SitesBLAST
Comparing WP_012757694.1 NCBI__GCF_000023185.1:WP_012757694.1 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)
6d9yB Crystal structure of a short chain dehydrogenase/reductase sdr from burkholderia phymatum with partially occupied NAD
54% identity, 100% coverage: 1:248/248 of query aligns to 2:251/251 of 6d9yB
- active site: G20 (= G19), S145 (= S142), Y158 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G16 (= G15), R19 (= R18), G20 (= G19), D40 (= D39), L41 (= L40), V64 (= V61), D65 (≠ N62), Q66 (≠ V63), A93 (= A90), S145 (= S142), Y158 (= Y155), K162 (= K159), P188 (= P185), A189 (≠ T186), A190 (≠ T187), A191 (= A188), T193 (= T190)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 98% coverage: 2:244/248 of query aligns to 1:241/244 of 4nbuB
- active site: G18 (= G19), N111 (≠ C114), S139 (= S142), Q149 (≠ I152), Y152 (= Y155), K156 (= K159)
- binding acetoacetyl-coenzyme a: D93 (≠ P95), K98 (≠ E101), S139 (= S142), N146 (= N149), V147 (≠ P150), Q149 (≠ I152), Y152 (= Y155), F184 (≠ T187), M189 (≠ I192), K200 (≠ Y203)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), N17 (≠ R18), G18 (= G19), I19 (= I20), D38 (= D39), F39 (≠ L40), V59 (= V61), D60 (≠ N62), V61 (= V63), N87 (≠ S89), A88 (= A90), G89 (= G91), I90 (= I92), T137 (≠ I140), S139 (= S142), Y152 (= Y155), K156 (= K159), P182 (= P185), F184 (≠ T187), T185 (≠ A188), T187 (= T190), M189 (≠ I192)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
40% identity, 94% coverage: 12:244/248 of query aligns to 8:243/246 of 3osuA
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, 97% coverage: 4:244/248 of query aligns to 1:240/244 of P0A2C9
- M125 (= M129) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (≠ L227) 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.
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
37% identity, 97% coverage: 4:244/248 of query aligns to 1:240/244 of 6t77A
- active site: G16 (= G19), S138 (= S142), Y151 (= Y155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (≠ A17), R15 (= R18), T37 (≠ L40), L58 (≠ V61), N59 (= N62), V60 (= V63), A87 (= A90), G88 (= G91), I89 (= I92)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
38% identity, 95% coverage: 9:244/248 of query aligns to 5:239/243 of 7emgB
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)
36% identity, 97% coverage: 4:244/248 of query aligns to 1:240/244 of P0AEK2
- GASR 12:15 (≠ GGAR 15:18) binding NADP(+)
- T37 (≠ L40) binding NADP(+)
- NV 59:60 (= NV 62:63) binding NADP(+)
- N86 (≠ S89) 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 (≠ A188) binding NADP(+)
- E233 (≠ S237) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
40% identity, 94% coverage: 12:244/248 of query aligns to 5:236/239 of 3sj7A
- active site: G12 (= G19), S138 (= S142), Q148 (≠ I152), Y151 (= Y155), K155 (= K159)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), S10 (≠ A17), R11 (= R18), I13 (= I20), N31 (= N41), Y32 (≠ E42), A33 (≠ N43), G34 (≠ M44), S35 (≠ A45), A58 (≠ V61), N59 (= N62), V60 (= V63), N86 (≠ S89), A87 (= A90), T109 (≠ V113), S138 (= S142), Y151 (= Y155), K155 (= K159), P181 (= P185), G182 (≠ T186)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
36% identity, 97% coverage: 5:244/248 of query aligns to 1:239/243 of 1q7bA
- active site: G15 (= G19), E101 (= E106), S137 (= S142), Q147 (≠ I152), Y150 (= Y155), K154 (= K159)
- binding calcium ion: E232 (≠ S237), T233 (= T238)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (≠ A17), R14 (= R18), T36 (≠ L40), N58 (= N62), V59 (= V63), N85 (≠ S89), A86 (= A90), G87 (= G91), I88 (= I92), S137 (= S142), Y150 (= Y155), K154 (= K159), P180 (= P185), G181 (≠ T186), I183 (≠ A188)
P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
39% identity, 99% coverage: 3:248/248 of query aligns to 1:247/247 of P73574
- A14 (≠ G16) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (= P150) mutation to F: 2.7-fold increase in activity on acetoacetyl-CoA.; mutation to V: 5.7-fold increase in activity on acetoacetyl-CoA.
- K160 (= K159) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ T187) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ T197) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
35% identity, 97% coverage: 5:244/248 of query aligns to 1:239/243 of 1q7cA
- active site: G15 (= G19), S137 (= S142), Q147 (≠ I152), F150 (≠ Y155), K154 (= K159)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (≠ A17), R14 (= R18), A35 (≠ D39), T36 (≠ L40), L57 (≠ V61), N58 (= N62), V59 (= V63), G87 (= G91), I88 (= I92)
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)
36% identity, 98% coverage: 2:244/248 of query aligns to 2:243/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (≠ A17), R18 (= R18), I20 (= I20), T40 (≠ L40), N62 (= N62), V63 (= V63), N89 (≠ S89), A90 (= A90), I92 (= I92), V139 (≠ I140), S141 (= S142), Y154 (= Y155), K158 (= K159), P184 (= P185), G185 (≠ T186), I187 (≠ A188), T189 (= T190), M191 (≠ I192)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
39% identity, 96% coverage: 8:244/248 of query aligns to 2:241/245 of 5vmlA
- active site: G13 (= G19), N111 (≠ C114), S139 (= S142), Y152 (= Y155), K156 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G15), G12 (≠ R18), G13 (= G19), I14 (= I20), C33 (≠ L40), G34 (≠ N41), R39 (≠ K46), G59 (≠ V61), N60 (= N62), V61 (= V63), N87 (≠ S89), G89 (= G91), I90 (= I92), S139 (= S142), Y152 (= Y155), K156 (= K159), P182 (= P185), G183 (≠ T186), I185 (≠ A188)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
34% identity, 97% coverage: 6:246/248 of query aligns to 3:246/248 of 6ixmC
- active site: G16 (= G19), S142 (= S142), Y155 (= Y155), K159 (= K159)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), S15 (≠ R18), G16 (= G19), I17 (= I20), D36 (= D39), I37 (≠ L40), A61 (≠ V61), D62 (≠ N62), T63 (≠ V63), N89 (≠ S89), A90 (= A90), M140 (≠ I140), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), A186 (≠ T186), Y187 (≠ T187), I188 (≠ A188), L192 (≠ I192)
5ts3A Crystal structure of a 3-oxoacyl-[acyl-carrier protein] reductase with bound NAD from brucella melitensis
40% identity, 96% coverage: 7:244/248 of query aligns to 18:261/265 of 5ts3A
- active site: G30 (= G19), S158 (= S142), V168 (≠ I152), Y172 (= Y155), K176 (= K159)
- binding nicotinamide-adenine-dinucleotide: G26 (= G15), R29 (= R18), G30 (= G19), I31 (= I20), D50 (= D39), L51 (= L40), D77 (≠ N62), V78 (= V63), N101 (≠ S89), V129 (= V113), T156 (≠ I140), Y172 (= Y155), K176 (= K159), P202 (= P185), I205 (≠ A188), T207 (= T190)
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)
37% identity, 96% coverage: 6:244/248 of query aligns to 1:242/246 of P14697
- GGI 13:15 (≠ RGI 18:20) binding NADP(+)
- G35 (≠ N41) binding NADP(+)
- R40 (≠ K46) binding NADP(+)
- Q47 (≠ S48) 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 (≠ VNV 61:63) binding NADP(+)
- NAGIT 88:92 (≠ SAGIT 89:93) binding NADP(+)
- D94 (≠ P95) mutation to A: About 6% of wild-type activity.
- K99 (≠ E101) mutation to A: Nearly loss of activity.
- Q147 (≠ N149) mutation to A: About 30% of wild-type activity.
- F148 (≠ P150) mutation to A: About 30% of wild-type activity.
- Q150 (≠ I152) mutation to A: About 20% of wild-type activity.
- T173 (≠ K175) 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 (≠ PTTA 185:188) binding NADP(+)
- Y185 (≠ T187) mutation to A: Nearly loss of activity.
- R195 (≠ T197) mutation to A: Nearly loss of activity.
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
36% identity, 98% coverage: 2:244/248 of query aligns to 2:239/243 of 4i08A
- active site: G19 (= G19), N113 (≠ C114), S141 (= S142), Q151 (≠ I152), Y154 (= Y155), K158 (= K159)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (≠ A17), R18 (= R18), I20 (= I20), T40 (≠ L40), N62 (= N62), V63 (= V63), N89 (≠ S89), A90 (= A90), G140 (≠ S141), S141 (= S142), Y154 (= Y155), K158 (= K159), P184 (= P185), G185 (≠ T186), T189 (= T190)
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
38% identity, 96% coverage: 8:244/248 of query aligns to 6:245/249 of 3vzsB
- active site: N115 (≠ C114), S143 (= S142), Y156 (= Y155), K160 (= K159)
- binding acetoacetyl-coenzyme a: D97 (≠ P95), Q150 (≠ N149), F151 (≠ P150), Q153 (≠ I152), Y156 (= Y155), G187 (≠ T186), Y188 (≠ T187), R198 (≠ T197)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G15), I18 (= I20), G38 (≠ N41), R43 (≠ K46), G63 (≠ V61), N64 (= N62), V65 (= V63), G93 (= G91), I94 (= I92), T95 (= T93), P186 (= P185), I189 (≠ A188), M193 (≠ I192), V194 (≠ L193)
8y83A Crystal structure of a ketoreductase from sphingobacterium siyangense sy1 with co-enzyme (see paper)
33% identity, 97% coverage: 6:246/248 of query aligns to 4:247/249 of 8y83A
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), S16 (≠ R18), G17 (= G19), I18 (= I20), D37 (= D39), I38 (≠ L40), A62 (≠ V61), D63 (≠ N62), S64 (≠ V63), N90 (≠ S89), M141 (≠ I140), Y156 (= Y155), K160 (= K159), P186 (= P185), G187 (≠ T186), Y188 (≠ T187), I189 (≠ A188), L193 (≠ I192)
7krmC Putative fabg bound to nadh from acinetobacter baumannii
36% identity, 98% coverage: 6:248/248 of query aligns to 3:244/244 of 7krmC
- active site: G18 (= G19), S140 (= S142), Y155 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), S15 (vs. gap), G18 (= G19), I19 (= I20), D38 (= D39), L39 (= L40), A60 (≠ V61), N61 (= N62), V62 (= V63), N88 (≠ S89), V111 (= V113), S140 (= S142), Y155 (= Y155), K159 (= K159), I188 (≠ A188), T190 (= T190)
Query Sequence
>WP_012757694.1 NCBI__GCF_000023185.1:WP_012757694.1
MNMIDLKERIIVITGGARGIGYAIAERVIQSGGKVAIWDLNENMAKDSASALGSGTVAFG
VNVADPVSVKNAAGRTEEIFGRIDGLVNSAGITGPVKPTIEYDVSEWKDVVDVCLTGTFN
CCRHVVPVMLKRDYGRIVNISSVAGKEGNPNIAAYSAAKAGVLGFTKSLGKELAKTGIAV
NAVTPTTAKTPILDGLTAEFIEYMRVRIPRDRFAELHEIASMVVWLLSEENSFTTASTFD
LSGGRTTY
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