SitesBLAST
Comparing WP_035219698.1 NCBI__GCF_000429905.1:WP_035219698.1 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)
4fw8A Crystal structure of fabg4 complexed with coenzyme nadh (see paper)
49% identity, 80% coverage: 95:479/479 of query aligns to 41:427/427 of 4fw8A
- active site: S320 (= S372), Y333 (= Y385), K337 (= K389)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G193 (= G246), R196 (= R249), I198 (= I251), D217 (= D270), L239 (≠ C292), V241 (≠ I294), N268 (= N322), A269 (= A323), G270 (= G324), L318 (= L370), Y333 (= Y385), K337 (= K389), P363 (= P415)
3q6iA Crystal structure of fabg4 and coenzyme binary complex
49% identity, 80% coverage: 95:479/479 of query aligns to 41:427/427 of 3q6iA
- active site: S320 (= S372), Y333 (= Y385), K337 (= K389)
- binding nicotinamide-adenine-dinucleotide: G193 (= G246), I198 (= I251), D217 (= D270), L239 (≠ C292), D240 (= D293), V241 (≠ I294), N268 (= N322), A269 (= A323), G270 (= G324), L318 (= L370), Y333 (= Y385), K337 (= K389), P363 (= P415), T368 (= T420)
I6Y778 3-oxoacyl-[acyl-carrier-protein] reductase [NADH]; Beta-ketoacyl CoA reductase; FASII-like 3-oxoacyl-thioester reductase; HMwFabG; EC 1.1.1.212 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
50% identity, 77% coverage: 109:479/479 of query aligns to 82:454/454 of I6Y778
- R146 (≠ K173) mutation to A: 2.2-fold decrease in catalytic efficiency with NADH as substrate. 26-fold decrease in catalytic efficiency; when associated with A-445.
- RGI 223:225 (= RGI 249:251) binding NAD(+)
- D244 (= D270) binding NAD(+)
- DV 267:268 (≠ DI 293:294) binding NAD(+)
- NAG 295:297 (= NAG 322:324) binding NAD(+)
- KLLAN 302:306 (≠ KMLAN 329:333) binding substrate
- N354 (= N379) binding substrate
- Y360 (= Y385) binding NAD(+)
- K364 (= K389) binding NAD(+)
- T395 (= T420) binding NAD(+)
- R445 (= R470) mutation to A: 12-fold decrease in catalytic efficiency with NADH as substrate. 26-fold decrease in catalytic efficiency; when associated with A-146.
- QAMIGA 449:454 (≠ QNFIGA 474:479) mutation Missing: Drastic reduction of ketoreductase activity.
3v1uA Crystal structure of a beta-ketoacyl reductase fabg4 from mycobacterium tuberculosis h37rv complexed with NAD+ and hexanoyl-coa at 2.5 angstrom resolution (see paper)
49% identity, 77% coverage: 109:479/479 of query aligns to 47:416/416 of 3v1uA
- active site: S312 (= S372), Y325 (= Y385), K329 (= K389)
- binding hexanoyl-coenzyme a: G262 (= G324), K267 (= K329), L268 (≠ M330), N271 (= N333), N319 (= N379)
- binding nicotinamide-adenine-dinucleotide: G185 (= G246), R188 (= R249), G189 (= G250), I190 (= I251), D209 (= D270), V210 (≠ R271), D232 (= D293), V233 (≠ I294), N260 (= N322), A261 (= A323), I263 (≠ V325), V283 (≠ I345), S312 (= S372), Y325 (= Y385), K329 (= K389), P355 (= P415), G356 (= G416), Q361 (= Q421)
5vp5A Crystal structure of a 3-oxoacyl-acyl-carrier protein reductase fabg4 from mycobacterium smegmatis bound to NAD
46% identity, 77% coverage: 109:479/479 of query aligns to 53:411/411 of 5vp5A
- active site: S318 (= S372), Y331 (= Y385), K335 (= K389)
- binding nicotinamide-adenine-dinucleotide: G191 (= G246), R194 (= R249), I196 (= I251), D215 (= D270), V216 (≠ R271), D238 (= D293), V239 (≠ I294), N266 (= N322), A267 (= A323), I269 (≠ V325), S318 (= S372), Y331 (= Y385), K335 (= K389), P361 (= P415)
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)
43% identity, 50% coverage: 237:477/479 of query aligns to 6:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G246), S17 (≠ A248), R18 (= R249), I20 (= I251), T40 (≠ M269), N62 (= N291), V63 (≠ I294), N89 (= N322), A90 (= A323), I92 (≠ V325), V139 (≠ L370), S141 (= S372), Y154 (= Y385), K158 (= K389), P184 (= P415), G185 (= G416), I187 (= I418), T189 (= T420), M191 (= M422)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
41% identity, 50% coverage: 240:477/479 of query aligns to 6:243/244 of 6t77A
- active site: G16 (= G250), S138 (= S372), Y151 (= Y385)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G246), S14 (≠ A248), R15 (= R249), T37 (≠ M269), L58 (≠ C292), N59 (≠ D293), V60 (≠ I294), A87 (= A323), G88 (= G324), I89 (≠ V325)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
42% identity, 50% coverage: 237:477/479 of query aligns to 6:242/243 of 4i08A
- active site: G19 (= G250), N113 (= N346), S141 (= S372), Q151 (= Q382), Y154 (= Y385), K158 (= K389)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G246), S17 (≠ A248), R18 (= R249), I20 (= I251), T40 (≠ M269), N62 (= N291), V63 (≠ I294), N89 (= N322), A90 (= A323), G140 (≠ S371), S141 (= S372), Y154 (= Y385), K158 (= K389), P184 (= P415), G185 (= G416), T189 (= T420)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
39% identity, 49% coverage: 237:473/479 of query aligns to 5:240/244 of 4nbuB
- active site: G18 (= G250), N111 (= N346), S139 (= S372), Q149 (= Q382), Y152 (= Y385), K156 (= K389)
- binding acetoacetyl-coenzyme a: D93 (= D328), K98 (≠ N333), S139 (= S372), N146 (= N379), V147 (= V380), Q149 (= Q382), Y152 (= Y385), F184 (= F417), M189 (= M422), K200 (≠ A433)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G246), N17 (≠ R249), G18 (= G250), I19 (= I251), D38 (= D270), F39 (≠ R271), V59 (≠ C292), D60 (= D293), V61 (≠ I294), N87 (= N322), A88 (= A323), G89 (= G324), I90 (≠ V325), T137 (≠ L370), S139 (= S372), Y152 (= Y385), K156 (= K389), P182 (= P415), F184 (= F417), T185 (≠ I418), T187 (= T420), M189 (= M422)
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)
42% identity, 50% coverage: 240:477/479 of query aligns to 6:243/244 of P0A2C9
- M125 (= M361) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A457) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S458) 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.
4ag3A Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with NADPH at 1.8a resolution (see paper)
43% identity, 51% coverage: 236:477/479 of query aligns to 9:253/254 of 4ag3A
- active site: G23 (= G250), S148 (= S372), Y161 (= Y385), K165 (= K389)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G246), S21 (≠ A248), R22 (= R249), G23 (= G250), I24 (= I251), T44 (≠ M269), L68 (≠ C292), D69 (= D293), V70 (≠ I294), N96 (= N322), A97 (= A323), I146 (≠ L370), S148 (= S372), Y161 (= Y385), K165 (= K389), P191 (= P415), G192 (= G416), F193 (= F417), I194 (= I418), T196 (= T420), M198 (= M422), T199 (= T423)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
41% identity, 50% coverage: 240:477/479 of query aligns to 5:242/243 of 1q7bA
- active site: G15 (= G250), E101 (≠ R338), S137 (= S372), Q147 (= Q382), Y150 (= Y385), K154 (= K389)
- binding calcium ion: E232 (≠ G467), T233 (≠ V468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G246), S13 (≠ A248), R14 (= R249), T36 (≠ M269), N58 (≠ D293), V59 (≠ I294), N85 (= N322), A86 (= A323), G87 (= G324), I88 (≠ V325), S137 (= S372), Y150 (= Y385), K154 (= K389), P180 (= P415), G181 (= G416), I183 (= I418)
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)
41% identity, 50% coverage: 240:477/479 of query aligns to 6:243/244 of P0AEK2
- GASR 12:15 (≠ GAAR 246:249) binding NADP(+)
- T37 (≠ M269) binding NADP(+)
- NV 59:60 (≠ DI 293:294) binding NADP(+)
- N86 (= N322) binding NADP(+)
- Y151 (= Y385) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YAASK 385:389) binding NADP(+)
- A154 (≠ S388) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K389) mutation to A: Defect in the affinity for NADPH.
- I184 (= I418) binding NADP(+)
- E233 (≠ G467) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
6wprA Crystal structure of a putative 3-oxoacyl-acp reductase (fabg) with NADP(h) from acinetobacter baumannii (see paper)
41% identity, 49% coverage: 240:473/479 of query aligns to 6:239/244 of 6wprA
- active site: G16 (= G250), S138 (= S372), Y151 (= Y385)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G246), S14 (≠ A248), R15 (= R249), T37 (≠ M269), L58 (≠ C292), D59 (= D293), V60 (≠ I294), N86 (= N322), A87 (= A323), G88 (= G324), I89 (≠ V325), I136 (≠ L370), Y151 (= Y385), K155 (= K389), P181 (= P415)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
41% identity, 50% coverage: 240:477/479 of query aligns to 5:242/243 of 1q7cA
- active site: G15 (= G250), S137 (= S372), Q147 (= Q382), F150 (≠ Y385), K154 (= K389)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G246), S13 (≠ A248), R14 (= R249), A35 (≠ V268), T36 (≠ M269), L57 (≠ C292), N58 (≠ D293), V59 (≠ I294), G87 (= G324), I88 (≠ V325)
6t62A Crystal structure of acinetobacter baumannii fabg in complex with NADPH at 1.8 a resolution (see paper)
41% identity, 49% coverage: 240:473/479 of query aligns to 6:239/244 of 6t62A
- active site: G16 (= G250), S138 (= S372), Y151 (= Y385)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G246), S14 (≠ A248), R15 (= R249), A36 (≠ V268), T37 (≠ M269), L58 (≠ C292), D59 (= D293), V60 (≠ I294), N86 (= N322), A87 (= A323), G88 (= G324), I89 (≠ V325), I136 (≠ L370), S137 (= S371), S138 (= S372), Y151 (= Y385), K155 (= K389), P181 (= P415), G182 (= G416), I184 (= I418), M188 (= M422)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
38% identity, 50% coverage: 240:477/479 of query aligns to 5:242/243 of 7emgB
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)
42% identity, 51% coverage: 236:477/479 of query aligns to 15:254/255 of 4bo4C
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
39% identity, 49% coverage: 240:473/479 of query aligns to 6:243/247 of 4jroC
- active site: G16 (= G250), S142 (= S372), Q152 (= Q382), Y155 (= Y385), K159 (= K389)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G246), S14 (≠ A248), R15 (= R249), G16 (= G250), I17 (= I251), N35 (≠ M269), Y36 (vs. gap), N37 (vs. gap), G38 (≠ D270), S39 (≠ R271), N63 (≠ D293), V64 (≠ I294), N90 (= N322), A91 (= A323), I93 (≠ V325), I113 (= I345), S142 (= S372), Y155 (= Y385), K159 (= K389), P185 (= P415), I188 (= I418), T190 (= T420)
4bnzA Crystal structure of 3-oxoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with 1-methyl-n-phenylindole- 3-carboxamide at 2.5a resolution (see paper)
41% identity, 50% coverage: 237:477/479 of query aligns to 5:240/241 of 4bnzA
Query Sequence
>WP_035219698.1 NCBI__GCF_000429905.1:WP_035219698.1
MGDILLELGKKDAARKVVKNLGLPLPLPQELSRPKGPWEEMPLLDVNAAVGHLPGSELAP
QIAQALGGMGAMVHAAADSKKFSHYQKQGTARGRLAKALDMDAKPEGLNFRVLIFDATGV
SDPAELEMMYEFFNTKIRSLSPCGRLIVLGRPADELEDISQAAASRALLGFVKSAGKEIG
KKGATSQAIYVEKGAEDRLEPVLRFFLSDRSAYVSGQMVRVSAKVKAPESFTNIRPLDVK
IALVTGAARGIGEQIARTMAGEGARVIVMDRPGEEDLTSKLARKINGSALNCDITASDAP
KAIKDHIAENYGKKGLDVIVHNAGVTRDKMLANMDADRWNMVMNINLLALIASTKELLKI
MPDNGRIVCLSSIAGIAGNVGQTNYAASKAGVIGFVEALAPTVADRGITVNAVAPGFIET
QMTAAIPFATREAGRRLASLSQGGLPQDVAQVVTFLASPQASGVTGGVLRICGQNFIGA
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