SitesBLAST
Comparing GFF2390 FitnessBrowser__psRCH2:GFF2390 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)
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
52% identity, 100% coverage: 1:295/296 of query aligns to 1:294/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), N10 (= N10), M11 (= M11), Y29 (≠ F29), D30 (= D30), V31 (≠ L31), M63 (= M64), L64 (= L65), P65 (= P66), T95 (= T96), V120 (= V121), G122 (= G123), F238 (= F239), K245 (= K246)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
52% identity, 99% coverage: 3:295/296 of query aligns to 42:333/336 of P31937
- LP 103:104 (= LP 65:66) binding
- N108 (≠ H70) binding
- T134 (= T96) binding
- K284 (= K246) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
- 40:68 binding
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
51% identity, 99% coverage: 3:295/296 of query aligns to 41:332/335 of P29266
- D68 (= D30) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K171) mutation K->A,H,N,R: Complete loss of activity.
- N212 (= N175) mutation to Q: Decrease in activity.
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)
56% identity, 97% coverage: 2:288/296 of query aligns to 3:288/298 of Q9I5I6
- P66 (= P66) binding
- T96 (= T96) binding ; mutation to A: Almost abolished activity.
- S122 (= S122) mutation to A: Strongly reduced activity.
- K171 (= K171) active site
- N175 (= N175) mutation to A: Strongly reduced activity.
- W214 (= W214) mutation to A: Almost abolished activity.
- Y219 (= Y219) mutation to A: Strongly reduced activity.
- K246 (= K246) binding ; mutation to A: Almost abolished activity.
- D247 (= D247) mutation to A: Almost abolished activity.
Sites not aligning to the query:
3q3cA Crystal structure of a serine dehydrogenase from pseudomonas aeruginosa pao1 in complex with NAD (see paper)
56% identity, 97% coverage: 2:288/296 of query aligns to 2:286/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), H10 (≠ N10), M11 (= M11), F29 (= F29), D30 (= D30), L31 (= L31), M63 (= M64), L64 (= L65), P65 (= P66), T94 (= T96), V119 (= V121), G121 (= G123), F237 (= F239), K244 (= K246)
3obbA Crystal structure of a possible 3-hydroxyisobutyrate dehydrogenase from pseudomonas aeruginosa pao1 (see paper)
56% identity, 97% coverage: 2:288/296 of query aligns to 3:287/295 of 3obbA
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
45% identity, 98% coverage: 3:293/296 of query aligns to 3:288/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (≠ Q148), E148 (≠ A152), A151 (≠ G155), K153 (≠ N157)
- binding nicotinamide-adenine-dinucleotide: G7 (= G7), G9 (= G9), N10 (= N10), M11 (= M11), F29 (= F29), D30 (= D30), P31 (≠ L31), M63 (= M64), L64 (= L65), G120 (= G124), L239 (= L243), K242 (= K246)
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
45% identity, 98% coverage: 3:293/296 of query aligns to 4:289/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (= T132), E149 (≠ A152), A152 (≠ G155), G153 (≠ K156), G153 (≠ K156), K154 (≠ N157)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S122), G120 (= G123), W211 (= W214), F236 (= F239)
- binding nicotinamide-adenine-dinucleotide: G8 (= G7), G10 (= G9), N11 (= N10), M12 (= M11), F30 (= F29), D31 (= D30), P32 (≠ L31), M64 (= M64), L65 (= L65), T93 (= T96), G121 (= G124), K168 (= K171), L240 (= L243), K243 (= K246)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
45% identity, 98% coverage: 3:293/296 of query aligns to 4:289/290 of 5y8kA
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
45% identity, 98% coverage: 3:293/296 of query aligns to 3:288/292 of 5y8iA
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
35% identity, 97% coverage: 1:288/296 of query aligns to 14:293/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G7), L21 (= L8), G22 (= G9), I23 (≠ N10), M24 (= M11), N43 (≠ D30), R44 (≠ L31), T45 (≠ N32), K48 (≠ A35), V77 (≠ L65), S78 (≠ P66), D82 (≠ H70), Q85 (≠ G73), V133 (= V121), F244 (= F239), K245 (≠ G240), H248 (≠ L243), K251 (= K246)
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
38% identity, 98% coverage: 3:293/296 of query aligns to 3:286/294 of 6smyA
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
38% identity, 98% coverage: 3:293/296 of query aligns to 3:286/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), Q10 (≠ N10), M11 (= M11), F29 (= F29), D30 (= D30), V31 (≠ L31), M63 (= M64), L64 (= L65), V73 (= V74), S94 (= S95), T95 (= T96), R122 (≠ G123)
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)
38% identity, 98% coverage: 3:293/296 of query aligns to 4:287/298 of P0A9V8
- QM 11:12 (≠ NM 10:11) binding
- D31 (= D30) binding
- L65 (= L65) binding
- T96 (= T96) binding
- G122 (≠ S122) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G123) 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 (≠ G124) 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 (≠ NN-ML 174:177) binding
- K240 (= K246) binding
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)
35% identity, 97% coverage: 1:288/296 of query aligns to 14:290/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G7), L21 (= L8), G22 (= G9), I23 (≠ N10), M24 (= M11), N43 (≠ D30), R44 (≠ L31), T45 (≠ N32), K48 (≠ A35), M76 (= M64), V77 (≠ L65), S78 (≠ P66), D82 (≠ H70), Q85 (≠ G73), V133 (= V121), F241 (= F239), K242 (≠ G240), H245 (≠ L243), K248 (= K246)
- binding sulfate ion: T134 (≠ S122), G135 (= G123), K183 (= K171)
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
34% identity, 99% coverage: 2:294/296 of query aligns to 5:288/294 of 5je8B
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
32% identity, 99% coverage: 2:294/296 of query aligns to 3:287/287 of 3pefA
- binding glycerol: D67 (≠ A67), G123 (= G123), K171 (= K171), N175 (= N175), M178 (≠ L178), L203 (≠ A203), G207 (≠ N207), N213 (= N220), A217 (≠ G224), F232 (= F239), H236 (≠ L243), K239 (= K246), R242 (≠ G249), R269 (≠ S276)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G9), I11 (≠ N10), M12 (= M11), N31 (≠ D30), R32 (≠ L31), S33 (≠ N32), K36 (≠ A35), M64 (= M64), L65 (= L65), A66 (≠ P66), A70 (≠ H70), E73 (≠ G73), T96 (= T96), V121 (= V121), G123 (= G123), S124 (≠ G124), A231 (≠ G238), F232 (= F239), H236 (≠ L243), K239 (= K246)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
33% identity, 97% coverage: 4:290/296 of query aligns to 5:283/287 of 3pduA
- binding glycerol: R242 (≠ G249), E246 (= E253), E246 (= E253), R250 (≠ Q257)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G7), G10 (= G9), I11 (≠ N10), M12 (= M11), N31 (≠ D30), R32 (≠ L31), N33 (= N32), M64 (= M64), L65 (= L65), A66 (≠ P66), A70 (≠ H70), T96 (= T96), V121 (= V121), G123 (= G123), T124 (≠ G124), K171 (= K171), S231 (≠ G238), F232 (= F239), P233 (≠ G240), H236 (≠ L243), K239 (= K246)
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
35% identity, 92% coverage: 2:273/296 of query aligns to 3:261/289 of 2cvzC
- active site: S117 (= S122), K165 (= K171), N168 (= N174), N169 (= N175)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G7), L9 (= L8), G10 (= G9), A11 (≠ N10), M12 (= M11), N30 (vs. gap), R31 (≠ S27), T32 (≠ V28), C62 (≠ M64), L63 (= L65), P64 (= P66), E68 (≠ G73), E71 (≠ L76), S91 (≠ T96), V116 (= V121), F227 (= F239), K234 (= K246)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
35% identity, 92% coverage: 2:273/296 of query aligns to 2:260/288 of 1wp4A
- active site: S116 (= S122), K164 (= K171), N167 (= N174), N168 (= N175)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G7), L8 (= L8), G9 (= G9), A10 (≠ N10), M11 (= M11), N29 (vs. gap), R30 (≠ S27), T31 (≠ V28), K34 (≠ N32), C61 (≠ M64), L62 (= L65), P63 (= P66), E67 (≠ G73), S90 (≠ T96), V115 (= V121), T225 (≠ G238), F226 (= F239), K233 (= K246)
- binding sulfate ion: S116 (= S122), G117 (= G123), G118 (= G124), K164 (= K171)
Query Sequence
>GFF2390 FitnessBrowser__psRCH2:GFF2390
MHIGFIGLGNMGAPMAHNLLKAGHQLSVFDLNAAAVENLVGAGALPVDSPTAIAQGNAEL
IITMLPAAAHVKGVYLGVNGLIAHSRAGVMLIDCSTIDPHSAREVAKAAAEHGNPMLDAP
VSGGTGGAAAGTLTFMVGGSDPDFDHAQPILAAMGKNIVHCGAAGNGQVAKVANNMLLGI
SMIGVAEAMALGVALGMDAKTLAGVINTSSGRCWSSDTYNPFPGVLDNVPSSRGYSGGFG
SDLMLKDLGLATEAAKQVRQPVILGALAQQLYQSFSAQGHGGLDFSAIINQYRKDT
Or try a new SitesBLAST search
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