SitesBLAST
Comparing BPHYT_RS08825 FitnessBrowser__BFirm:BPHYT_RS08825 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)
41% identity, 89% coverage: 3:270/302 of query aligns to 15:284/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G8), L21 (= L9), G22 (= G10), I23 (= I11), M24 (= M12), N43 (≠ P34), R44 (≠ V35), T45 (≠ P36), K48 (≠ L39), V77 (= V63), S78 (≠ P64), D82 (= D68), Q85 (≠ N71), 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)
41% identity, 89% coverage: 3:270/302 of query aligns to 15:281/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G8), L21 (= L9), G22 (= G10), I23 (= I11), M24 (= M12), N43 (≠ P34), R44 (≠ V35), T45 (≠ P36), K48 (≠ L39), M76 (= M62), V77 (= V63), S78 (≠ P64), D82 (= D68), Q85 (≠ N71), 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)
34% identity, 95% coverage: 4:289/302 of query aligns to 41:335/335 of P29266
- D68 (≠ G31) 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.
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
33% identity, 95% coverage: 4:289/302 of query aligns to 42:336/336 of P31937
- LP 103:104 (≠ VP 63:64) binding
- N108 (≠ D68) binding
- T134 (≠ S94) binding
- K284 (= K237) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
- 40:68 binding
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
33% identity, 93% coverage: 4:284/302 of query aligns to 3:292/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), N10 (≠ I11), M11 (= M12), Y29 (≠ N30), D30 (≠ G31), V31 (≠ A32), M63 (= M62), L64 (≠ V63), P65 (= P64), T95 (≠ S94), V120 (= V119), G122 (= G121), F238 (= F230), K245 (= K237)
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)
34% identity, 95% coverage: 1:287/302 of query aligns to 1:290/298 of P0A9V8
- QM 11:12 (≠ IM 11:12) binding
- D31 (≠ V29) binding
- L65 (≠ V63) binding
- T96 (≠ S94) binding
- 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 ; 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 (≠ NQII- 172:175) binding
- K240 (= K237) binding
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
29% identity, 94% coverage: 1:283/302 of query aligns to 3:289/294 of 5je8B
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
33% identity, 95% coverage: 2:287/302 of query aligns to 1:289/294 of 6smyA
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
33% identity, 95% coverage: 2:287/302 of query aligns to 1:289/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), Q10 (≠ I11), M11 (= M12), F29 (= F28), D30 (≠ V29), V31 (≠ N30), M63 (= M62), L64 (≠ V63), V73 (= V72), S94 (= S93), T95 (≠ S94), R122 (≠ G121)
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
30% identity, 93% coverage: 3:284/302 of query aligns to 3:286/287 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 (≠ N240), R269 (≠ A267)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G10), I11 (= I11), M12 (= M12), N31 (≠ G31), R32 (≠ A32), S33 (≠ Y33), K36 (≠ P36), M64 (= M62), L65 (≠ V63), A66 (≠ P64), A70 (≠ D68), E73 (≠ N71), 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)
31% identity, 94% coverage: 1:284/302 of query aligns to 1:286/287 of 3pduA
- binding glycerol: R242 (≠ N240), E246 (≠ D244), E246 (≠ D244), R250 (≠ K248)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G8), G10 (= G10), I11 (= I11), M12 (= M12), N31 (≠ G31), R32 (≠ A32), N33 (≠ Y33), M64 (= M62), L65 (≠ V63), 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)
36% identity, 80% coverage: 1:241/302 of query aligns to 1:250/298 of Q9I5I6
- 2:31 (vs. 2:31, 57% identical) binding
- P66 (= P64) binding
- T96 (≠ S94) binding ; 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 ; mutation to A: Almost abolished activity.
- D247 (= D238) mutation to A: Almost abolished activity.
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
36% identity, 79% coverage: 3:241/302 of query aligns to 2:248/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), H10 (≠ I11), M11 (= M12), F29 (≠ N30), D30 (≠ G31), L31 (≠ A32), M63 (= M62), L64 (≠ V63), 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)
35% identity, 80% coverage: 1:241/302 of query aligns to 1:249/295 of 3obbA
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
29% identity, 96% coverage: 1:291/302 of query aligns to 1:288/289 of 2cvzC
- active site: S117 (= S120), K165 (= K169), N168 (= N172), N169 (≠ Q173)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G8), L9 (= L9), G10 (= G10), A11 (≠ I11), M12 (= M12), N30 (= N30), R31 (≠ G31), T32 (≠ A32), C62 (≠ M62), L63 (≠ V63), P64 (= P64), E68 (≠ D68), E71 (≠ N71), S91 (= S94), V116 (= V119), F227 (= F230), K234 (= K237)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
29% identity, 96% coverage: 3:291/302 of query aligns to 2:287/288 of 1wp4A
- active site: S116 (= S120), K164 (= K169), N167 (= N172), N168 (≠ Q173)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G8), L8 (= L9), G9 (= G10), A10 (≠ I11), M11 (= M12), N29 (= N30), R30 (≠ G31), T31 (≠ A32), K34 (≠ E37), C61 (≠ M62), L62 (≠ V63), P63 (= P64), E67 (≠ D68), S90 (= S94), V115 (= V119), T225 (≠ G229), F226 (= F230), K233 (= K237)
- binding sulfate ion: S116 (= S120), G117 (= G121), G118 (= G122), K164 (= K169)
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
34% identity, 94% coverage: 1:284/302 of query aligns to 1:289/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (≠ S130), E149 (= E150), A152 (≠ G153), G153 (≠ K154), G153 (≠ K154), K154 (≠ N155)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S120), G120 (= G121), W211 (≠ L214), F236 (= F230)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G10 (= G10), N11 (≠ I11), M12 (= M12), F30 (≠ A32), D31 (≠ Y33), P32 (= P34), M64 (= M62), L65 (≠ V63), T93 (≠ S94), G121 (= G122), K168 (= K169), L240 (= L234), K243 (= K237)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
34% identity, 94% coverage: 1:284/302 of query aligns to 1:289/290 of 5y8kA
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
33% identity, 95% coverage: 3:288/302 of query aligns to 2:292/292 of 5y8iA
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
34% identity, 93% coverage: 3:284/302 of query aligns to 2:288/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (≠ K146), E148 (= E150), A151 (≠ G153), K153 (≠ N155)
- binding nicotinamide-adenine-dinucleotide: G7 (= G8), G9 (= G10), N10 (≠ I11), M11 (= M12), F29 (≠ A32), D30 (≠ Y33), P31 (= P34), M63 (= M62), L64 (≠ V63), G120 (= G122), L239 (= L234), K242 (= K237)
Query Sequence
>BPHYT_RS08825 FitnessBrowser__BFirm:BPHYT_RS08825
MAKIGFIGLGIMGAHMARNLIKGGHSLFVNGAYPVPEDLSKTTSVVANSTAVAQAADIVI
IMVPDTPDVANVLFADDGVAAGLSKGKLVIDMSSISPLDTQAFAKKINALGVDYLDAPVS
GGEVGAREASLTIMVGGPEKAFATAKPLFELMGKNISLIGENGAGQTCKVANQIIVALNI
EAVAEALLFAARSGADPERVRKALMGGFASSRILEVHGERMTKRKFDPGFRIELHQKDLN
LALDGARKLGIALPHTASAQQLFSVCAANGGKAWDHSAMVRALEIMANFEVAQAPGSEAK
AA
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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