SitesBLAST
Comparing SMc00274 FitnessBrowser__Smeli:SMc00274 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)
31% identity, 98% coverage: 1:290/295 of query aligns to 35:331/335 of P29266
- D68 (= D34) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K174) mutation K->A,H,N,R: Complete loss of activity.
- N212 (≠ Q178) mutation to Q: Decrease in activity.
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
31% identity, 98% coverage: 7:295/295 of query aligns to 3:292/294 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, 98% coverage: 7:295/295 of query aligns to 4:293/298 of P0A9V8
- QM 11:12 (≠ SM 14:15) binding
- D31 (= D34) binding
- L65 (≠ V68) 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 (≠ NQLLC 177:181) binding
- K240 (= K242) binding
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
31% identity, 98% coverage: 7:295/295 of query aligns to 3:292/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), Q10 (≠ S14), M11 (= M15), F29 (= F33), D30 (= D34), V31 (= V35), M63 (= M67), L64 (≠ V68), V73 (= V77), S94 (≠ A97), T95 (= T98), R122 (≠ G125)
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
30% identity, 92% coverage: 6:276/295 of query aligns to 15:287/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G11), L21 (= L12), G22 (= G13), I23 (≠ S14), M24 (= M15), N43 (≠ D34), R44 (≠ V35), T45 (≠ R36), K48 (≠ A39), V77 (= V68), S78 (≠ V69), D82 (≠ Q73), Q85 (≠ S76), V133 (= V123), F244 (≠ S235), K245 (≠ A236), H248 (≠ I239), K251 (= K242)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
32% identity, 97% coverage: 4:290/295 of query aligns to 39:332/336 of P31937
- 40:68 (vs. 5:33, 45% identical) binding
- LP 103:104 (≠ V- 68) binding
- N108 (= N70) binding
- T134 (= T98) binding
- K284 (= K242) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
32% identity, 96% coverage: 7:290/295 of query aligns to 3:293/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), N10 (≠ S14), M11 (= M15), Y29 (≠ F33), D30 (= D34), V31 (= V35), M63 (= M67), L64 (≠ V68), P65 (vs. gap), T95 (= T98), V120 (= V123), G122 (= G125), F238 (vs. gap), K245 (= K242)
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)
30% identity, 92% coverage: 6:276/295 of query aligns to 15:284/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G11), L21 (= L12), G22 (= G13), I23 (≠ S14), M24 (= M15), N43 (≠ D34), R44 (≠ V35), T45 (≠ R36), K48 (≠ A39), M76 (= M67), V77 (= V68), S78 (≠ V69), D82 (≠ Q73), Q85 (≠ S76), V133 (= V123), F241 (≠ S235), K242 (≠ A236), H245 (≠ I239), K248 (= K242)
- binding sulfate ion: T134 (≠ S124), G135 (= G125), K183 (= K174)
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
31% identity, 97% coverage: 5:290/295 of query aligns to 2:287/287 of 3pefA
- binding glycerol: D67 (≠ N70), G123 (= G125), K171 (= K174), N175 (≠ Q178), M178 (≠ C181), L203 (= L206), G207 (≠ S210), N213 (≠ S216), A217 (≠ K220), F232 (≠ S235), H236 (≠ I239), K239 (= K242), R242 (≠ G245), R269 (≠ S272)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G13), I11 (≠ S14), M12 (= M15), N31 (≠ D34), R32 (≠ V35), S33 (≠ R36), K36 (≠ A39), M64 (= M67), L65 (≠ V68), A66 (≠ V69), A70 (≠ Q73), E73 (≠ S76), T96 (= T98), V121 (= V123), G123 (= G125), S124 (≠ G126), A231 (≠ T234), F232 (≠ S235), H236 (≠ I239), K239 (= K242)
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
28% identity, 97% coverage: 5:291/295 of query aligns to 4:289/294 of 5je8B
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
36% identity, 75% coverage: 5:224/295 of query aligns to 1:219/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), H10 (≠ S14), M11 (= M15), F29 (= F33), D30 (= D34), L31 (≠ V35), M63 (= M67), L64 (≠ V68), P65 (≠ V69), T94 (= T98), V119 (= V123), G121 (= G125)
Sites not aligning to the query:
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
31% identity, 94% coverage: 9:285/295 of query aligns to 6:282/287 of 3pduA
- binding glycerol: R242 (≠ G245), E246 (≠ A249), E246 (≠ A249), R250 (≠ S253)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), G10 (= G13), I11 (≠ S14), M12 (= M15), N31 (≠ D34), R32 (≠ V35), N33 (≠ R36), M64 (= M67), L65 (≠ V68), A66 (≠ V69), A70 (≠ Q73), T96 (= T98), V121 (= V123), G123 (= G125), T124 (≠ G126), K171 (= K174), S231 (≠ T234), F232 (≠ S235), P233 (≠ A236), H236 (≠ I239), K239 (= K242)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
34% identity, 89% coverage: 5:268/295 of query aligns to 1:259/288 of 1wp4A
- active site: S116 (= S124), K164 (= K174), N167 (= N177), N168 (≠ Q178)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G11), L8 (= L12), G9 (= G13), A10 (≠ S14), M11 (= M15), N29 (vs. gap), R30 (= R31), T31 (≠ G32), K34 (≠ V35), C61 (≠ M67), L62 (≠ V68), P63 (≠ V69), E67 (≠ Q73), S90 (≠ T98), V115 (= V123), T225 (= T234), F226 (≠ S235), K233 (= K242)
- binding sulfate ion: S116 (= S124), G117 (= G125), G118 (= G126), K164 (= K174)
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
34% identity, 89% coverage: 5:268/295 of query aligns to 2:260/289 of 2cvzC
- active site: S117 (= S124), K165 (= K174), N168 (= N177), N169 (≠ Q178)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), L9 (= L12), G10 (= G13), A11 (≠ S14), M12 (= M15), N30 (vs. gap), R31 (= R31), T32 (≠ G32), C62 (≠ M67), L63 (≠ V68), P64 (≠ V69), E68 (≠ Q73), E71 (≠ S76), S91 (≠ T98), V116 (= V123), F227 (≠ S235), K234 (= K242)
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, 75% coverage: 5:224/295 of query aligns to 2:221/298 of Q9I5I6
- 2:31 (vs. 5:34, 57% identical) binding
- P66 (≠ V69) binding
- T96 (= T98) binding ; mutation to A: Almost abolished activity.
- S122 (= S124) mutation to A: Strongly reduced activity.
- K171 (= K174) active site
- N175 (≠ Q178) mutation to A: Strongly reduced activity.
- W214 (= W217) mutation to A: Almost abolished activity.
- Y219 (≠ R222) mutation to A: Strongly reduced activity.
Sites not aligning to the query:
- 246 binding ; K→A: Almost abolished activity.
- 247 D→A: Almost abolished activity.
3obbA Crystal structure of a possible 3-hydroxyisobutyrate dehydrogenase from pseudomonas aeruginosa pao1 (see paper)
35% identity, 75% coverage: 5:224/295 of query aligns to 2:220/295 of 3obbA
Sites not aligning to the query:
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
33% identity, 96% coverage: 7:289/295 of query aligns to 3:288/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (≠ V150), E148 (≠ Q154), A151 (≠ G157), K153 (= K159)
- binding nicotinamide-adenine-dinucleotide: G7 (= G11), G9 (= G13), N10 (≠ S14), M11 (= M15), F29 (= F33), D30 (= D34), P31 (≠ V35), M63 (= M67), L64 (≠ V68), G120 (= G126), L239 (vs. gap), K242 (= K242)
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
33% identity, 96% coverage: 7:289/295 of query aligns to 3:288/292 of 5y8iA
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
33% identity, 96% coverage: 7:289/295 of query aligns to 4:289/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (≠ A134), E149 (≠ Q154), A152 (≠ G157), G153 (≠ D158), G153 (≠ D158), K154 (= K159)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S124), G120 (= G125), W211 (= W217), F236 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: G8 (= G11), G10 (= G13), N11 (≠ S14), M12 (= M15), F30 (= F33), D31 (= D34), P32 (≠ V35), M64 (= M67), L65 (≠ V68), T93 (≠ L95), G121 (= G126), K168 (= K174), L240 (vs. gap), K243 (= K242)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
33% identity, 96% coverage: 7:289/295 of query aligns to 4:289/290 of 5y8kA
Query Sequence
>SMc00274 FitnessBrowser__Smeli:SMc00274
MNDKKRVAFVGLGSMGLPMAENLIRAGHAVRGFDVRAAAMETLAATGGIRSANPAEACSG
ADVLVLMVVNAEQARSVLLESGALSSLPQGAHICLMATCPPDEVKRLADEVEASGRVLVD
CPVSGGVVGAKAGALTIMVGAPEKAYHAVVPVLQAMGDKVFHCGPEQGQGAVVKAINQLL
CGVHLATAAEALALGEKAGVDAATLLEIVSNSAASSWMLKDRGPRMITKTPPVTSAVDIF
VKDLGIALATGRSVSMALPLAAAAHQMFLAESGSGNGLEDDSQVIAAYRRLNGIT
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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