SitesBLAST
Comparing WP_045585723.1 NCBI__GCF_001305595.1:WP_045585723.1 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)
7krmC Putative fabg bound to nadh from acinetobacter baumannii
64% identity, 100% coverage: 1:249/249 of query aligns to 1:244/244 of 7krmC
- active site: G18 (= G18), S140 (= S140), Y155 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (= S15), G18 (= G18), I19 (= I19), D38 (= D38), L39 (= L39), A60 (≠ C60), N61 (≠ D61), V62 (= V62), N88 (= N88), V111 (= V111), S140 (= S140), Y155 (= Y155), K159 (= K159), I188 (= I188), T190 (= T190)
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)
40% identity, 100% coverage: 1:248/249 of query aligns to 4:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G12), S17 (≠ A14), R18 (= R17), I20 (= I19), T40 (≠ A44), N62 (≠ D61), V63 (= V62), N89 (= N88), A90 (= A89), I92 (= I91), V139 (≠ I138), S141 (= S140), Y154 (= Y155), K158 (= K159), P184 (= P185), G185 (= G186), I187 (= I188), T189 (= T190), M191 (≠ I192)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
40% identity, 100% coverage: 1:248/249 of query aligns to 4:242/243 of 4i08A
- active site: G19 (= G18), N113 (≠ S112), S141 (= S140), Q151 (≠ G152), Y154 (= Y155), K158 (= K159)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G12), S17 (≠ A14), R18 (= R17), I20 (= I19), T40 (≠ A44), N62 (≠ D61), V63 (= V62), N89 (= N88), A90 (= A89), G140 (≠ S139), S141 (= S140), Y154 (= Y155), K158 (= K159), P184 (= P185), G185 (= G186), T189 (= T190)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
40% identity, 98% coverage: 6:248/249 of query aligns to 5:242/243 of 7emgB
4nbuB Crystal structure of fabg from bacillus sp (see paper)
38% identity, 99% coverage: 3:248/249 of query aligns to 5:244/244 of 4nbuB
- active site: G18 (= G18), N111 (≠ S112), S139 (= S140), Q149 (≠ G152), Y152 (= Y155), K156 (= K159)
- binding acetoacetyl-coenzyme a: D93 (≠ P94), K98 (≠ D99), S139 (= S140), N146 (≠ G147), V147 (≠ F150), Q149 (≠ G152), Y152 (= Y155), F184 (≠ L187), M189 (≠ I192), K200 (≠ E204)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ S15), G18 (= G18), I19 (= I19), D38 (= D38), F39 (≠ L39), V59 (≠ C60), D60 (= D61), V61 (= V62), N87 (= N88), A88 (= A89), G89 (= G90), I90 (= I91), T137 (≠ I138), S139 (= S140), Y152 (= Y155), K156 (= K159), P182 (= P185), F184 (≠ L187), T185 (≠ I188), T187 (= T190), M189 (≠ I192)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
41% identity, 100% coverage: 1:248/249 of query aligns to 1:247/247 of 4jroC
- active site: G16 (= G18), S142 (= S140), Q152 (≠ G152), Y155 (= Y155), K159 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ A14), R15 (= R17), G16 (= G18), I17 (= I19), N35 (≠ D38), Y36 (≠ L39), N37 (≠ D40), G38 (= G41), S39 (≠ A42), N63 (≠ F58), V64 (≠ A59), N90 (= N88), A91 (= A89), I93 (= I91), I113 (≠ V111), S142 (= S140), Y155 (= Y155), K159 (= K159), P185 (= P185), I188 (= I188), T190 (= T190)
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)
38% identity, 100% coverage: 1:248/249 of query aligns to 1:243/244 of P0AEK2
- GAS--R 12:15 (≠ GAASRR 12:17) binding NADP(+)
- T37 (≠ L37) binding NADP(+)
- NV 59:60 (≠ DV 61:62) binding NADP(+)
- N86 (= N88) binding NADP(+)
- Y151 (= Y155) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YSAAK 155:159) binding NADP(+)
- A154 (= A158) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K159) mutation to A: Defect in the affinity for NADPH.
- I184 (= I188) binding NADP(+)
- E233 (≠ A238) 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)
39% identity, 98% coverage: 6:248/249 of query aligns to 5:242/243 of 1q7bA
- active site: G15 (= G18), E101 (≠ N104), S137 (= S140), Q147 (≠ G152), Y150 (= Y155), K154 (= K159)
- binding calcium ion: E232 (≠ A238), T233 (= T239)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G12), S13 (≠ A14), R14 (= R17), T36 (≠ L37), N58 (≠ D61), V59 (= V62), N85 (= N88), A86 (= A89), G87 (= G90), I88 (= I91), S137 (= S140), Y150 (= Y155), K154 (= K159), P180 (= P185), G181 (= G186), I183 (= I188)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
38% identity, 98% coverage: 6:248/249 of query aligns to 5:242/243 of 1q7cA
- active site: G15 (= G18), S137 (= S140), Q147 (≠ G152), F150 (≠ Y155), K154 (= K159)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G12), S13 (≠ A14), R14 (= R17), A35 (≠ I36), T36 (≠ L37), L57 (≠ C60), N58 (≠ D61), V59 (= V62), G87 (= G90), I88 (= I91)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
40% identity, 98% coverage: 6:248/249 of query aligns to 5:246/246 of 3osuA
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
38% identity, 100% coverage: 1:248/249 of query aligns to 1:243/244 of 6t77A
- active site: G16 (= G18), S138 (= S140), Y151 (= Y155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ A14), R15 (= R17), T37 (≠ A44), L58 (≠ C60), N59 (≠ D61), V60 (= V62), A87 (= A89), G88 (= G90), I89 (= I91)
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)
37% identity, 100% coverage: 1:248/249 of query aligns to 1:243/244 of P0A2C9
- M125 (= M127) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A228) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S229) 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.
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
39% identity, 98% coverage: 6:248/249 of query aligns to 2:239/239 of 3sj7A
- active site: G12 (= G18), S138 (= S140), Q148 (≠ G152), Y151 (= Y155), K155 (= K159)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), S10 (≠ A14), R11 (= R17), I13 (= I19), N31 (≠ L37), Y32 (≠ D38), A33 (≠ L39), G34 (≠ D40), S35 (≠ G41), A58 (≠ C60), N59 (≠ D61), V60 (= V62), N86 (= N88), A87 (= A89), T109 (≠ V111), S138 (= S140), Y151 (= Y155), K155 (= K159), P181 (= P185), G182 (= G186)
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
40% identity, 97% coverage: 3:244/249 of query aligns to 6:236/240 of P73826
- S134 (= S140) mutation to A: 12% enzymatic activity.
- Y147 (= Y155) mutation to A: No enzymatic activity.
- K151 (= K159) mutation to A: 5% enzymatic activity.
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
38% identity, 100% coverage: 1:248/249 of query aligns to 4:247/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G12), R18 (= R17), G19 (= G18), I20 (= I19), D39 (= D38), R40 (≠ L39), C63 (= C60), I65 (≠ V62), N91 (= N88), G93 (= G90), I94 (= I91), V114 (= V111), Y155 (= Y155), K159 (= K159), I188 (= I188), T190 (= T190), T193 (= T193)
C1DMX5 L-rhamnose 1-dehydrogenase (NAD(P)(+)); RhaDH; AvLRA1; EC 1.1.1.378 from Azotobacter vinelandii (strain DJ / ATCC BAA-1303) (see paper)
38% identity, 100% coverage: 1:249/249 of query aligns to 1:254/256 of C1DMX5
- G12 (= G12) binding NADP(+)
- S14 (≠ A14) binding NADP(+)
- R15 (= R17) binding NADP(+); mutation to T: Increases specificity toward NAD(+). Shows a strong decrease in catalytic efficiency with NADP(+).
- I17 (= I19) binding NADP(+)
- S37 (≠ L39) binding NADP(+); mutation to H: Increases specificity toward NAD(+). Shows a strong decrease in catalytic efficiency with NADP(+) and an increase in catalytic efficiency with NAD(+).
- D66 (= D61) binding NADP(+)
- A67 (≠ V62) binding NADP(+)
- N93 (= N88) binding NADP(+)
- F99 (≠ P94) mutation F->A,Y: Shows a strong decrease in catalytic efficiency with L-rhamnose, L-lyxose and L-mannose.
- S146 (= S140) binding beta-L-rhamnose
- S148 (= S142) binding beta-L-rhamnose
- Q156 (≠ G152) binding beta-L-rhamnose; mutation to A: Almost loss of activity with L-rhamnose as substrate.
- Y159 (= Y155) binding beta-L-rhamnose; binding NADP(+)
- K163 (= K159) binding NADP(+)
- T191 (≠ L187) binding beta-L-rhamnose; mutation to F: Retains 4% of wild-type activity with L-rhamnose as substrate.
- I192 (= I188) binding NADP(+)
- I196 (= I192) mutation to A: Shows a strong decrease in catalytic efficiency with L-rhamnose as substrate, but does not affect catalytic efficiency with L-lyxose and L-mannose.
- N197 (≠ T193) binding beta-L-rhamnose
- D200 (≠ K196) mutation to A: Retains 16% of wild-type activity with L-rhamnose as substrate.; mutation to H: Retains 22% of wild-type activity with L-rhamnose as substrate.
3tzcA Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg)(y155f) from vibrio cholerae (see paper)
39% identity, 99% coverage: 1:246/249 of query aligns to 4:223/224 of 3tzcA
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
39% identity, 98% coverage: 3:246/249 of query aligns to 3:237/239 of 4nbtA
- active site: G16 (= G18), S132 (= S140), Y145 (= Y155), K149 (= K159)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), K15 (≠ R17), G16 (= G18), L17 (≠ I19), D36 (= D38), L37 (= L39), L52 (≠ C60), N53 (≠ D61), V54 (= V62), N80 (= N88), A81 (= A89), G82 (= G90), I130 (= I138), S132 (= S140), Y145 (= Y155), K149 (= K159), P177 (= P185), G178 (= G186), I180 (= I188), T182 (= T190)
7do7A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NAD and l-rhamnose bound-form) (see paper)
38% identity, 100% coverage: 2:249/249 of query aligns to 2:254/256 of 7do7A
- active site: G16 (= G18), S146 (= S140), Y159 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), R15 (= R17), G16 (= G18), I17 (= I19), S37 (≠ L39), D66 (= D61), A67 (≠ V62), N93 (= N88), A94 (= A89), G95 (= G90), I96 (= I91), V144 (≠ I138), S145 (= S139), S146 (= S140), Y159 (= Y155), K163 (= K159), P189 (= P185), G190 (= G186), I192 (= I188), T194 (= T190), I196 (= I192)
- binding beta-L-rhamnopyranose: F99 (≠ P94), S146 (= S140), S148 (= S142), Q156 (≠ G152), Y159 (= Y155), N197 (≠ T193), D235 (≠ E230), M236 (≠ L231), R238 (≠ S233)
7b81A Crystal structure of azotobacter vinelandii l-rhamnose 1-dehydrogenase (NAD bound-form) (see paper)
38% identity, 100% coverage: 2:249/249 of query aligns to 2:254/256 of 7b81A
- active site: G16 (= G18), S146 (= S140), Y159 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S14 (≠ A14), R15 (= R17), I17 (= I19), D66 (= D61), A67 (≠ V62), N93 (= N88), A94 (= A89), G95 (= G90), I96 (= I91), T116 (≠ V111), V144 (≠ I138), S146 (= S140), Y159 (= Y155), K163 (= K159), P189 (= P185), G190 (= G186), I192 (= I188), T194 (= T190), I196 (= I192)
Query Sequence
>WP_045585723.1 NCBI__GCF_001305595.1:WP_045585723.1
MLLSNKVCVITGAASRRGIGKATARLFALHGGRAIILDLDGAQAAEAAAELGEAHRGFAC
DVTDRDACFAAATRVVEEFGRIDVLVNNAGITQPLKFMDIGPKNYEAVTDVSLRGTLYMS
QAVVPHMRERKAGSIVCISSVSAQRGGGIFGGPHYSAAKAGVLGLAKAMARELGPDNVRV
NSVTPGLIQTDITGGKLTDELRTEILKGIPLNRLGDAEDVARSCLFLASELSSYITGATL
DVNGGMLIH
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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