SitesBLAST
Comparing RR42_RS19860 FitnessBrowser__Cup4G11:RR42_RS19860 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)
40% identity, 91% coverage: 3:283/308 of query aligns to 12:286/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G11), L21 (= L12), G22 (= G13), I23 (= I14), M24 (= M15), N43 (≠ D34), R44 (vs. gap), T45 (≠ V35), K48 (≠ A38), V77 (= V67), S78 (≠ P68), D82 (≠ H72), Q85 (≠ A75), V133 (= V130), F244 (= F241), K245 (≠ R242), H248 (≠ L245), K251 (= K248)
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)
40% identity, 91% coverage: 3:283/308 of query aligns to 12:283/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G11), L21 (= L12), G22 (= G13), I23 (= I14), M24 (= M15), N43 (≠ D34), R44 (vs. gap), T45 (≠ V35), K48 (≠ A38), M76 (= M66), V77 (= V67), S78 (≠ P68), D82 (≠ H72), Q85 (≠ A75), V133 (= V130), F241 (= F241), K242 (≠ R242), H245 (≠ L245), K248 (= K248)
- binding sulfate ion: T134 (≠ S131), G135 (= G132), K183 (= K180)
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
31% identity, 94% coverage: 1:290/308 of query aligns to 35:325/335 of P29266
- D68 (= D34) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K180) mutation K->A,H,N,R: Complete loss of activity.
- N212 (≠ Q184) mutation to Q: Decrease in activity.
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
32% identity, 94% coverage: 1:290/308 of query aligns to 36:326/336 of P31937
- 40:68 (vs. 5:33, 52% identical) binding
- LP 103:104 (≠ VP 67:68) binding
- N108 (≠ H72) binding
- T134 (≠ S105) binding
- K284 (= K248) 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, 92% coverage: 7:290/308 of query aligns to 3:287/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), N10 (≠ I14), M11 (= M15), Y29 (≠ H33), D30 (= D34), V31 (= V35), M63 (= M66), L64 (≠ V67), P65 (= P68), T95 (≠ S105), V120 (= V130), G122 (= G132), F238 (= F241), K245 (= K248)
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
30% identity, 94% coverage: 5:294/308 of query aligns to 4:289/294 of 5je8B
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)
33% identity, 94% coverage: 7:296/308 of query aligns to 4:288/298 of P0A9V8
- QM 11:12 (≠ IM 14:15) binding
- D31 (= D34) binding
- L65 (≠ V67) binding
- T96 (≠ S105) binding
- G122 (≠ S131) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G132) 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 (≠ G133) 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- 183:186) binding
- K240 (= K248) binding
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
33% identity, 94% coverage: 7:296/308 of query aligns to 3:287/294 of 6smyA
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
33% identity, 94% coverage: 7:296/308 of query aligns to 3:287/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), Q10 (≠ I14), M11 (= M15), F29 (≠ H33), D30 (= D34), V31 (= V35), M63 (= M66), L64 (≠ V67), V73 (= V76), S94 (= S104), T95 (≠ S105), R122 (≠ G132)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
32% identity, 94% coverage: 6:295/308 of query aligns to 3:286/287 of 3pduA
- binding glycerol: R242 (≠ N251), E246 (≠ Q255), E246 (≠ Q255), R250 (≠ A259)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), G10 (= G13), I11 (= I14), M12 (= M15), N31 (≠ D34), R32 (≠ V35), N33 (= N36), M64 (= M66), L65 (≠ V67), A66 (≠ P68), A70 (≠ H72), T96 (≠ S105), V121 (= V130), G123 (= G132), T124 (≠ G133), K171 (= K180), S231 (≠ G240), F232 (= F241), P233 (≠ R242), H236 (≠ L245), K239 (= K248)
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
30% identity, 95% coverage: 4:295/308 of query aligns to 1:286/287 of 3pefA
- binding glycerol: D67 (= D69), G123 (= G132), K171 (= K180), N175 (≠ Q184), M178 (≠ V187), L203 (≠ R212), G207 (≠ M216), N213 (≠ S222), A217 (≠ E226), F232 (= F241), H236 (≠ L245), K239 (= K248), R242 (≠ N251), R269 (≠ A278)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G13), I11 (= I14), M12 (= M15), N31 (≠ D34), R32 (≠ V35), S33 (≠ N36), K36 (≠ P39), M64 (= M66), L65 (≠ V67), A66 (≠ P68), A70 (≠ H72), E73 (≠ A75), T96 (≠ S105), V121 (= V130), G123 (= G132), S124 (≠ G133), A231 (≠ G240), F232 (= F241), H236 (≠ L245), K239 (= K248)
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)
34% identity, 81% coverage: 5:252/308 of query aligns to 2:250/298 of Q9I5I6
- 2:31 (vs. 5:34, 57% identical) binding
- P66 (= P68) binding
- T96 (≠ S105) binding ; mutation to A: Almost abolished activity.
- S122 (= S131) mutation to A: Strongly reduced activity.
- K171 (= K180) active site
- N175 (≠ Q184) mutation to A: Strongly reduced activity.
- W214 (≠ R223) mutation to A: Almost abolished activity.
- Y219 (≠ H228) mutation to A: Strongly reduced activity.
- K246 (= K248) binding ; mutation to A: Almost abolished activity.
- D247 (= D249) mutation to A: Almost abolished activity.
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
34% identity, 96% coverage: 6:302/308 of query aligns to 3:288/289 of 2cvzC
- active site: S117 (= S131), K165 (= K180), N168 (= N183), N169 (≠ Q184)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), L9 (= L12), G10 (= G13), A11 (≠ I14), M12 (= M15), N30 (≠ H33), R31 (≠ D34), T32 (≠ V35), C62 (≠ M66), L63 (≠ V67), P64 (= P68), E68 (≠ H72), E71 (≠ A75), S91 (= S105), V116 (= V130), F227 (= F241), K234 (= K248)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
34% identity, 96% coverage: 6:302/308 of query aligns to 2:287/288 of 1wp4A
- active site: S116 (= S131), K164 (= K180), N167 (= N183), N168 (≠ Q184)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G11), L8 (= L12), G9 (= G13), A10 (≠ I14), M11 (= M15), N29 (≠ H33), R30 (≠ D34), T31 (≠ V35), K34 (≠ A38), C61 (≠ M66), L62 (≠ V67), P63 (= P68), E67 (≠ H72), S90 (= S105), V115 (= V130), T225 (≠ G240), F226 (= F241), K233 (= K248)
- binding sulfate ion: S116 (= S131), G117 (= G132), G118 (= G133), K164 (= K180)
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
35% identity, 81% coverage: 5:252/308 of query aligns to 1:248/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), H10 (≠ I14), M11 (= M15), F29 (≠ H33), D30 (= D34), L31 (vs. gap), M63 (= M66), L64 (≠ V67), P65 (= P68), T94 (≠ S105), V119 (= V130), G121 (= G132), F237 (= F241), K244 (= K248)
3obbA Crystal structure of a possible 3-hydroxyisobutyrate dehydrogenase from pseudomonas aeruginosa pao1 (see paper)
34% identity, 81% coverage: 5:252/308 of query aligns to 2:249/295 of 3obbA
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
33% identity, 89% coverage: 6:280/308 of query aligns to 3:275/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (≠ S141), E149 (≠ D161), A152 (≠ G164), G153 (≠ K165), G153 (≠ K165), K154 (≠ N166)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S131), G120 (= G132), W211 (≠ L225), F236 (= F241)
- binding nicotinamide-adenine-dinucleotide: G8 (= G11), G10 (= G13), N11 (≠ I14), M12 (= M15), F30 (≠ V35), D31 (≠ N36), P32 (= P37), M64 (= M66), L65 (≠ V67), T93 (≠ S105), G121 (= G133), K168 (= K180), L240 (= L245), K243 (= K248)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
33% identity, 89% coverage: 6:280/308 of query aligns to 3:275/290 of 5y8kA
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
33% identity, 89% coverage: 6:280/308 of query aligns to 2:274/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (≠ K157), E148 (≠ D161), A151 (≠ G164), K153 (≠ N166)
- binding nicotinamide-adenine-dinucleotide: G7 (= G11), G9 (= G13), N10 (≠ I14), M11 (= M15), F29 (≠ V35), D30 (≠ N36), P31 (= P37), M63 (= M66), L64 (≠ V67), G120 (= G133), L239 (= L245), K242 (= K248)
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
33% identity, 89% coverage: 6:280/308 of query aligns to 2:274/292 of 5y8iA
Query Sequence
>RR42_RS19860 FitnessBrowser__Cup4G11:RR42_RS19860
MANQRNVGFIGLGIMGAPMAGHLRAAGHTLFVHDVNPAPQALVDAGVTVCTSAEEVAKRA
DIIVIMVPDTPHVEAVLFAEKGVAAALKGAGKQAAHGKIVVDMSSISPIATKDFAARVNK
LGAAYLDAPVSGGEVGAKAASLTIMVGGPQESFDEVKPLFDLLGKNVTLVGGNGDGQTTK
VANQIIVALNIQAVSEALLFASKAGADPARVRQALMGGFAASRILEVHGERMVKRTFDPG
FRIELHQKDLNLALQGAKALGVALPNTATAQELFNTCAANGLGKQDHSALCRAIEIMSNH
EIAKGGAK
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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