SitesBLAST
Comparing HSERO_RS15390 FitnessBrowser__HerbieS:HSERO_RS15390 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)
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)
57% identity, 99% coverage: 4:297/297 of query aligns to 3:296/298 of Q9I5I6
- P66 (= P67) binding
- T96 (= T97) binding ; mutation to A: Almost abolished activity.
- S122 (= S123) mutation to A: Strongly reduced activity.
- K171 (= K172) active site
- N175 (= N176) mutation to A: Strongly reduced activity.
- W214 (= W215) mutation to A: Almost abolished activity.
- Y219 (= Y220) mutation to A: Strongly reduced activity.
- K246 (= K247) binding ; mutation to A: Almost abolished activity.
- D247 (= D248) 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)
57% identity, 99% coverage: 4:297/297 of query aligns to 2:294/294 of 3q3cA
- binding nicotinamide-adenine-dinucleotide: G9 (= G11), H10 (≠ N12), M11 (= M13), F29 (≠ H31), D30 (= D32), L31 (= L33), M63 (= M65), L64 (= L66), P65 (= P67), T94 (= T97), V119 (= V122), G121 (= G124), F237 (= F240), K244 (= K247)
3obbA Crystal structure of a possible 3-hydroxyisobutyrate dehydrogenase from pseudomonas aeruginosa pao1 (see paper)
57% identity, 99% coverage: 4:297/297 of query aligns to 3:295/295 of 3obbA
P29266 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Rattus norvegicus (Rat) (see paper)
46% identity, 98% coverage: 7:297/297 of query aligns to 43:333/335 of P29266
- D68 (= D32) mutation to R: Decrease of activity with NAD, increase of activity with NADP.
- K208 (= K172) mutation K->A,H,N,R: Complete loss of activity.
- N212 (= N176) mutation to Q: Decrease in activity.
2i9pB Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+
45% identity, 98% coverage: 7:297/297 of query aligns to 5:295/296 of 2i9pB
- binding nicotinamide-adenine-dinucleotide: G9 (= G11), N10 (= N12), M11 (= M13), Y29 (≠ H31), D30 (= D32), V31 (≠ L33), M63 (= M65), L64 (= L66), P65 (= P67), T95 (= T97), V120 (= V122), G122 (= G124), F238 (= F240), K245 (= K247)
P31937 3-hydroxyisobutyrate dehydrogenase, mitochondrial; HIBADH; EC 1.1.1.31 from Homo sapiens (Human) (see paper)
45% identity, 98% coverage: 7:297/297 of query aligns to 44:334/336 of P31937
- LP 103:104 (= LP 66:67) binding
- N108 (≠ H71) binding
- T134 (= T97) binding
- K284 (= K247) binding
Sites not aligning to the query:
- 1:36 modified: transit peptide, Mitochondrion
- 40:68 binding
5y8hA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD+ (see paper)
42% identity, 98% coverage: 4:293/297 of query aligns to 2:287/291 of 5y8hA
- binding (2~{S})-2-methylpentanedioic acid: R144 (≠ Q149), E148 (≠ Q153), A151 (≠ G156), K153 (≠ A158)
- binding nicotinamide-adenine-dinucleotide: G7 (= G9), G9 (= G11), N10 (= N12), M11 (= M13), F29 (≠ H31), D30 (= D32), P31 (≠ L33), M63 (= M65), L64 (= L66), G120 (= G125), L239 (= L244), K242 (= K247)
5y8iA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + (s)-3-hydroxyisobutyrate (s-hiba) (see paper)
42% identity, 98% coverage: 4:293/297 of query aligns to 2:287/292 of 5y8iA
5y8lB Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + NAD +(s)-3-hydroxyisobutyrate (s-hiba) (see paper)
42% identity, 98% coverage: 4:293/297 of query aligns to 3:288/290 of 5y8lB
- binding (2~{S})-2-methylpentanedioic acid: T129 (= T133), E149 (≠ Q153), A152 (≠ G156), G153 (≠ K157), G153 (≠ K157), K154 (≠ A158)
- binding (2S)-2-methyl-3-oxidanyl-propanoic acid: S119 (= S123), G120 (= G124), W211 (= W215), F236 (= F240)
- binding nicotinamide-adenine-dinucleotide: G8 (= G9), G10 (= G11), N11 (= N12), M12 (= M13), F30 (≠ H31), D31 (= D32), P32 (≠ L33), M64 (= M65), L65 (= L66), T93 (= T97), G121 (= G125), K168 (= K172), L240 (= L244), K243 (= K247)
5y8kA Mycobacterium tuberculosis 3-hydroxyisobutyrate dehydrogenase (mthibadh) + l-serine (see paper)
42% identity, 98% coverage: 4:293/297 of query aligns to 3:288/290 of 5y8kA
5je8B The crystal structure of bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD (see paper)
38% identity, 96% coverage: 7:290/297 of query aligns to 8:286/294 of 5je8B
3w6zA Crystal structure of NADP bound l-serine 3-dehydrogenase (k170m) from hyperthermophilic archaeon pyrobaculum calidifontis (see paper)
35% identity, 95% coverage: 7:289/297 of query aligns to 18:293/296 of 3w6zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G9), L21 (= L10), G22 (= G11), I23 (≠ N12), M24 (= M13), N43 (≠ D32), R44 (≠ L33), T45 (≠ V34), K48 (≠ S37), V77 (≠ L66), S78 (≠ P67), D82 (≠ H71), Q85 (≠ S74), V133 (= V122), F244 (= F240), K245 (≠ G241), H248 (≠ L244), K251 (= K247)
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)
36% identity, 95% coverage: 7:289/297 of query aligns to 18:290/293 of 3ws7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G9), L21 (= L10), G22 (= G11), I23 (≠ N12), M24 (= M13), N43 (≠ D32), R44 (≠ L33), T45 (≠ V34), K48 (≠ S37), M76 (= M65), V77 (≠ L66), S78 (≠ P67), D82 (≠ H71), Q85 (≠ S74), V133 (= V122), F241 (= F240), K242 (≠ G241), H245 (≠ L244), K248 (= K247)
- binding sulfate ion: T134 (≠ S123), G135 (= G124), K183 (= K172)
6smyA Crystal structure of sla reductase yihu from e. Coli with nadh and product dhps
34% identity, 98% coverage: 3:293/297 of query aligns to 1:285/294 of 6smyA
6smzC Crystal structure of sla reductase yihu from e. Coli in complex with nadh
34% identity, 98% coverage: 3:293/297 of query aligns to 1:285/295 of 6smzC
- binding nicotinamide-adenine-dinucleotide: G9 (= G11), Q10 (≠ N12), M11 (= M13), F29 (≠ H31), D30 (= D32), V31 (≠ L33), M63 (= M65), L64 (= L66), V73 (≠ L75), S94 (= S96), T95 (= T97), R122 (≠ G124)
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)
35% identity, 97% coverage: 3:290/297 of query aligns to 2:283/298 of P0A9V8
- QM 11:12 (≠ NM 12:13) binding
- D31 (= D32) binding
- L65 (= L66) binding
- T96 (= T97) binding
- G122 (≠ S123) mutation to S: 25-fold decrease in catalytic efficiency with SLA as substrate. 5-fold decrease in catalytic efficiency with NADH as substrate.
- R123 (≠ G124) 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 (≠ G125) 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 (≠ NNMLL 175:179) binding
- K240 (= K247) binding
2cvzC Structure of hydroxyisobutyrate dehydrogenase from thermus thermophilus hb8 (see paper)
33% identity, 92% coverage: 4:275/297 of query aligns to 3:262/289 of 2cvzC
- active site: S117 (= S123), K165 (= K172), N168 (= N175), N169 (= N176)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), L9 (= L10), G10 (= G11), A11 (≠ N12), M12 (= M13), N30 (≠ H31), R31 (≠ D32), T32 (≠ L33), C62 (≠ M65), L63 (= L66), P64 (= P67), E68 (≠ H71), E71 (vs. gap), S91 (≠ T97), V116 (= V122), F227 (= F240), K234 (= K247)
1wp4A Structure of tt368 protein from thermus thermophilus hb8 (see paper)
33% identity, 92% coverage: 4:275/297 of query aligns to 2:261/288 of 1wp4A
- active site: S116 (= S123), K164 (= K172), N167 (= N175), N168 (= N176)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G9), L8 (= L10), G9 (= G11), A10 (≠ N12), M11 (= M13), N29 (≠ H31), R30 (≠ D32), T31 (≠ L33), K34 (≠ A36), C61 (≠ M65), L62 (= L66), P63 (= P67), E67 (≠ H71), S90 (≠ T97), V115 (= V122), T225 (≠ G239), F226 (= F240), K233 (= K247)
- binding sulfate ion: S116 (= S123), G117 (= G124), G118 (= G125), K164 (= K172)
3pefA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter metallireducens in complex with NADP+ (see paper)
32% identity, 98% coverage: 2:291/297 of query aligns to 1:283/287 of 3pefA
- binding glycerol: D67 (≠ A68), G123 (= G124), K171 (= K172), N175 (= N176), M178 (≠ L179), L203 (≠ S204), G207 (≠ S208), N213 (= N221), A217 (≠ G225), F232 (= F240), H236 (≠ L244), K239 (= K247), R242 (≠ G250), R269 (≠ S277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G11), I11 (≠ N12), M12 (= M13), N31 (≠ D32), R32 (≠ L33), S33 (≠ V34), K36 (≠ S37), M64 (= M65), L65 (= L66), A66 (≠ P67), A70 (≠ H71), E73 (≠ S74), T96 (= T97), V121 (= V122), G123 (= G124), S124 (≠ G125), A231 (≠ G239), F232 (= F240), H236 (≠ L244), K239 (= K247)
3pduA Crystal structure of gamma-hydroxybutyrate dehydrogenase from geobacter sulfurreducens in complex with NADP+ (see paper)
33% identity, 97% coverage: 7:293/297 of query aligns to 6:285/287 of 3pduA
- binding glycerol: R242 (≠ G250), E246 (= E254), E246 (= E254), R250 (≠ N260)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), G10 (= G11), I11 (≠ N12), M12 (= M13), N31 (≠ D32), R32 (≠ L33), N33 (≠ V34), M64 (= M65), L65 (= L66), A66 (≠ P67), A70 (≠ H71), T96 (= T97), V121 (= V122), G123 (= G124), T124 (≠ G125), K171 (= K172), S231 (≠ G239), F232 (= F240), P233 (≠ G241), H236 (≠ L244), K239 (= K247)
Query Sequence
>HSERO_RS15390 FitnessBrowser__HerbieS:HSERO_RS15390
MSANIVFIGLGNMGLPMAQNLVKAGFSVSGHDLVKASVDKLVEVGGKTEADSMAAVAKAD
VVITMLPASRHVESLYLGEAGVLASAKPGTLLIDCSTIAPEAARKVAAAAKARGFEMLDA
PVSGGTNGATAGTLTFMVGGSKEAFEAAQPYLQKMGKAIYHAGESGSGQTVKVCNNMLLG
ILMIGTSEAIRLGMANGMDPKVLSEIMSKSSGRNWTLEVYNPCPGVMETAPASKGYAGGF
GVDLMLKDLGLAVENALATNCAIPLGATARNLYDIHSMNGAGKLDFSSIFNMLGKAQ
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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