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Comparing CCNA_00545 FitnessBrowser__Caulo:CCNA_00545 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)
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
55% identity, 99% coverage: 3:239/240 of query aligns to 7:248/249 of 3vzsB
- active site: N115 (= N106), S143 (= S134), Y156 (= Y147), K160 (= K151)
- binding acetoacetyl-coenzyme a: D97 (= D88), Q150 (= Q141), F151 (≠ M142), Q153 (= Q144), Y156 (= Y147), G187 (= G178), Y188 (= Y179), R198 (≠ P189)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G9), I18 (= I14), G38 (≠ S34), R43 (≠ A39), G63 (= G54), N64 (= N55), V65 (= V56), G93 (= G84), I94 (= I85), T95 (= T86), P186 (= P177), I189 (= I180), M193 (= M184), V194 (= V185)
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)
55% identity, 99% coverage: 3:239/240 of query aligns to 4:245/246 of P14697
- GGI 13:15 (≠ RGI 12:14) binding
- G35 (≠ S34) binding
- R40 (≠ A39) binding
- 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 (= GNV 54:56) binding
- NAGIT 88:92 (= NAGIT 82:86) binding
- D94 (= D88) mutation to A: About 6% of wild-type activity.
- K99 (= K93) mutation to A: Nearly loss of activity.
- Q147 (= Q141) mutation to A: About 30% of wild-type activity.
- F148 (≠ M142) mutation to A: About 30% of wild-type activity.
- Q150 (= Q144) mutation to A: About 20% of wild-type activity.
- T173 (≠ K167) 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 (= PGYI 177:180) binding
- Y185 (= Y179) mutation to A: Nearly loss of activity.
- R195 (≠ P189) mutation to A: Nearly loss of activity.
4k6fB X-ray crystal structure of a putative acetoacetyl-coa reductase from burkholderia cenocepacia bound to the co-factor NADP
52% identity, 99% coverage: 3:239/240 of query aligns to 2:244/245 of 4k6fB
- active site: G12 (= G13), N102 (≠ Q98), S138 (= S134), Y151 (= Y147), K155 (= K151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), Y32 (= Y33), S33 (= S34), N36 (≠ E37), V58 (= V52), D59 (≠ N55), V60 (= V56), A87 (= A83), G88 (= G84), I89 (= I85)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
55% identity, 99% coverage: 3:239/240 of query aligns to 3:244/245 of 5vmlA
- active site: G13 (= G13), N111 (= N106), S139 (= S134), Y152 (= Y147), K156 (= K151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G9), G12 (≠ R12), G13 (= G13), I14 (= I14), C33 (≠ Y33), G34 (≠ S34), R39 (vs. gap), G59 (= G54), N60 (= N55), V61 (= V56), N87 (= N82), G89 (= G84), I90 (= I85), S139 (= S134), Y152 (= Y147), K156 (= K151), P182 (= P177), G183 (= G178), I185 (= I180)
5vt6A Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b complexed with NADP
48% identity, 99% coverage: 3:240/240 of query aligns to 2:245/245 of 5vt6A
- active site: G12 (= G13), D102 (≠ Q98), S138 (= S134), Y151 (= Y147), K155 (= K151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), G11 (≠ R12), G12 (= G13), L13 (≠ I14), H32 (≠ Y33), S33 (= S34), N36 (≠ E37), V58 (= V52), D59 (≠ N55), V60 (= V56), N86 (= N82), A87 (= A83), G88 (= G84), I89 (= I85), I136 (= I132), Y151 (= Y147), K155 (= K151), P181 (= P177), Y183 (= Y179), L184 (≠ I180), T186 (= T182)
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)
47% identity, 99% coverage: 3:239/240 of query aligns to 6:243/244 of P0AEK2
- GASR 12:15 (≠ GGTR 9:12) binding
- T37 (≠ G35) binding
- NV 59:60 (= NV 55:56) binding
- N86 (= N82) binding
- Y151 (= Y147) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YSAAK 147:151) binding
- A154 (= A150) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K151) mutation to A: Defect in the affinity for NADPH.
- I184 (= I180) binding
- E233 (≠ A229) 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)
47% identity, 99% coverage: 3:239/240 of query aligns to 5:242/243 of 1q7bA
- active site: G15 (= G13), E101 (≠ Q98), S137 (= S134), Q147 (= Q144), Y150 (= Y147), K154 (= K151)
- binding calcium ion: E232 (≠ A229), T233 (= T230)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), S13 (≠ T11), R14 (= R12), T36 (≠ G35), N58 (= N55), V59 (= V56), N85 (= N82), A86 (= A83), G87 (= G84), I88 (= I85), S137 (= S134), Y150 (= Y147), K154 (= K151), P180 (= P177), G181 (= G178), I183 (= I180)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
47% identity, 99% coverage: 3:239/240 of query aligns to 5:242/243 of 1q7cA
- active site: G15 (= G13), S137 (= S134), Q147 (= Q144), F150 (≠ Y147), K154 (= K151)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), S13 (≠ T11), R14 (= R12), A35 (≠ S34), T36 (≠ G35), L57 (≠ V51), N58 (= N55), V59 (= V56), G87 (= G84), I88 (= I85)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
46% identity, 99% coverage: 3:239/240 of query aligns to 6:243/244 of 6t77A
- active site: G16 (= G13), S138 (= S134), Y151 (= Y147)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (≠ T11), R15 (= R12), T37 (≠ G35), L58 (≠ V51), N59 (= N55), V60 (= V56), A87 (= A83), G88 (= G84), I89 (= I85)
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)
46% identity, 99% coverage: 3:239/240 of query aligns to 6:243/244 of P0A2C9
- M125 (= M121) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A219) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (≠ G220) 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.
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
46% identity, 99% coverage: 3:239/240 of query aligns to 5:242/243 of 7emgB
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)
46% identity, 99% coverage: 3:239/240 of query aligns to 9:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), S17 (≠ T11), R18 (= R12), I20 (= I14), T40 (≠ G35), N62 (= N55), V63 (= V56), N89 (= N82), A90 (= A83), I92 (= I85), V139 (≠ I132), S141 (= S134), Y154 (= Y147), K158 (= K151), P184 (= P177), G185 (= G178), I187 (= I180), T189 (= T182), M191 (= M184)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
47% identity, 99% coverage: 3:239/240 of query aligns to 9:242/243 of 4i08A
- active site: G19 (= G13), N113 (= N106), S141 (= S134), Q151 (= Q144), Y154 (= Y147), K158 (= K151)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), S17 (≠ T11), R18 (= R12), I20 (= I14), T40 (≠ G35), N62 (= N55), V63 (= V56), N89 (= N82), A90 (= A83), G140 (≠ S133), S141 (= S134), Y154 (= Y147), K158 (= K151), P184 (= P177), G185 (= G178), T189 (= T182)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
42% identity, 100% coverage: 1:239/240 of query aligns to 3:246/246 of 3osuA
4ag3A Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with NADPH at 1.8a resolution (see paper)
45% identity, 99% coverage: 3:240/240 of query aligns to 13:254/254 of 4ag3A
- active site: G23 (= G13), S148 (= S134), Y161 (= Y147), K165 (= K151)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G9), S21 (≠ T11), R22 (= R12), G23 (= G13), I24 (= I14), T44 (≠ G35), L68 (vs. gap), D69 (≠ N55), V70 (= V56), N96 (= N82), A97 (= A83), I146 (= I132), S148 (= S134), Y161 (= Y147), K165 (= K151), P191 (= P177), G192 (= G178), F193 (≠ Y179), I194 (= I180), T196 (= T182), M198 (= M184), T199 (≠ V185)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
42% identity, 99% coverage: 2:239/240 of query aligns to 1:239/239 of 3sj7A
- active site: G12 (= G13), S138 (= S134), Q148 (= Q144), Y151 (= Y147), K155 (= K151)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), S10 (≠ T11), R11 (= R12), I13 (= I14), N31 (≠ G32), Y32 (= Y33), A33 (≠ S34), G34 (= G35), S35 (≠ N36), A58 (≠ G54), N59 (= N55), V60 (= V56), N86 (= N82), A87 (= A83), T109 (≠ V105), S138 (= S134), Y151 (= Y147), K155 (= K151), P181 (= P177), G182 (= G178)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
43% identity, 99% coverage: 3:239/240 of query aligns to 8:244/244 of 4nbuB
- active site: G18 (= G13), N111 (= N106), S139 (= S134), Q149 (= Q144), Y152 (= Y147), K156 (= K151)
- binding acetoacetyl-coenzyme a: D93 (= D88), K98 (= K93), S139 (= S134), N146 (≠ Q141), V147 (≠ M142), Q149 (= Q144), Y152 (= Y147), F184 (≠ Y179), M189 (= M184), K200 (≠ Q195)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G9), N17 (≠ R12), G18 (= G13), I19 (= I14), D38 (≠ Y33), F39 (≠ S34), V59 (≠ G54), D60 (≠ N55), V61 (= V56), N87 (= N82), A88 (= A83), G89 (= G84), I90 (= I85), T137 (≠ I132), S139 (= S134), Y152 (= Y147), K156 (= K151), P182 (= P177), F184 (≠ Y179), T185 (≠ I180), T187 (= T182), M189 (= M184)
6wprA Crystal structure of a putative 3-oxoacyl-acp reductase (fabg) with NADP(h) from acinetobacter baumannii (see paper)
40% identity, 99% coverage: 3:240/240 of query aligns to 6:244/244 of 6wprA
- active site: G16 (= G13), S138 (= S134), Y151 (= Y147)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (≠ T11), R15 (= R12), T37 (≠ G35), L58 (≠ G54), D59 (≠ N55), V60 (= V56), N86 (= N82), A87 (= A83), G88 (= G84), I89 (= I85), I136 (= I132), Y151 (= Y147), K155 (= K151), P181 (= P177)
6t62A Crystal structure of acinetobacter baumannii fabg in complex with NADPH at 1.8 a resolution (see paper)
40% identity, 99% coverage: 3:240/240 of query aligns to 6:244/244 of 6t62A
- active site: G16 (= G13), S138 (= S134), Y151 (= Y147)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (≠ T11), R15 (= R12), A36 (≠ S34), T37 (≠ G35), L58 (≠ G54), D59 (≠ N55), V60 (= V56), N86 (= N82), A87 (= A83), G88 (= G84), I89 (= I85), I136 (= I132), S137 (= S133), S138 (= S134), Y151 (= Y147), K155 (= K151), P181 (= P177), G182 (= G178), I184 (= I180), M188 (= M184)
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)
45% identity, 99% coverage: 3:240/240 of query aligns to 19:255/255 of 4bo4C
Query Sequence
>CCNA_00545 FitnessBrowser__Caulo:CCNA_00545
MTRVAFVTGGTRGIGRAICERLIADGHKVAAGYSGNEAAAEACAKELGVMVVKGNVGVFE
DCQAAVKKVEAELGPIDILVNNAGITRDGMLHKMTYEQWSEVIRVNMDSAFNMTRPVIEG
MRDRSWGRIINISSINGQKGQMGQTNYSAAKAGLIGFTKALALENAKKGVTVNVICPGYI
DTEMVAAVPENVLAQIVAGIPVGRLGRGEEIADMVSFLAGERAGFVTGATLTLNGGQYMA
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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