SitesBLAST
Comparing WP_090273523.1 NCBI__GCF_900105005.1:WP_090273523.1 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)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
43% identity, 100% coverage: 2:252/252 of query aligns to 4:244/244 of 4nbuB
- active site: G18 (= G16), N111 (= N121), S139 (= S150), Q149 (= Q159), Y152 (= Y162), K156 (= K166)
- binding acetoacetyl-coenzyme a: D93 (= D95), K98 (= K108), S139 (= S150), N146 (= N156), V147 (≠ M157), Q149 (= Q159), Y152 (= Y162), F184 (= F194), M189 (= M199), K200 (= K210)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ Q15), G18 (= G16), I19 (≠ L17), D38 (= D36), F39 (≠ L37), V59 (≠ C61), D60 (≠ N62), V61 (≠ I63), N87 (= N89), A88 (= A90), G89 (= G91), I90 (= I92), T137 (≠ I148), S139 (= S150), Y152 (= Y162), K156 (= K166), P182 (= P192), F184 (= F194), T185 (≠ I195), T187 (= T197), M189 (= M199)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
39% identity, 100% coverage: 1:252/252 of query aligns to 4:247/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G12), R18 (≠ Q15), G19 (= G16), I20 (≠ L17), D39 (= D36), R40 (≠ L37), C63 (= C61), I65 (= I63), N91 (= N89), G93 (= G91), I94 (= I92), V114 (= V120), Y155 (= Y162), K159 (= K166), I188 (= I195), T190 (= T197), T193 (= T200)
4nbwA Crystal structure of fabg from plesiocystis pacifica (see paper)
43% identity, 97% coverage: 7:250/252 of query aligns to 3:249/253 of 4nbwA
- active site: G12 (= G16), S146 (= S150), Y159 (= Y162), K163 (= K166)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), N11 (≠ Q15), G12 (= G16), I13 (≠ L17), D32 (= D36), L33 (= L37), V57 (≠ C61), D58 (≠ N62), V59 (≠ I63), N85 (= N89), A86 (= A90), G87 (= G91), S146 (= S150), Y159 (= Y162), K163 (= K166), I192 (= I195), T194 (= T197)
4cqlI Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD (see paper)
39% identity, 99% coverage: 2:250/252 of query aligns to 5:249/251 of 4cqlI
- active site: G19 (= G16), S146 (= S150), Y159 (= Y162), K163 (= K166)
- binding nicotinamide-adenine-dinucleotide: S18 (≠ Q15), G19 (= G16), I20 (≠ L17), D39 (= D36), L40 (= L37), A64 (≠ C61), D65 (≠ N62), V66 (≠ I63), C93 (≠ N89), A94 (= A90), G95 (= G91), I96 (= I92), V116 (= V120), I144 (= I148), S146 (= S150), Y159 (= Y162), K163 (= K166), P189 (= P192), G190 (= G193), I192 (= I195), T194 (= T197), M196 (= M199)
4cqmA Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
39% identity, 99% coverage: 2:250/252 of query aligns to 3:246/248 of 4cqmA
- active site: G17 (= G16), S143 (= S150), Y156 (= Y162), K160 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), S16 (≠ Q15), G17 (= G16), I18 (≠ L17), D37 (= D36), L38 (= L37), A61 (≠ C61), V63 (≠ I63), C90 (≠ N89), A91 (= A90), G92 (= G91), I93 (= I92), V113 (= V120), I141 (= I148), S143 (= S150), Y156 (= Y162), K160 (= K166), P186 (= P192), G187 (= G193), I189 (= I195), T191 (= T197), P192 (≠ E198), M193 (= M199), T194 (= T200)
4cqmF Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
39% identity, 98% coverage: 5:252/252 of query aligns to 6:239/241 of 4cqmF
- active site: G17 (= G16), S139 (= S150), Q149 (= Q159), Y152 (= Y162), K156 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), R16 (≠ Q15), G17 (= G16), I18 (≠ L17), A37 (≠ D36), R38 (≠ L37), N39 (≠ D38), D60 (≠ N62), V61 (≠ I63), A87 (≠ N89), A88 (= A90), G89 (= G91), V137 (≠ I148), S139 (= S150), Y152 (= Y162), K156 (= K166), V185 (≠ I195), T187 (= T197), M189 (= M199)
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)
42% identity, 98% coverage: 3:250/252 of query aligns to 4:244/247 of P73574
- A14 (≠ G13) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ M157) 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 (= K166) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (= F194) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ K204) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
Q8N4T8 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-[acyl-carrier-protein] reductase beta subunit; KAR beta subunit; Carbonyl reductase family member 4; CBR4; Quinone reductase CBR4; Short chain dehydrogenase/reductase family 45C member 1; EC 1.1.1.100; EC 1.6.5.10 from Homo sapiens (Human) (see 4 papers)
39% identity, 98% coverage: 5:252/252 of query aligns to 2:235/237 of Q8N4T8
- G9 (= G12) mutation to S: Unable to restore growth of an OAR1-deficient yeast mutant.
- SRGI 11:14 (≠ GQGL 14:17) binding NADP(+)
- R12 (≠ Q15) mutation to A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant.
- R34 (≠ L37) mutation to A: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Strongly reduces NADPH-dependent reductase activity with acetoacetyl-CoA and 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- RN 34:35 (≠ LD 37:38) binding NADP(+)
- D56 (≠ N62) binding NADP(+)
- L70 (≠ V76) to M: in dbSNP:rs2877380
- AAG 83:85 (≠ NAG 89:91) binding NADP(+)
- S135 (= S150) mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- Y148 (= Y162) binding NADP(+); mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant.
- K152 (= K166) binding NADP(+); mutation to A: Unable to restore growth of an OAR1-deficient yeast mutant. Abolishes NADPH-dependent reductase activity with acetoacetyl-CoA. Strongly reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- R168 (= R182) mutation to E: Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- K169 (≠ Y183) mutation to E: Unable to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.
- VHT 181:183 (≠ IET 195:197) binding NADP(+)
Q92506 (3R)-3-hydroxyacyl-CoA dehydrogenase; 17-beta-hydroxysteroid dehydrogenase 8; 17-beta-HSD 8; HSD17B8; 3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit; KAR alpha subunit; 3-oxoacyl-[acyl-carrier-protein] reductase; Estradiol 17-beta-dehydrogenase 8; Protein Ke6; Ke6; Short chain dehydrogenase/reductase family 30C member 1; Testosterone 17-beta-dehydrogenase 8; EC 1.1.1.n12; EC 1.1.1.62; EC 1.1.1.239 from Homo sapiens (Human) (see 2 papers)
38% identity, 99% coverage: 2:250/252 of query aligns to 8:259/261 of Q92506
- 15:23 (vs. 9:17, 56% identical) binding NAD(+)
- D42 (= D36) mutation to A: Reduced NADH-dependent reductase activity with acetoacetyl-CoA. Reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Increases NADPH-dependent reductase activities. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- DL 42:43 (= DL 36:37) binding NAD(+)
- ADV 74:76 (≠ CNI 61:63) binding NAD(+)
- R148 (≠ K142) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- V158 (vs. gap) to L: in a breast cancer sample; somatic mutation
- Y169 (= Y162) mutation to A: Strongly reduced NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- YAASK 169:173 (≠ YSAAK 162:166) binding NAD(+)
- K173 (= K166) mutation to A: Abolishes NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Slightly decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- R189 (= R182) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- IAT 202:204 (≠ IET 195:197) binding NAD(+)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
39% identity, 97% coverage: 9:252/252 of query aligns to 8:246/246 of 3osuA
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
38% identity, 98% coverage: 3:248/252 of query aligns to 6:236/240 of P73826
- S134 (= S150) mutation to A: 12% enzymatic activity.
- Y147 (= Y162) mutation to A: No enzymatic activity.
- K151 (= K166) mutation to A: 5% enzymatic activity.
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
39% identity, 97% coverage: 9:252/252 of query aligns to 5:239/239 of 3sj7A
- active site: G12 (= G16), S138 (= S150), Q148 (= Q159), Y151 (= Y162), K155 (= K166)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), S10 (≠ G14), R11 (≠ Q15), I13 (≠ L17), N31 (≠ V35), Y32 (≠ D36), A33 (≠ L37), G34 (vs. gap), S35 (≠ D38), A58 (≠ C61), N59 (= N62), V60 (≠ I63), N86 (= N89), A87 (= A90), T109 (≠ V120), S138 (= S150), Y151 (= Y162), K155 (= K166), P181 (= P192), G182 (= G193)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
39% identity, 100% coverage: 2:252/252 of query aligns to 2:239/239 of 4nbtA
- active site: G16 (= G16), S132 (= S150), Y145 (= Y162), K149 (= K166)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), K15 (≠ Q15), G16 (= G16), L17 (= L17), D36 (= D36), L37 (= L37), L52 (≠ C61), N53 (= N62), V54 (≠ I63), N80 (= N89), A81 (= A90), G82 (= G91), I130 (= I148), S132 (= S150), Y145 (= Y162), K149 (= K166), P177 (= P192), G178 (= G193), I180 (= I195), T182 (= T197)
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)
35% identity, 100% coverage: 1:252/252 of query aligns to 4:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G12), S17 (≠ G14), R18 (≠ Q15), I20 (≠ L17), T40 (≠ L37), N62 (= N62), V63 (≠ I63), N89 (= N89), A90 (= A90), I92 (= I92), V139 (≠ I148), S141 (= S150), Y154 (= Y162), K158 (= K166), P184 (= P192), G185 (= G193), I187 (= I195), T189 (= T197), M191 (= M199)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
37% identity, 99% coverage: 1:250/252 of query aligns to 1:245/247 of 4jroC
- active site: G16 (= G16), S142 (= S150), Q152 (= Q159), Y155 (= Y162), K159 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ G14), R15 (≠ Q15), G16 (= G16), I17 (≠ L17), N35 (vs. gap), Y36 (≠ V35), N37 (≠ D36), G38 (≠ L37), S39 (≠ D38), N63 (= N62), V64 (≠ I63), N90 (= N89), A91 (= A90), I93 (= I92), I113 (≠ V120), S142 (= S150), Y155 (= Y162), K159 (= K166), P185 (= P192), I188 (= I195), T190 (= T197)
9clyB Crystal structure of the 3-ketoacyl-(acyl-carrier-protein) reductase, cylg, from streptococcus agalactiae 2603v/r
37% identity, 97% coverage: 7:250/252 of query aligns to 5:239/242 of 9clyB
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G10 (= G12), R13 (≠ Q15), G14 (= G16), I15 (≠ L17), Y34 (≠ V35), N35 (≠ D36), S36 (≠ L37), C56 (= C61), N57 (= N62), I58 (= I63), N84 (= N89), I135 (= I148), S137 (= S150), Y150 (= Y162), K154 (= K166), G181 (= G193), I183 (= I195), T185 (= T197), M187 (= M199)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
37% identity, 96% coverage: 10:252/252 of query aligns to 7:244/245 of 5vmlA
- active site: G13 (= G16), N111 (= N121), S139 (= S150), Y152 (= Y162), K156 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G12), G12 (≠ Q15), G13 (= G16), I14 (≠ L17), C33 (≠ V35), G34 (≠ D36), R39 (≠ K41), G59 (≠ C61), N60 (= N62), V61 (≠ I63), N87 (= N89), G89 (= G91), I90 (= I92), S139 (= S150), Y152 (= Y162), K156 (= K166), P182 (= P192), G183 (= G193), I185 (= I195)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
34% identity, 100% coverage: 1:252/252 of query aligns to 1:243/244 of 6t77A
- active site: G16 (= G16), S138 (= S150), Y151 (= Y162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ G14), R15 (≠ Q15), T37 (≠ L37), L58 (≠ C61), N59 (= N62), V60 (≠ I63), A87 (= A90), G88 (= G91), I89 (= I92)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
33% identity, 100% coverage: 2:252/252 of query aligns to 1:242/243 of 7emgB
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
36% identity, 96% coverage: 10:252/252 of query aligns to 11:248/249 of 3vzsB
- active site: N115 (= N121), S143 (= S150), Y156 (= Y162), K160 (= K166)
- binding acetoacetyl-coenzyme a: D97 (= D95), Q150 (≠ N156), F151 (≠ M157), Q153 (= Q159), Y156 (= Y162), G187 (= G193), Y188 (≠ F194), R198 (≠ K204)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), I18 (≠ L17), G38 (≠ D36), R43 (≠ K41), G63 (≠ C61), N64 (= N62), V65 (≠ I63), G93 (= G91), I94 (= I92), T95 (≠ L93), P186 (= P192), I189 (= I195), M193 (= M199), V194 (≠ T200)
Query Sequence
>WP_090273523.1 NCBI__GCF_900105005.1:WP_090273523.1
MQLKDSVIIVTGGGQGLGRAMAEYLAGRGARLALVDLDQAKLDEAVAACKTAGGDARAYV
CNIANEQQVTDMVGQVATDYGTINGLINNAGILRDGLLLKSKDGEIQKMSLNQWQSVIDV
NLTGVFLGTREVAAKMVELGSKGLIINISSISRAGNMGQSNYSAAKAGVAALTVVWAKEL
ARYGIRVAGIAPGFIETEMTSGMKPEALEKMTSGIPLRRMGMPEEIAHSAAYLFENDYYS
GRILELDGGLRL
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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