93), V120 (= V118), G122 (= G120), F238 (= F236), K245 (= K243)
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
49% identity, 96% coverage: 3:289/298 of query aligns to 2:290/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), H10 (≠ N11), M11 (= M12), F29 (= F30), D30 (= D31), L31 (= L32), M63 (= M64), L64 (= L65), P65 (= P66), T94 (= T93), V119 (= V118), G121 (= G120), F237 (= F236), K244 (= K243)
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)
49% identity, 97% coverage: 1:289/298 of query aligns to 1:292/298 of Q9I5I6
- 2:31 (vs. 2:31, 63% identical) binding NAD(+)
- P66 (= P66) binding NAD(+)
- T96 (= T93) binding NAD(+); mutation to A: Almost abolished activity.
- S122 (= S119) mutation to A: Strongly reduced activity.
- K171 (= K168) active site
- N175 (= N172) mutation to A: Strongly reduced activity.
- W214 (= W211) mutation to A: Almost abolished activity.
- Y219 (= Y216) mutation to A: Strongly reduced activity.
- K246 (= K243) binding NAD(+); mutation to A: Almost abolished activity.
- D247 (= D244) mutation to A: Almost abolished activity.
3obbA Crystal structure of a possible 3-hydroxyisobutyrate dehydrogenase from pseudomonas aeruginosa pao1 (see paper)
48% identity, 97% coverage: 1:289/298 of query aligns to 1:291/295 of 3obbA
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
33% identity, 96% coverage: 1:285/298 of query aligns to 3:285/294 of 5je8B
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)
34% identity, 95% coverage: 3:285/298 of query aligns to 15:290/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G8), L21 (= L9), G22 (= G10), I23 (≠ N11), M24 (= M12), N43 (≠ D31), R44 (≠ L32), T45 (≠ L33), K48 (≠ S36), M76 (= M64), V77 (≠ L65), S78 (vs. gap), D82 (≠ A67), Q85 (≠ H70), V133 (= V118), F241 (= F236), K242 (≠ A237), H245 (≠ L240), K248 (= K243)
- binding sulfate ion: T134 (≠ S119), G135 (= G120), K183 (= K168)
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
33% identity, 95% coverage: 3:285/298 of query aligns to 15:293/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G8), L21 (= L9), G22 (= G10), I23 (≠ N11), M24 (= M12), N43 (≠ D31), R44 (≠ L32), T45 (≠ L33), K48 (≠ S36), V77 (≠ L65), S78 (vs. gap), D82 (≠ A67), Q85 (≠ H70), V133 (= V118), F244 (= F236), K245 (≠ A237), H248 (≠ L240), K251 (= K243)
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
32% identity, 97% coverage: 1:290/298 of query aligns to 1:282/289 of 2cvzC
- active site: S117 (= S119), K165 (= K168), N168 (= N171), N169 (= N172)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G8), L9 (= L9), G10 (= G10), A11 (≠ N11), M12 (= M12), N30 (≠ F30), R31 (≠ D31), T32 (≠ L32), C62 (≠ M64), L63 (= L65), P64 (= P66), E68 (≠ H70), E71 (≠ Y73), S91 (≠ T93), V116 (= V118), F227 (= F236), K234 (= K243)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
32% identity, 97% coverage: 3:290/298 of query aligns to 2:281/288 of 1wp4A
- active site: S116 (= S119), K164 (= K168), N167 (= N171), N168 (= N172)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G8), L8 (= L9), G9 (= G10), A10 (≠ N11), M11 (= M12), N29 (≠ F30), R30 (≠ D31), T31 (≠ L32), K34 (≠ A35), C61 (≠ M64), L62 (= L65), P63 (= P66), E67 (≠ H70), S90 (≠ T93), V115 (= V118), T225 (≠ G235), F226 (= F236), K233 (= K243)
- binding sulfate ion: S116 (= S119), G117 (= G120), G118 (= G121), K164 (= K168)
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: 1:290/298 of query aligns to 1:287/298 of P0A9V8
- QM 11:12 (≠ NM 11:12) binding NAD(+)
- D31 (= D31) binding NAD(+)
- L65 (= L65) binding NAD(+)
- T96 (= T93) binding NAD(+)
- G122 (≠ S119) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G120) 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 (≠ G121) 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 171:175) binding 2,3-dihydroxypropane-1-sulfonate
- K240 (= K243) binding NAD(+)
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
32% identity, 96% coverage: 4:290/298 of query aligns to 3:286/294 of 6smyA
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
32% identity, 96% coverage: 4:290/298 of query aligns to 3:286/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), Q10 (≠ N11), M11 (= M12), F29 (= F30), D30 (= D31), V31 (≠ L32), M63 (= M64), L64 (= L65), V73 (= V71), S94 (= S92), T95 (= T93), R122 (≠ G120)
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
31% identity, 96% coverage: 3:287/298 of query aligns to 3:283/287 of 3pefA
- binding glycerol: D67 (vs. gap), G123 (= G120), K171 (= K168), N175 (= N172), M178 (≠ L175), L203 (≠ F200), G207 (vs. gap), N213 (≠ G208), A217 (≠ S212), F232 (= F236), H236 (≠ L240), K239 (= K243), R242 (≠ K246), R269 (≠ E273)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G10), I11 (≠ N11), M12 (= M12), N31 (≠ D31), R32 (≠ L32), S33 (≠ L33), K36 (≠ S36), M64 (= M64), L65 (= L65), A66 (vs. gap), A70 (≠ S68), E73 (vs. gap), T96 (= T93), V121 (= V118), G123 (= G120), S124 (≠ G121), A231 (≠ G235), F232 (= F236), H236 (≠ L240), K239 (= K243)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
32% identity, 97% coverage: 1:289/298 of query aligns to 1:285/287 of 3pduA
- binding glycerol: R242 (≠ K246), E246 (≠ Q250), E246 (≠ Q250), R250 (≠ A254)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G8), G10 (= G10), I11 (≠ N11), M12 (= M12), N31 (≠ D31), R32 (≠ L32), N33 (≠ L33), M64 (= M64), L65 (= L65), A66 (vs. gap), A70 (≠ S68), T96 (= T93), V121 (= V118), G123 (= G120), T124 (≠ G121), K171 (= K168), S231 (= S226), F232 (= F236), P233 (≠ A237), H236 (≠ L240), K239 (= K243)
Query Sequence
>WP_011969870.1 NCBI__GCF_000017145.1:WP_011969870.1
MTKIAFIGLGNMGGPMAANLVKAGHAVTGFDLLEASRNAAAKSGVSVAGSIAQAVREMEC
VITMLPASAHVLYVWDELLGFVDPGTLLIDSSTIDVESARKVHGLAEKANCPSLDAPVSG
GTAGAAGATLTFMVGGSDGAFSRGKHLLEAMGKKIVHCGDAGAGQAAKICNNMILGVSMA
AVCEAFVLAERLGLSHQALFDVASTSSGQCWSLTTYCPVPGPVPTSPANSGYKPGFAASL
MLKDLKLSQQAASASGAATPMGAQAMQLYSLFEKLGHGSEDFSALIHLLRGNEEGKAE
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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