SitesBLAST
Comparing WP_086008421.1 NCBI__GCF_000015305.1:WP_086008421.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
47% identity, 98% coverage: 4:247/250 of query aligns to 1:241/244 of 4nbuB
- active site: G18 (= G21), N111 (≠ H117), S139 (= S145), Q149 (= Q155), Y152 (= Y158), K156 (= K162)
- binding acetoacetyl-coenzyme a: D93 (= D99), K98 (= K104), S139 (= S145), N146 (≠ M152), V147 (= V153), Q149 (= Q155), Y152 (= Y158), F184 (≠ L190), M189 (= M195), K200 (≠ S206)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G17), N17 (≠ Q20), G18 (= G21), I19 (≠ L22), D38 (= D41), F39 (≠ V42), V59 (≠ C65), D60 (= D66), V61 (= V67), N87 (= N93), A88 (= A94), G89 (= G95), I90 (= I96), T137 (≠ M143), S139 (= S145), Y152 (= Y158), K156 (= K162), P182 (= P188), F184 (≠ L190), T185 (≠ I191), T187 (≠ S193), M189 (= M195)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
47% identity, 96% coverage: 8:247/250 of query aligns to 6:244/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G17), R18 (≠ Q20), G19 (= G21), I20 (≠ L22), D39 (= D41), R40 (≠ V42), C63 (= C65), I65 (≠ V67), N91 (= N93), G93 (= G95), I94 (= I96), V114 (= V116), Y155 (= Y158), K159 (= K162), I188 (= I191), T190 (≠ S193), T193 (= T196)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
46% identity, 97% coverage: 8:250/250 of query aligns to 3:239/239 of 4nbtA
- active site: G16 (= G21), S132 (= S145), Y145 (= Y158), K149 (= K162)
- binding nicotinamide-adenine-dinucleotide: G12 (= G17), K15 (≠ Q20), G16 (= G21), L17 (= L22), D36 (= D41), L37 (≠ V42), L52 (≠ C65), N53 (≠ D66), V54 (= V67), N80 (= N93), A81 (= A94), G82 (= G95), I130 (≠ M143), S132 (= S145), Y145 (= Y158), K149 (= K162), P177 (= P188), G178 (= G189), I180 (= I191), T182 (≠ S193)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
42% identity, 96% coverage: 8:247/250 of query aligns to 3:244/247 of 4jroC
- active site: G16 (= G21), S142 (= S145), Q152 (= Q155), Y155 (= Y158), K159 (= K162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G17), S14 (≠ A19), R15 (≠ Q20), G16 (= G21), I17 (≠ L22), N35 (= N43), Y36 (≠ L44), N37 (≠ D45), G38 (≠ A46), S39 (≠ T47), N63 (≠ D66), V64 (= V67), N90 (= N93), A91 (= A94), I93 (= I96), I113 (≠ V116), S142 (= S145), Y155 (= Y158), K159 (= K162), P185 (= P188), I188 (= I191), T190 (≠ S193)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
42% identity, 96% coverage: 11:250/250 of query aligns to 5:246/246 of 3osuA
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
41% identity, 96% coverage: 11:250/250 of query aligns to 2:239/239 of 3sj7A
- active site: G12 (= G21), S138 (= S145), Q148 (= Q155), Y151 (= Y158), K155 (= K162)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G17), S10 (≠ A19), R11 (≠ Q20), I13 (≠ L22), N31 (= N43), Y32 (≠ L44), A33 (≠ D45), G34 (≠ A46), S35 (≠ T47), A58 (≠ C65), N59 (≠ D66), V60 (= V67), N86 (= N93), A87 (= A94), T109 (≠ V116), S138 (= S145), Y151 (= Y158), K155 (= K162), P181 (= P188), G182 (= G189)
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
42% identity, 97% coverage: 8:250/250 of query aligns to 2:244/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G17), M16 (≠ L22), D35 (= D41), I36 (≠ V42), I62 (≠ V67), N88 (= N93), G90 (= G95), I138 (≠ M143), S140 (= S145), Y152 (= Y158), K156 (= K162), I185 (= I191)
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)
42% identity, 97% coverage: 8:250/250 of query aligns to 3:245/248 of Q9KJF1
- S15 (≠ Q20) binding NAD(+)
- D36 (= D41) binding NAD(+)
- D62 (= D66) binding NAD(+)
- I63 (≠ V67) binding NAD(+)
- N89 (= N93) binding NAD(+)
- Y153 (= Y158) binding NAD(+)
- K157 (= K162) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4cqlI Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD (see paper)
43% identity, 94% coverage: 13:247/250 of query aligns to 11:248/251 of 4cqlI
- active site: G19 (= G21), S146 (= S145), Y159 (= Y158), K163 (= K162)
- binding nicotinamide-adenine-dinucleotide: S18 (≠ Q20), G19 (= G21), I20 (≠ L22), D39 (= D41), L40 (≠ V42), A64 (≠ C65), D65 (= D66), V66 (= V67), C93 (≠ N93), A94 (= A94), G95 (= G95), I96 (= I96), V116 (= V116), I144 (≠ M143), S146 (= S145), Y159 (= Y158), K163 (= K162), P189 (= P188), G190 (= G189), I192 (= I191), T194 (≠ S193), M196 (= M195)
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)
42% identity, 94% coverage: 13:247/250 of query aligns to 14:258/261 of Q92506
- 15:23 (vs. 14:22, 33% identical) binding NAD(+)
- D42 (= D41) 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 (≠ DV 41:42) binding NAD(+)
- ADV 74:76 (≠ CDV 65:67) binding NAD(+)
- R148 (= R137) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- V158 (≠ S147) to L: in a breast cancer sample; somatic mutation
- Y169 (= Y158) 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 158:162) binding NAD(+)
- K173 (= K162) 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 (≠ Y178) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
- IAT 202:204 (≠ IRS 191:193) binding NAD(+)
4cqmA Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
42% identity, 94% coverage: 13:247/250 of query aligns to 9:245/248 of 4cqmA
- active site: G17 (= G21), S143 (= S145), Y156 (= Y158), K160 (= K162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G17), S16 (≠ Q20), G17 (= G21), I18 (≠ L22), D37 (= D41), L38 (≠ V42), A61 (≠ C65), V63 (= V67), C90 (≠ N93), A91 (= A94), G92 (= G95), I93 (= I96), V113 (= V116), I141 (≠ M143), S143 (= S145), Y156 (= Y158), K160 (= K162), P186 (= P188), G187 (= G189), I189 (= I191), T191 (≠ S193), P192 (≠ A194), M193 (= M195), T194 (= T196)
1vl8B Crystal structure of gluconate 5-dehydrogenase (tm0441) from thermotoga maritima at 2.07 a resolution
41% identity, 96% coverage: 8:247/250 of query aligns to 4:248/252 of 1vl8B
- active site: G17 (= G21), S143 (= S145), I154 (≠ Q155), Y157 (= Y158), K161 (= K162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G17), R16 (≠ Q20), G17 (= G21), L18 (= L22), S37 (≠ D41), R38 (≠ V42), C63 (= C65), D64 (= D66), V65 (= V67), A91 (≠ N93), A92 (= A94), G93 (= G95), I94 (= I96), V114 (= V116), I141 (≠ M143), S143 (= S145), Y157 (= Y158), K161 (= K162), P187 (= P188), G188 (= G189), Y190 (≠ I191), T192 (≠ S193), M194 (= M195), T195 (= T196)
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, 99% coverage: 4:250/250 of query aligns to 2:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G17), S17 (≠ A19), R18 (≠ Q20), I20 (≠ L22), T40 (≠ V42), N62 (≠ D66), V63 (= V67), N89 (= N93), A90 (= A94), I92 (= I96), V139 (≠ M143), S141 (= S145), Y154 (= Y158), K158 (= K162), P184 (= P188), G185 (= G189), I187 (= I191), T189 (≠ S193), M191 (= M195)
4k6fB X-ray crystal structure of a putative acetoacetyl-coa reductase from burkholderia cenocepacia bound to the co-factor NADP
40% identity, 96% coverage: 11:250/250 of query aligns to 2:244/245 of 4k6fB
- active site: G12 (= G21), N102 (≠ Q109), S138 (= S145), Y151 (= Y158), K155 (= K162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G17), Y32 (vs. gap), S33 (vs. gap), N36 (≠ D41), V58 (= V63), D59 (= D66), V60 (= V67), A87 (= A94), G88 (= G95), I89 (= I96)
P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
42% identity, 96% coverage: 8:247/250 of query aligns to 4:243/247 of P73574
- A14 (≠ G18) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ V153) 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 (= K162) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ L190) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ P200) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
38% identity, 99% coverage: 4:250/250 of query aligns to 2:242/243 of 4i08A
- active site: G19 (= G21), N113 (≠ H117), S141 (= S145), Q151 (= Q155), Y154 (= Y158), K158 (= K162)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G17), S17 (≠ A19), R18 (≠ Q20), I20 (≠ L22), T40 (≠ V42), N62 (≠ D66), V63 (= V67), N89 (= N93), A90 (= A94), G140 (≠ S144), S141 (= S145), Y154 (= Y158), K158 (= K162), P184 (= P188), G185 (= G189), T189 (≠ S193)
1nfqA Rv2002 gene product from mycobacterium tuberculosis (see paper)
41% identity, 96% coverage: 8:247/250 of query aligns to 4:236/244 of 1nfqA
- active site: G17 (= G21), S139 (= S145), Y152 (= Y158), K156 (= K162)
- binding Androsterone: L91 (≠ T97), E141 (≠ S147), C149 (≠ Q155), Y152 (= Y158), V193 (≠ M199), I197 (= I203), F198 (≠ W204)
- binding 1,4-dihydronicotinamide adenine dinucleotide: R16 (≠ Q20), G17 (= G21), M18 (≠ L22), D37 (= D41), L39 (= L44), L59 (≠ C65), D60 (= D66), V61 (= V67), N87 (= N93), A88 (= A94), I137 (≠ M143), S139 (= S145), Y152 (= Y158), K156 (= K162), P182 (= P188), V185 (≠ I191), T187 (≠ S193), P188 (≠ A194), M189 (= M195), T190 (= T196)
1nffA Crystal structure of rv2002 gene product from mycobacterium tuberculosis (see paper)
41% identity, 96% coverage: 8:247/250 of query aligns to 4:236/244 of 1nffA
- active site: G17 (= G21), S139 (= S145), Y152 (= Y158), K156 (= K162)
- binding nicotinamide-adenine-dinucleotide: G13 (= G17), R16 (≠ Q20), G17 (= G21), M18 (≠ L22), D37 (= D41), I38 (≠ V42), L39 (= L44), L59 (≠ C65), D60 (= D66), V61 (= V67), N87 (= N93), A88 (= A94), G89 (= G95), I90 (= I96), I137 (≠ M143), S139 (= S145), Y152 (= Y158), K156 (= K162), P182 (= P188), V185 (≠ I191), T187 (≠ S193), P188 (≠ A194), M189 (= M195), T190 (= T196)
4nbwA Crystal structure of fabg from plesiocystis pacifica (see paper)
42% identity, 95% coverage: 11:247/250 of query aligns to 2:248/253 of 4nbwA
- active site: G12 (= G21), S146 (= S145), Y159 (= Y158), K163 (= K162)
- binding nicotinamide-adenine-dinucleotide: G8 (= G17), N11 (≠ Q20), G12 (= G21), I13 (≠ L22), D32 (= D41), L33 (≠ V42), V57 (≠ C65), D58 (= D66), V59 (= V67), N85 (= N93), A86 (= A94), G87 (= G95), S146 (= S145), Y159 (= Y158), K163 (= K162), I192 (= I191), T194 (≠ S193)
P9WGT1 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase; NADH-dependent 3alpha, 20beta-hydroxysteroid dehydrogenase; EC 1.1.1.53 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
41% identity, 96% coverage: 8:247/250 of query aligns to 5:237/260 of P9WGT1
- I6 (≠ T9) mutation to T: Maximal improvement in solubility; when associated with M-47 and K-69.
- RGM 17:19 (≠ QGL 20:22) binding NAD(+)
- D38 (= D41) binding NAD(+)
- V47 (≠ E52) mutation to M: Maximal improvement in solubility; when associated with T-6 and K-69.
- DV 61:62 (= DV 66:67) binding NAD(+)
- T69 (≠ D74) mutation to K: Maximal improvement in solubility; when associated with T-6 and M-47.
- N88 (= N93) binding NAD(+)
- S140 (= S145) mutation to A: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- Y153 (= Y158) binding NAD(+); mutation to F: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- K157 (= K162) binding NAD(+)
- 183:191 (vs. 188:196, 56% identical) binding NAD(+)
Query Sequence
>WP_086008421.1 NCBI__GCF_000015305.1:WP_086008421.1
MGEQVSLLTGQTAVITGGAQGLGFAIAQRFVEEGARVVLGDVNLDATVAAAEKLGGEDVA
RAVRCDVTDSAEVDALIAAAVDGFGSLDIMVNNAGITRDATMRKMTEEQFDQVIAVHLKG
TWNGLRAAAAVMREQKRGAIVNMSSISGKVGMVGQTNYSAAKAGIVGMTKAASKELAYLG
VRVNAIQPGLIRSAMTEAMPQRIWDSKVAEVPMGRAGEPEEVANVALFLASDLSSYMTGT
VLEVTGGRHL
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