SitesBLAST
Comparing WP_005456138.1 NCBI__GCF_000244975.1:WP_005456138.1 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)
39% identity, 96% coverage: 6:251/255 of query aligns to 5:241/244 of 4nbuB
- active site: G18 (= G19), N111 (= N116), S139 (= S145), Q149 (≠ R162), Y152 (= Y167), K156 (= K171)
- binding acetoacetyl-coenzyme a: D93 (≠ R98), K98 (≠ T103), S139 (= S145), N146 (≠ G152), V147 (≠ P153), Q149 (≠ R162), Y152 (= Y167), F184 (≠ P199), M189 (≠ L204), K200 (≠ Q215)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), N17 (≠ R18), G18 (= G19), I19 (= I20), D38 (= D39), F39 (≠ L40), V59 (= V64), D60 (= D65), V61 (= V66), N87 (= N92), A88 (= A93), G89 (= G94), I90 (≠ T95), T137 (≠ V143), S139 (= S145), Y152 (= Y167), K156 (= K171), P182 (= P197), F184 (≠ P199), T185 (≠ I200), T187 (= T202), M189 (≠ L204)
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)
43% identity, 96% coverage: 6:251/255 of query aligns to 4:243/247 of P73574
- A14 (≠ G16) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (= P153) 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 (= K171) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ P199) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ T209) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
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)
37% identity, 98% coverage: 6:254/255 of query aligns to 3:245/248 of Q9KJF1
- S15 (≠ R18) binding NAD(+)
- D36 (= D39) binding NAD(+)
- D62 (= D65) binding NAD(+)
- I63 (≠ V66) binding NAD(+)
- N89 (= N92) binding NAD(+)
- Y153 (= Y167) binding NAD(+)
- K157 (= K171) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
37% identity, 98% coverage: 6:254/255 of query aligns to 2:244/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), M16 (≠ I20), D35 (= D39), I36 (≠ L40), I62 (≠ V66), N88 (= N92), G90 (= G94), I138 (≠ V143), S140 (= S145), Y152 (= Y167), K156 (= K171), I185 (= I200)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
40% identity, 94% coverage: 12:251/255 of query aligns to 8:243/246 of 3osuA
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
40% identity, 94% coverage: 12:251/255 of query aligns to 5:236/239 of 3sj7A
- active site: G12 (= G19), S138 (= S145), Q148 (≠ R162), Y151 (= Y167), K155 (= K171)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), S10 (≠ A17), R11 (= R18), I13 (= I20), N31 (≠ D39), Y32 (≠ L40), A33 (= A41), G34 (≠ D42), S35 (≠ P43), A58 (≠ V64), N59 (≠ D65), V60 (= V66), N86 (= N92), A87 (= A93), T109 (= T115), S138 (= S145), Y151 (= Y167), K155 (= K171), P181 (= P197), G182 (= G198)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
37% identity, 96% coverage: 6:251/255 of query aligns to 3:244/247 of 4jroC
- active site: G16 (= G19), S142 (= S145), Q152 (≠ E158), Y155 (= Y167), K159 (= K171)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (≠ A17), R15 (= R18), G16 (= G19), I17 (= I20), N35 (≠ V38), Y36 (≠ D39), N37 (≠ L40), G38 (≠ A41), S39 (≠ D42), N63 (≠ D65), V64 (= V66), N90 (= N92), A91 (= A93), I93 (≠ T95), I113 (≠ T115), S142 (= S145), Y155 (= Y167), K159 (= K171), P185 (= P197), I188 (= I200), T190 (= T202)
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: 4:251/255 of query aligns to 4:243/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (≠ A17), R18 (= R18), I20 (= I20), T40 (≠ D42), N62 (≠ D65), V63 (= V66), N89 (= N92), A90 (= A93), I92 (≠ T95), V139 (= V143), S141 (= S145), Y154 (= Y167), K158 (= K171), P184 (= P197), G185 (= G198), I187 (= I200), T189 (= T202), M191 (≠ V208)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
39% identity, 97% coverage: 4:251/255 of query aligns to 4:239/243 of 4i08A
- active site: G19 (= G19), N113 (= N116), S141 (= S145), Q151 (≠ P165), Y154 (= Y167), K158 (= K171)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (≠ A17), R18 (= R18), I20 (= I20), T40 (≠ D42), N62 (≠ D65), V63 (= V66), N89 (= N92), A90 (= A93), G140 (≠ S144), S141 (= S145), Y154 (= Y167), K158 (= K171), P184 (= P197), G185 (= G198), T189 (= T202)
2d1yA Crystal structure of tt0321 from thermus thermophilus hb8 (see paper)
40% identity, 96% coverage: 6:251/255 of query aligns to 3:235/240 of 2d1yA
- active site: G16 (= G19), S135 (= S145), N145 (≠ G164), Y148 (= Y167), K152 (= K171)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), R15 (= R18), I17 (= I20), D36 (= D39), L37 (= L40), R38 (vs. gap), V55 (= V64), D56 (= D65), L57 (≠ V66), N83 (= N92), A84 (= A93), A85 (≠ G94), I86 (≠ T95), V133 (= V143), S135 (= S145), Y148 (= Y167), K152 (= K171), P178 (= P197), G179 (= G198), I181 (= I200), T183 (= T205), A185 (≠ N207), V186 (= V208)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
37% identity, 96% coverage: 6:251/255 of query aligns to 3:236/239 of 4nbtA
- active site: G16 (= G19), S132 (= S145), Y145 (= Y167), K149 (= K171)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), K15 (≠ R18), G16 (= G19), L17 (≠ I20), D36 (= D39), L37 (= L40), L52 (≠ V64), N53 (≠ D65), V54 (= V66), N80 (= N92), A81 (= A93), G82 (= G94), I130 (≠ V143), S132 (= S145), Y145 (= Y167), K149 (= K171), P177 (= P197), G178 (= G198), I180 (= I200), T182 (= T202)
6d9yB Crystal structure of a short chain dehydrogenase/reductase sdr from burkholderia phymatum with partially occupied NAD
37% identity, 99% coverage: 1:253/255 of query aligns to 2:249/251 of 6d9yB
- active site: G20 (= G19), S145 (= S145), Y158 (= Y167)
- binding nicotinamide-adenine-dinucleotide: G16 (= G15), R19 (= R18), G20 (= G19), D40 (= D39), L41 (= L40), V64 (= V64), D65 (= D65), Q66 (≠ V66), A93 (= A93), S145 (= S145), Y158 (= Y167), K162 (= K171), P188 (= P197), A189 (≠ G198), A190 (≠ P199), A191 (≠ I200), T193 (= T202)
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
41% identity, 96% coverage: 6:251/255 of query aligns to 3:236/240 of 4dmmB
- active site: G16 (= G19), S142 (= S145), Q152 (≠ E158), Y155 (= Y167), K159 (= K171)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (≠ A17), R15 (= R18), G16 (= G19), I17 (= I20), A37 (= A41), S38 (≠ D42), S39 (≠ P43), A62 (≠ V64), D63 (= D65), V64 (= V66), N90 (= N92), A91 (= A93), L113 (≠ T115), I140 (≠ V143), S142 (= S145), Y155 (= Y167), K159 (= K171), P185 (= P197), G186 (= G198), I188 (= I200), T190 (= T202), M192 (≠ L204)
7krmC Putative fabg bound to nadh from acinetobacter baumannii
37% identity, 98% coverage: 6:254/255 of query aligns to 3:243/244 of 7krmC
- active site: G18 (= G19), S140 (= S145), Y155 (= Y167)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), S15 (vs. gap), G18 (= G19), I19 (= I20), D38 (= D39), L39 (= L40), A60 (≠ V64), N61 (≠ D65), V62 (= V66), N88 (= N92), V111 (≠ T115), S140 (= S145), Y155 (= Y167), K159 (= K171), I188 (= I200), T190 (= T202)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
37% identity, 96% coverage: 6:251/255 of query aligns to 8:249/258 of 4wecA
- active site: G21 (= G19), S143 (= S145), Q154 (≠ G164), Y157 (= Y167), K161 (= K171)
- binding nicotinamide-adenine-dinucleotide: G17 (= G15), A19 (= A17), S20 (≠ R18), G21 (= G19), I22 (= I20), D41 (= D39), I42 (≠ L40), V61 (= V64), D62 (= D65), V63 (= V66), N89 (= N92), T141 (≠ V143), Y157 (= Y167), K161 (= K171), P187 (= P197), P189 (= P199), V190 (≠ I200)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
35% identity, 97% coverage: 4:251/255 of query aligns to 4:244/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G15), R18 (= R18), G19 (= G19), I20 (= I20), D39 (= D39), R40 (≠ L40), C63 (≠ V64), I65 (≠ V66), N91 (= N92), G93 (= G94), I94 (≠ T95), V114 (≠ T115), Y155 (= Y167), K159 (= K171), I188 (= I200), T190 (= T202), T193 (= T205)
Q9L9F8 Short-chain reductase protein NovJ; Novobiocin biosynthesis protein J; EC 1.1.1.- from Streptomyces niveus (Streptomyces spheroides) (see paper)
39% identity, 95% coverage: 10:251/255 of query aligns to 18:260/262 of Q9L9F8
- S152 (= S145) mutation to A: 2-3-fold decrease in beta-ketotyrosine product formation.
- Y164 (= Y167) mutation to F: 50-fold reduction in catalytic activity.
- K168 (= K171) mutation to I: Does not alter the catalytic turnover.
1nfqA Rv2002 gene product from mycobacterium tuberculosis (see paper)
38% identity, 98% coverage: 6:255/255 of query aligns to 4:240/244 of 1nfqA
- active site: G17 (= G19), S139 (= S145), Y152 (= Y167), K156 (= K171)
- binding Androsterone: L91 (≠ A96), E141 (≠ S147), C149 (≠ S155), Y152 (= Y167), V193 (= V208), I197 (≠ L212), F198 (≠ D213)
- binding 1,4-dihydronicotinamide adenine dinucleotide: R16 (= R18), G17 (= G19), M18 (≠ I20), D37 (= D39), L39 (≠ A41), L59 (≠ V64), D60 (= D65), V61 (= V66), N87 (= N92), A88 (= A93), I137 (≠ V143), S139 (= S145), Y152 (= Y167), K156 (= K171), P182 (= P197), V185 (≠ I200), T187 (= T202), P188 (≠ A203), M189 (≠ L204), T190 (= T205)
1nffA Crystal structure of rv2002 gene product from mycobacterium tuberculosis (see paper)
38% identity, 98% coverage: 6:255/255 of query aligns to 4:240/244 of 1nffA
- active site: G17 (= G19), S139 (= S145), Y152 (= Y167), K156 (= K171)
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), R16 (= R18), G17 (= G19), M18 (≠ I20), D37 (= D39), I38 (≠ L40), L39 (≠ A41), L59 (≠ V64), D60 (= D65), V61 (= V66), N87 (= N92), A88 (= A93), G89 (= G94), I90 (≠ T95), I137 (≠ V143), S139 (= S145), Y152 (= Y167), K156 (= K171), P182 (= P197), V185 (≠ I200), T187 (= T202), P188 (≠ A203), M189 (≠ L204), T190 (= T205)
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)
38% identity, 98% coverage: 6:255/255 of query aligns to 5:241/260 of P9WGT1
- I6 (≠ T7) mutation to T: Maximal improvement in solubility; when associated with M-47 and K-69.
- RGM 17:19 (≠ RGI 18:20) binding NAD(+)
- D38 (= D39) binding NAD(+)
- V47 (≠ A49) mutation to M: Maximal improvement in solubility; when associated with T-6 and K-69.
- DV 61:62 (= DV 65:66) binding NAD(+)
- T69 (≠ R73) mutation to K: Maximal improvement in solubility; when associated with T-6 and M-47.
- N88 (= N92) 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 (= Y167) 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 (= K171) binding NAD(+)
- 183:191 (vs. 197:205, 44% identical) binding NAD(+)
Query Sequence
>WP_005456138.1 NCBI__GCF_000244975.1:WP_005456138.1
MTVFDLTGRVVLVTGGARGIGAATARVLAGQGADVLVVDLADPVDVASALREEFPGQRFA
SRRVDVRDEDDVRRSVDELVDGFGRIDVLVNNAGTASRSGLDTLTEPEWYRDLDTNLRGT
FLYCRAAVHPHMAGQGSGRIVNVSSISGIMGGPRSGGEGGGRSGPAYAASKGGVIALTKW
LAKEVGPYGITCNSVAPGPIATALTSNVTYALDDQVIKRMGTPEEVGAAVAYLASPGAAY
VTGQVLSVCGGAAIG
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