SitesBLAST
Comparing WP_058929193.1 NCBI__GCF_001484605.1:WP_058929193.1 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: 1:250/250 of query aligns to 2:251/251 of 6d9yB
- active site: G20 (= G19), S145 (= S144), Y158 (= Y157)
- binding nicotinamide-adenine-dinucleotide: G16 (= G15), R19 (≠ Q18), G20 (= G19), D40 (= D39), L41 (≠ V40), V64 (= V63), D65 (= D64), Q66 (= Q65), A93 (= A92), S145 (= S144), Y158 (= Y157), K162 (= K161), P188 (= P187), A189 (≠ T188), A190 (= A189), A191 (≠ V190), T193 (= T192)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
38% identity, 97% coverage: 4:246/250 of query aligns to 1:240/244 of 6t77A
- active site: G16 (= G19), S138 (= S144), Y151 (= Y157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (≠ A17), R15 (≠ Q18), T37 (≠ A44), L58 (≠ H61), N59 (≠ E62), V60 (= V63), A87 (= A92), G88 (= G93), I89 (= I94)
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)
37% identity, 97% coverage: 4:246/250 of query aligns to 1:240/244 of P0AEK2
- GASR 12:15 (≠ GGAQ 15:18) binding NADP(+)
- T37 (≠ A44) binding NADP(+)
- NV 59:60 (≠ EV 62:63) binding NADP(+)
- N86 (= N91) binding NADP(+)
- Y151 (= Y157) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YSAAK 157:161) binding NADP(+)
- A154 (= A160) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K161) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ V190) binding NADP(+)
- E233 (≠ A239) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
38% identity, 97% coverage: 4:246/250 of query aligns to 1:247/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), Q15 (= Q18), G16 (= G19), I17 (= I20), D36 (= D39), V63 (≠ Q65), N89 (= N91), A91 (≠ G93), S94 (≠ G96), I142 (≠ V142), S143 (≠ A143), S144 (= S144), Y157 (= Y157), K161 (= K161), P187 (= P187), H188 (≠ T188), I190 (≠ V190), I194 (= I194)
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
36% identity, 98% coverage: 6:250/250 of query aligns to 2:245/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), M16 (≠ I20), D35 (= D39), I36 (≠ V40), I62 (≠ Q65), N88 (= N91), G90 (= G93), I138 (≠ V142), S140 (= S144), Y152 (= Y157), K156 (= K161), I185 (≠ V190)
Q9KJF1 (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase subunit BbsD; (S,R)-2-(alpha-hydroxybenzyl)succinyl-CoA dehydrogenase subunit BbsD; EC 1.1.1.429 from Thauera aromatica (see 2 papers)
36% identity, 98% coverage: 6:250/250 of query aligns to 3:246/248 of Q9KJF1
- S15 (≠ Q18) binding NAD(+)
- D36 (= D39) binding NAD(+)
- D62 (= D64) binding NAD(+)
- I63 (≠ Q65) binding NAD(+)
- N89 (= N91) binding NAD(+)
- Y153 (= Y157) binding NAD(+)
- K157 (= K161) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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: 4:246/250 of query aligns to 1:240/244 of P0A2C9
- M125 (= M131) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (≠ V229) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S230) 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.
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
37% identity, 97% coverage: 5:246/250 of query aligns to 1:239/243 of 1q7bA
- active site: G15 (= G19), E101 (= E108), S137 (= S144), Q147 (≠ A154), Y150 (= Y157), K154 (= K161)
- binding calcium ion: E232 (≠ A239), T233 (≠ A240)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (≠ A17), R14 (≠ Q18), T36 (≠ A44), N58 (≠ E62), V59 (= V63), N85 (= N91), A86 (= A92), G87 (= G93), I88 (= I94), S137 (= S144), Y150 (= Y157), K154 (= K161), P180 (= P187), G181 (≠ T188), I183 (≠ V190)
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)
38% identity, 97% coverage: 4:246/250 of query aligns to 4:243/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (≠ A17), R18 (≠ Q18), I20 (= I20), T40 (≠ A44), N62 (≠ E62), V63 (= V63), N89 (= N91), A90 (= A92), I92 (= I94), V139 (= V142), S141 (= S144), Y154 (= Y157), K158 (= K161), P184 (= P187), G185 (≠ T188), I187 (≠ V190), T189 (= T192), M191 (≠ I194)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
37% identity, 97% coverage: 5:246/250 of query aligns to 1:239/243 of 1q7cA
- active site: G15 (= G19), S137 (= S144), Q147 (≠ A154), F150 (≠ Y157), K154 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (≠ A17), R14 (≠ Q18), A35 (= A43), T36 (≠ A44), L57 (≠ H61), N58 (≠ E62), V59 (= V63), G87 (= G93), I88 (= I94)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
38% identity, 97% coverage: 4:246/250 of query aligns to 4:239/243 of 4i08A
- active site: G19 (= G19), N113 (≠ D116), S141 (= S144), Q151 (≠ A154), Y154 (= Y157), K158 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (≠ A17), R18 (≠ Q18), I20 (= I20), T40 (≠ A44), N62 (≠ E62), V63 (= V63), N89 (= N91), A90 (= A92), G140 (≠ A143), S141 (= S144), Y154 (= Y157), K158 (= K161), P184 (= P187), G185 (≠ T188), T189 (= T192)
5ts3A Crystal structure of a 3-oxoacyl-[acyl-carrier protein] reductase with bound NAD from brucella melitensis
38% identity, 94% coverage: 12:246/250 of query aligns to 23:261/265 of 5ts3A
- active site: G30 (= G19), S158 (= S144), V168 (≠ A154), Y172 (= Y157), K176 (= K161)
- binding nicotinamide-adenine-dinucleotide: G26 (= G15), R29 (≠ Q18), G30 (= G19), I31 (= I20), D50 (= D39), L51 (≠ V40), D77 (= D64), V78 (≠ Q65), N101 (= N91), V129 (= V115), T156 (≠ V142), Y172 (= Y157), K176 (= K161), P202 (= P187), I205 (≠ V190), T207 (= T192)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
38% identity, 96% coverage: 6:246/250 of query aligns to 5:241/244 of 4nbuB
- active site: G18 (= G19), N111 (≠ D116), S139 (= S144), Q149 (≠ A154), Y152 (= Y157), K156 (= K161)
- binding acetoacetyl-coenzyme a: D93 (≠ P97), K98 (≠ E103), S139 (= S144), N146 (= N151), V147 (≠ P152), Q149 (≠ A154), Y152 (= Y157), F184 (≠ A189), M189 (≠ I194), K200 (≠ Y205)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), N17 (≠ Q18), G18 (= G19), I19 (= I20), D38 (= D39), F39 (≠ V40), V59 (= V63), D60 (= D64), V61 (≠ Q65), N87 (= N91), A88 (= A92), G89 (= G93), I90 (= I94), T137 (≠ V142), S139 (= S144), Y152 (= Y157), K156 (= K161), P182 (= P187), F184 (≠ A189), T185 (≠ V190), T187 (= T192), M189 (≠ I194)
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
37% identity, 97% coverage: 4:246/250 of query aligns to 1:236/240 of 4dmmB
- active site: G16 (= G19), S142 (= S144), Q152 (≠ A154), Y155 (= Y157), K159 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (≠ A17), R15 (≠ Q18), G16 (= G19), I17 (= I20), A37 (≠ V40), S38 (≠ D41), S39 (≠ T42), A62 (≠ V63), D63 (= D64), V64 (≠ Q65), N90 (= N91), A91 (= A92), L113 (≠ V115), I140 (≠ V142), S142 (= S144), Y155 (= Y157), K159 (= K161), P185 (= P187), G186 (≠ T188), I188 (≠ V190), T190 (= T192), M192 (≠ I194)
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)
38% identity, 98% coverage: 6:250/250 of query aligns to 4:247/247 of P73574
- A14 (≠ G16) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (= P152) 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 (= K161) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ A189) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ T199) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
8y83A Crystal structure of a ketoreductase from sphingobacterium siyangense sy1 with co-enzyme (see paper)
34% identity, 96% coverage: 6:246/250 of query aligns to 4:245/249 of 8y83A
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), S16 (≠ Q18), G17 (= G19), I18 (= I20), D37 (= D39), I38 (≠ V40), A62 (≠ V63), D63 (= D64), S64 (≠ Q65), N90 (= N91), M141 (≠ V142), Y156 (= Y157), K160 (= K161), P186 (= P187), G187 (≠ T188), Y188 (≠ A189), I189 (≠ V190), L193 (≠ I194)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
37% identity, 95% coverage: 9:246/250 of query aligns to 5:243/246 of 3osuA
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
36% identity, 96% coverage: 6:246/250 of query aligns to 2:239/243 of 7emgB
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)
35% identity, 96% coverage: 6:246/250 of query aligns to 1:242/246 of P14697
- GGI 13:15 (≠ QGI 18:20) binding NADP(+)
- G35 (≠ A44) binding NADP(+)
- R40 (≠ A49) binding NADP(+)
- Q47 (vs. gap) 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 (≠ VDQ 63:65) binding NADP(+)
- NAGIT 88:92 (≠ NAGIA 91:95) binding NADP(+)
- D94 (≠ P97) mutation to A: About 6% of wild-type activity.
- K99 (≠ E103) mutation to A: Nearly loss of activity.
- Q147 (≠ N151) mutation to A: About 30% of wild-type activity.
- F148 (≠ P152) mutation to A: About 30% of wild-type activity.
- Q150 (≠ A154) mutation to A: About 20% of wild-type activity.
- T173 (≠ H177) 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 (≠ PTAV 187:190) binding NADP(+)
- Y185 (≠ A189) mutation to A: Nearly loss of activity.
- R195 (≠ T199) mutation to A: Nearly loss of activity.
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
36% identity, 95% coverage: 9:246/250 of query aligns to 2:236/239 of 3sj7A
- active site: G12 (= G19), S138 (= S144), Q148 (≠ A154), Y151 (= Y157), K155 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), S10 (≠ A17), R11 (≠ Q18), I13 (= I20), N31 (≠ D41), Y32 (≠ T42), A33 (= A43), G34 (≠ A44), S35 (≠ L45), A58 (vs. gap), N59 (vs. gap), V60 (vs. gap), N86 (= N91), A87 (= A92), T109 (≠ V115), S138 (= S144), Y151 (= Y157), K155 (= K161), P181 (= P187), G182 (≠ T188)
Query Sequence
>WP_058929193.1 NCBI__GCF_001484605.1:WP_058929193.1
MNTIDLNNKVAIVTGGAQGIGRAIAERLLRSGAEVHIWDVDTAALSTSAQELGLLGKVVA
HEVDQTDFAAVATAAKAVEQSHGKIDILVNNAGIAGPAKPLLEYSPQEWGAVIDVDLNGA
FNCCHAVVPVMVKNNYGRVLNVASVAGKEGNPNAAAYSAAKAGVIAMTKSLAKELAHHEI
AVNCITPTAVATKIFDQVTVEHIGYILERIPRGRFLKAEELAAMVAWLVSAENSFTTGAA
FDLSGGRATY
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