SitesBLAST
Comparing Pf1N1B4_1271 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1271 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)
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)
48% identity, 100% coverage: 2:450/450 of query aligns to 7:454/454 of I6Y778
- R146 (= R150) 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 223:225) binding
- D244 (= D244) binding
- DV 267:268 (≠ DI 267:268) binding
- NAG 295:297 (= NAG 291:293) binding
- KLLAN 302:306 (≠ KTLAN 298:302) binding
- N354 (= N350) binding
- Y360 (= Y356) binding
- K364 (= K360) binding
- T395 (= T391) binding
- R445 (= R441) 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 (≠ QSVLGA 445:450) mutation Missing: Drastic reduction of ketoreductase activity.
4fw8A Crystal structure of fabg4 complexed with coenzyme nadh (see paper)
49% identity, 96% coverage: 21:450/450 of query aligns to 7:427/427 of 4fw8A
- active site: S320 (= S343), Y333 (= Y356), K337 (= K360)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G193 (= G220), R196 (= R223), I198 (= I225), D217 (= D244), L239 (= L266), V241 (≠ I268), N268 (= N291), A269 (= A292), G270 (= G293), L318 (= L341), Y333 (= Y356), K337 (= K360), P363 (= P386)
3q6iA Crystal structure of fabg4 and coenzyme binary complex
49% identity, 96% coverage: 21:450/450 of query aligns to 7:427/427 of 3q6iA
- active site: S320 (= S343), Y333 (= Y356), K337 (= K360)
- binding nicotinamide-adenine-dinucleotide: G193 (= G220), I198 (= I225), D217 (= D244), L239 (= L266), D240 (= D267), V241 (≠ I268), N268 (= N291), A269 (= A292), G270 (= G293), L318 (= L341), Y333 (= Y356), K337 (= K360), P363 (= P386), T368 (= T391)
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, 95% coverage: 24:450/450 of query aligns to 1:416/416 of 3v1uA
- active site: S312 (= S343), Y325 (= Y356), K329 (= K360)
- binding hexanoyl-coenzyme a: G262 (= G293), K267 (= K298), L268 (≠ T299), N271 (= N302), N319 (= N350)
- binding nicotinamide-adenine-dinucleotide: G185 (= G220), R188 (= R223), G189 (= G224), I190 (= I225), D209 (= D244), V210 (= V245), D232 (= D267), V233 (≠ I268), N260 (= N291), A261 (= A292), I263 (= I294), V283 (= V314), S312 (= S343), Y325 (= Y356), K329 (= K360), P355 (= P386), G356 (= G387), Q361 (= Q392)
5vp5A Crystal structure of a 3-oxoacyl-acyl-carrier protein reductase fabg4 from mycobacterium smegmatis bound to NAD
48% identity, 94% coverage: 26:450/450 of query aligns to 2:411/411 of 5vp5A
- active site: S318 (= S343), Y331 (= Y356), K335 (= K360)
- binding nicotinamide-adenine-dinucleotide: G191 (= G220), R194 (= R223), I196 (= I225), D215 (= D244), V216 (= V245), D238 (= D267), V239 (≠ I268), N266 (= N291), A267 (= A292), I269 (= I294), S318 (= S343), Y331 (= Y356), K335 (= K360), P361 (= P386)
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)
41% identity, 52% coverage: 211:444/450 of query aligns to 6:242/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G220), S17 (≠ A222), R18 (= R223), I20 (= I225), T40 (≠ P247), N62 (≠ D267), V63 (≠ I268), N89 (= N291), A90 (= A292), I92 (= I294), V139 (≠ L341), S141 (= S343), Y154 (= Y356), K158 (= K360), P184 (= P386), G185 (= G387), I187 (= I389), T189 (= T391), M191 (= M393)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
40% identity, 52% coverage: 211:444/450 of query aligns to 5:240/244 of 4nbuB
- active site: G18 (= G224), N111 (= N315), S139 (= S343), Q149 (= Q353), Y152 (= Y356), K156 (= K360)
- binding acetoacetyl-coenzyme a: D93 (= D297), K98 (≠ N302), S139 (= S343), N146 (= N350), V147 (≠ R351), Q149 (= Q353), Y152 (= Y356), F184 (= F388), M189 (= M393), K200 (≠ A404)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G220), N17 (≠ R223), G18 (= G224), I19 (= I225), D38 (= D244), F39 (≠ V245), V59 (≠ L266), D60 (= D267), V61 (≠ I268), N87 (= N291), A88 (= A292), G89 (= G293), I90 (= I294), T137 (≠ L341), S139 (= S343), Y152 (= Y356), K156 (= K360), P182 (= P386), F184 (= F388), T185 (≠ I389), T187 (= T391), M189 (= M393)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
40% identity, 52% coverage: 211:444/450 of query aligns to 6:238/243 of 4i08A
- active site: G19 (= G224), N113 (= N315), S141 (= S343), Q151 (= Q353), Y154 (= Y356), K158 (= K360)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G220), S17 (≠ A222), R18 (= R223), I20 (= I225), T40 (≠ P247), N62 (≠ D267), V63 (≠ I268), N89 (= N291), A90 (= A292), G140 (≠ A342), S141 (= S343), Y154 (= Y356), K158 (= K360), P184 (= P386), G185 (= G387), T189 (= T391)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
39% identity, 52% coverage: 210:444/450 of query aligns to 2:239/244 of 6t77A
- active site: G16 (= G224), S138 (= S343), Y151 (= Y356)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G220), S14 (≠ A222), R15 (= R223), T37 (≠ P247), L58 (= L266), N59 (≠ D267), V60 (≠ I268), A87 (= A292), G88 (= G293), I89 (= I294)
4ag3A Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with NADPH at 1.8a resolution (see paper)
42% identity, 53% coverage: 208:444/450 of query aligns to 7:249/254 of 4ag3A
- active site: G23 (= G224), S148 (= S343), Y161 (= Y356), K165 (= K360)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G220), S21 (≠ A222), R22 (= R223), G23 (= G224), I24 (= I225), T44 (≠ V245), L68 (= L266), D69 (= D267), V70 (≠ I268), N96 (= N291), A97 (= A292), I146 (≠ L341), S148 (= S343), Y161 (= Y356), K165 (= K360), P191 (= P386), G192 (= G387), F193 (= F388), I194 (= I389), T196 (= T391), M198 (= M393), T199 (= T394)
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)
40% identity, 52% coverage: 211:444/450 of query aligns to 3:239/244 of P0AEK2
- GASR 12:15 (≠ GAAR 220:223) binding
- T37 (≠ P247) binding
- NV 59:60 (≠ DI 267:268) binding
- N86 (= N291) binding
- Y151 (= Y356) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YAASK 356:360) binding
- A154 (≠ S359) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K360) mutation to A: Defect in the affinity for NADPH.
- I184 (= I389) binding
- E233 (≠ Q438) 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)
40% identity, 52% coverage: 211:444/450 of query aligns to 2:238/243 of 1q7bA
- active site: G15 (= G224), E101 (≠ F307), S137 (= S343), Q147 (= Q353), Y150 (= Y356), K154 (= K360)
- binding calcium ion: E232 (≠ Q438), T233 (≠ A439)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G220), S13 (≠ A222), R14 (= R223), T36 (≠ P247), N58 (≠ D267), V59 (≠ I268), N85 (= N291), A86 (= A292), G87 (= G293), I88 (= I294), S137 (= S343), Y150 (= Y356), K154 (= K360), P180 (= P386), G181 (= G387), I183 (= I389)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
40% identity, 52% coverage: 211:444/450 of query aligns to 2:238/243 of 1q7cA
- active site: G15 (= G224), S137 (= S343), Q147 (= Q353), F150 (≠ Y356), K154 (= K360)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G220), S13 (≠ A222), R14 (= R223), A35 (≠ P246), T36 (≠ P247), L57 (= L266), N58 (≠ D267), V59 (≠ I268), G87 (= G293), I88 (= I294)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
39% identity, 53% coverage: 210:448/450 of query aligns to 2:247/247 of 4jroC
- active site: G16 (= G224), S142 (= S343), Q152 (= Q353), Y155 (= Y356), K159 (= K360)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G220), S14 (≠ A222), R15 (= R223), G16 (= G224), I17 (= I225), N35 (≠ D244), Y36 (≠ V245), N37 (≠ P246), G38 (≠ P247), S39 (≠ A248), N63 (≠ D272), V64 (≠ A273), N90 (= N291), A91 (= A292), I93 (= I294), I113 (≠ V314), S142 (= S343), Y155 (= Y356), K159 (= K360), P185 (= P386), I188 (= I389), T190 (= T391)
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)
39% identity, 52% coverage: 210:444/450 of query aligns to 2:239/244 of P0A2C9
- M125 (≠ G330) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A428) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (≠ Q429) 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)
39% identity, 52% coverage: 210:444/450 of query aligns to 1:238/243 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, 53% coverage: 208:444/450 of query aligns to 13:250/255 of 4bo4C
6wprA Crystal structure of a putative 3-oxoacyl-acp reductase (fabg) with NADP(h) from acinetobacter baumannii (see paper)
36% identity, 51% coverage: 214:444/450 of query aligns to 6:239/244 of 6wprA
- active site: G16 (= G224), S138 (= S343), Y151 (= Y356)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G220), S14 (≠ A222), R15 (= R223), T37 (≠ P247), L58 (= L266), D59 (= D267), V60 (≠ I268), N86 (= N291), A87 (= A292), G88 (= G293), I89 (= I294), I136 (≠ L341), Y151 (= Y356), K155 (= K360), P181 (= P386)
6t62A Crystal structure of acinetobacter baumannii fabg in complex with NADPH at 1.8 a resolution (see paper)
36% identity, 51% coverage: 214:444/450 of query aligns to 6:239/244 of 6t62A
- active site: G16 (= G224), S138 (= S343), Y151 (= Y356)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G220), S14 (≠ A222), R15 (= R223), A36 (≠ P246), T37 (≠ P247), L58 (= L266), D59 (= D267), V60 (≠ I268), N86 (= N291), A87 (= A292), G88 (= G293), I89 (= I294), I136 (≠ L341), S137 (≠ A342), S138 (= S343), Y151 (= Y356), K155 (= K360), P181 (= P386), G182 (= G387), I184 (= I389), M188 (= M393)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
38% identity, 53% coverage: 210:448/450 of query aligns to 5:247/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G220), R18 (= R223), G19 (= G224), I20 (= I225), D39 (= D244), R40 (≠ A248), C63 (≠ L266), I65 (= I268), N91 (= N291), G93 (= G293), I94 (= I294), V114 (= V314), Y155 (= Y356), K159 (= K360), I188 (= I389), T190 (= T391), T193 (= T394)
Query Sequence
>Pf1N1B4_1271 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1271
MSDRYIDFANSSIGHRVVGALGLPSPVRLERWQAGRLRPIEGALLIGGGPLAEKVSTLAN
RLTDTIYSYGTDPTLASAWIPGHGQKLKAVVYDASDLVQVDQLKQLREFFQPLMKNLDHH
AHLVILGRAPETLSDPFAASAQRALEGFSRSLAKELRSGGTLQLIYVGEGAEDQLEGPLR
FFLSPKSAFISGQVIRLKACDAQVMDWSRPLSGRKALVTGAARGIGASIAETLARDGAEV
ILLDVPPAKADLEALAARLGGRGITLDICAEDAATQLIEHLPDGIDIVIHNAGITRDKTL
ANMTPEFWDAVLAVNLNAPQVLTKALLDSGTLRDNGRVILLASISGIAGNRGQTNYAASK
AGLIGLAQAWAPLLSERGISINAVAPGFIETQMTAHLPFGVREAGRRMSSLGQGGLPQDV
AEAVAWLAQPGTGAFTGQALRVCGQSVLGA
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