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Comparing BPHYT_RS27640 FitnessBrowser__BFirm:BPHYT_RS27640 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)
5vt6A Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b complexed with NADP
77% identity, 98% coverage: 4:247/248 of query aligns to 1:244/245 of 5vt6A
- active site: G12 (= G15), D102 (= D105), S138 (= S141), Y151 (= Y154), K155 (= K158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), G11 (= G14), G12 (= G15), L13 (= L16), H32 (= H35), S33 (= S36), N36 (= N39), V58 (≠ A61), D59 (= D62), V60 (= V63), N86 (= N89), A87 (= A90), G88 (= G91), I89 (= I92), I136 (= I139), Y151 (= Y154), K155 (= K158), P181 (= P184), Y183 (= Y186), L184 (= L187), T186 (= T189)
4k6fB X-ray crystal structure of a putative acetoacetyl-coa reductase from burkholderia cenocepacia bound to the co-factor NADP
63% identity, 98% coverage: 4:247/248 of query aligns to 1:244/245 of 4k6fB
- active site: G12 (= G15), N102 (≠ D105), S138 (= S141), Y151 (= Y154), K155 (= K158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), Y32 (≠ H35), S33 (= S36), N36 (= N39), V58 (≠ A61), D59 (= D62), V60 (= V63), A87 (= A90), G88 (= G91), I89 (= I92)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
52% identity, 99% coverage: 3:248/248 of query aligns to 1:245/245 of 5vmlA
- active site: G13 (= G15), N111 (≠ D113), S139 (= S141), Y152 (= Y154), K156 (= K158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G11), G12 (= G14), G13 (= G15), I14 (≠ L16), C33 (≠ H35), G34 (≠ S36), R39 (≠ H41), G59 (≠ A61), N60 (≠ D62), V61 (= V63), N87 (= N89), G89 (= G91), I90 (= I92), S139 (= S141), Y152 (= Y154), K156 (= K158), P182 (= P184), G183 (= G185), I185 (≠ L187)
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
51% identity, 100% coverage: 2:248/248 of query aligns to 4:249/249 of 3vzsB
- active site: N115 (≠ D113), S143 (= S141), Y156 (= Y154), K160 (= K158)
- binding acetoacetyl-coenzyme a: D97 (= D95), Q150 (≠ A148), F151 (= F149), Q153 (= Q151), Y156 (= Y154), G187 (= G185), Y188 (= Y186), R198 (≠ P196)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G11), I18 (≠ L16), G38 (≠ S36), R43 (≠ H41), G63 (≠ A61), N64 (≠ D62), V65 (= V63), G93 (= G91), I94 (= I92), T95 (≠ A93), P186 (= P184), I189 (≠ L187), M193 (= M191), V194 (≠ T192)
P14697 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) (see 2 papers)
51% identity, 99% coverage: 4:248/248 of query aligns to 3:246/246 of P14697
- GGI 13:15 (≠ GGL 14:16) binding
- G35 (≠ S36) binding
- R40 (≠ H41) binding
- Q47 (≠ H48) mutation to L: 2.4-fold increase in activity. 2-fold decrease in affinity for NADPH and 2.8-fold decrease in affinity for acetoacetyl-CoA.
- GNV 60:62 (≠ ADV 61:63) binding
- NAGIT 88:92 (≠ NAGIA 89:93) binding
- D94 (= D95) mutation to A: About 6% of wild-type activity.
- K99 (= K100) mutation to A: Nearly loss of activity.
- Q147 (≠ A148) mutation to A: About 30% of wild-type activity.
- F148 (= F149) mutation to A: About 30% of wild-type activity.
- Q150 (= Q151) mutation to A: About 20% of wild-type activity.
- T173 (≠ K174) mutation to S: 3.5-fold increase in activity. 4-fold decrease in affinity for NADPH and 2.4-fold decrease in affinity for acetoacetyl-CoA.
- PGYI 183:186 (≠ PGYL 184:187) binding
- Y185 (= Y186) mutation to A: Nearly loss of activity.
- R195 (≠ P196) mutation to A: Nearly loss of activity.
3op4A Crystal structure of putative 3-ketoacyl-(acyl-carrier-protein) reductase from vibrio cholerae o1 biovar eltor str. N16961 in complex with NADP+ (see paper)
43% identity, 98% coverage: 5:247/248 of query aligns to 9:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G11), S17 (≠ M13), R18 (≠ G14), I20 (≠ L16), T40 (≠ H35), N62 (≠ H57), V63 (= V63), N89 (= N89), A90 (= A90), I92 (= I92), V139 (≠ I139), S141 (= S141), Y154 (= Y154), K158 (= K158), P184 (= P184), G185 (= G185), I187 (≠ L187), T189 (= T189), M191 (= M191)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
42% identity, 98% coverage: 5:247/248 of query aligns to 9:242/243 of 4i08A
- active site: G19 (= G15), N113 (≠ D113), S141 (= S141), Q151 (= Q151), Y154 (= Y154), K158 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G11), S17 (≠ M13), R18 (≠ G14), I20 (≠ L16), T40 (≠ H35), N62 (≠ H57), V63 (= V63), N89 (= N89), A90 (= A90), G140 (≠ A140), S141 (= S141), Y154 (= Y154), K158 (= K158), P184 (= P184), G185 (= G185), T189 (= T189)
4ag3A Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with NADPH at 1.8a resolution (see paper)
43% identity, 98% coverage: 5:247/248 of query aligns to 13:253/254 of 4ag3A
- active site: G23 (= G15), S148 (= S141), Y161 (= Y154), K165 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G11), S21 (≠ M13), R22 (≠ G14), G23 (= G15), I24 (≠ L16), T44 (≠ S36), L68 (≠ A61), D69 (= D62), V70 (= V63), N96 (= N89), A97 (= A90), I146 (= I139), S148 (= S141), Y161 (= Y154), K165 (= K158), P191 (= P184), G192 (= G185), F193 (≠ Y186), I194 (≠ L187), T196 (= T189), M198 (= M191), T199 (= T192)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
41% identity, 98% coverage: 5:247/248 of query aligns to 6:243/244 of 6t77A
- active site: G16 (= G15), S138 (= S141), Y151 (= Y154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G11), S14 (≠ M13), R15 (≠ G14), T37 (≠ H35), L58 (≠ F56), N59 (≠ D62), V60 (= V63), A87 (= A90), G88 (= G91), I89 (= I92)
P0A2C9 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
41% identity, 98% coverage: 5:247/248 of query aligns to 6:243/244 of P0A2C9
- M125 (= M128) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (≠ C227) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S228) mutation to F: Distorts the local conformation and prevent stacking around Phe-221. The S224F mutation would additionally disrupt the hydrogen bond formed between Ser-224 and Glu-226.
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
39% identity, 100% coverage: 1:247/248 of query aligns to 1:246/246 of 3osuA
P0AEK2 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Escherichia coli (strain K12) (see 2 papers)
41% identity, 98% coverage: 5:247/248 of query aligns to 6:243/244 of P0AEK2
- GASR 12:15 (≠ GGMG 11:14) binding
- T37 (≠ H35) binding
- NV 59:60 (≠ DV 62:63) binding
- N86 (= N89) binding
- Y151 (= Y154) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (= YAAAK 154:158) binding
- A154 (= A157) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K158) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ L187) binding
- E233 (≠ A237) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
41% identity, 98% coverage: 5:247/248 of query aligns to 5:242/243 of 1q7bA
- active site: G15 (= G15), E101 (≠ D105), S137 (= S141), Q147 (= Q151), Y150 (= Y154), K154 (= K158)
- binding calcium ion: E232 (≠ A237), T233 (≠ N238)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G11), S13 (≠ M13), R14 (≠ G14), T36 (≠ H35), N58 (≠ D62), V59 (= V63), N85 (= N89), A86 (= A90), G87 (= G91), I88 (= I92), S137 (= S141), Y150 (= Y154), K154 (= K158), P180 (= P184), G181 (= G185), I183 (≠ L187)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
40% identity, 98% coverage: 5:247/248 of query aligns to 5:242/243 of 1q7cA
- active site: G15 (= G15), S137 (= S141), Q147 (= Q151), F150 (≠ Y154), K154 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G11), S13 (≠ M13), R14 (≠ G14), A35 (≠ H35), T36 (≠ S36), L57 (≠ A61), N58 (≠ D62), V59 (= V63), G87 (= G91), I88 (= I92)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
41% identity, 98% coverage: 5:247/248 of query aligns to 5:242/243 of 7emgB
6wprA Crystal structure of a putative 3-oxoacyl-acp reductase (fabg) with NADP(h) from acinetobacter baumannii (see paper)
40% identity, 98% coverage: 4:247/248 of query aligns to 5:243/244 of 6wprA
- active site: G16 (= G15), S138 (= S141), Y151 (= Y154)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G11), S14 (≠ M13), R15 (≠ G14), T37 (≠ H35), L58 (≠ F56), D59 (= D62), V60 (= V63), N86 (= N89), A87 (= A90), G88 (= G91), I89 (= I92), I136 (= I139), Y151 (= Y154), K155 (= K158), P181 (= P184)
6t62A Crystal structure of acinetobacter baumannii fabg in complex with NADPH at 1.8 a resolution (see paper)
40% identity, 98% coverage: 4:247/248 of query aligns to 5:243/244 of 6t62A
- active site: G16 (= G15), S138 (= S141), Y151 (= Y154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G11), S14 (≠ M13), R15 (≠ G14), A36 (≠ S34), T37 (≠ H35), L58 (≠ F56), D59 (= D62), V60 (= V63), N86 (= N89), A87 (= A90), G88 (= G91), I89 (= I92), I136 (= I139), S137 (≠ A140), S138 (= S141), Y151 (= Y154), K155 (= K158), P181 (= P184), G182 (= G185), I184 (≠ L187), M188 (= M191)
4bo4C Crystal structure of 3-oxoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with n-(2-methoxyphenyl)-3,4- dihydro-2h-quinoline-1-carboxamide at 2.7a resolution (see paper)
42% identity, 98% coverage: 5:247/248 of query aligns to 19:254/255 of 4bo4C
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
38% identity, 98% coverage: 5:247/248 of query aligns to 2:239/239 of 3sj7A
- active site: G12 (= G15), S138 (= S141), Q148 (= Q151), Y151 (= Y154), K155 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), S10 (≠ M13), R11 (≠ G14), I13 (≠ L16), N31 (≠ S34), Y32 (≠ H35), A33 (≠ S36), G34 (≠ E37), S35 (≠ R38), A58 (= A61), N59 (≠ D62), V60 (= V63), N86 (= N89), A87 (= A90), T109 (= T112), S138 (= S141), Y151 (= Y154), K155 (= K158), P181 (= P184), G182 (= G185)
4bnzA Crystal structure of 3-oxoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with 1-methyl-n-phenylindole- 3-carboxamide at 2.5a resolution (see paper)
42% identity, 98% coverage: 5:247/248 of query aligns to 8:240/241 of 4bnzA
Query Sequence
>BPHYT_RS27640 FitnessBrowser__BFirm:BPHYT_RS27640
MSAKRVAFITGGMGGLGAAVSRRLHDAGMVVAMSHSERNDHVATWLMHERDAGRRFHAYE
ADVTSFDSCAHCAARVLDEFGSVDVLVNNAGIARDSTFAKMSKDDWDAVLRTDLDSMFNM
TKPLLGSMVAQRFGRIVNIASVNGARGAFGQTNYAAAKAGIHGFTMSLALEVAKHGVTVN
TVSPGYLATAMTAAVPKEVMETKILPQIPVGRLGQPDEVAALVAFLCSDDAAFVTGANFA
INGGMHMG
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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