SitesBLAST
Comparing GFF4128 FitnessBrowser__WCS417:GFF4128 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)
5wuwA Serratia marcescens short-chain dehydrogenase/reductase f98l/f202l mutant (see paper)
70% identity, 98% coverage: 6:248/248 of query aligns to 3:245/245 of 5wuwA
- active site: G16 (= G19), S140 (= S143), Y154 (= Y157), L161 (= L164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), R15 (= R18), I17 (= I20), Y36 (= Y39), A37 (≠ V40), A38 (≠ S41), D63 (= D66), S64 (= S67), N90 (= N93), A91 (= A94), G92 (= G95), Y154 (= Y157), K158 (= K161), G185 (= G188), P186 (= P189), V187 (= V190)
6j7uA Crystal structure of blue fluorescent protein from metagenomic library in complex with NADPH (see paper)
54% identity, 99% coverage: 4:248/248 of query aligns to 1:247/247 of 6j7uA
- active site: G16 (= G19), S142 (= S143), Y156 (= Y157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (= S17), R15 (= R18), I17 (= I20), Y36 (= Y39), V37 (= V40), S38 (= S41), S41 (≠ A44), D65 (= D66), S66 (= S67), N92 (= N93), A93 (= A94), G94 (= G95), I115 (= I116), G141 (= G142), S142 (= S143), Y156 (= Y157), K160 (= K161), P186 (= P187), T191 (= T192), M193 (= M194), N194 (= N195)
5u2wA Crystal structure of a short chain dehydrogenase from burkholderia cenocepacia j2315 in complex with NADP
54% identity, 98% coverage: 6:248/248 of query aligns to 4:246/246 of 5u2wA
- active site: G17 (= G19), S141 (= S143), M152 (≠ G154), Y155 (= Y157), K159 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G15), S15 (= S17), R16 (= R18), G17 (= G19), I18 (= I20), Y37 (= Y39), E38 (≠ V40), K39 (≠ S41), S40 (= S42), A63 (= A65), D64 (= D66), S65 (= S67), N91 (= N93), A92 (= A94), G93 (= G95), T139 (≠ I141), Y155 (= Y157), K159 (= K161), P185 (= P187), G186 (= G188), T188 (≠ V190), T190 (= T192), M192 (= M194), N193 (= N195)
5z2lK Crystal structure of bdca in complex with NADPH (see paper)
50% identity, 98% coverage: 6:248/248 of query aligns to 3:236/244 of 5z2lK
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S14 (= S17), R15 (= R18), I17 (= I20), Y36 (= Y39), A37 (≠ V40), G38 (≠ S41), S39 (= S42), T57 (≠ A65), D58 (= D66), S59 (= S67), N81 (= N93), A82 (= A94), G83 (= G95), I129 (= I141), S131 (= S143), Y145 (= Y157), K149 (= K161), P175 (= P187), I178 (≠ V190), T180 (= T192), A182 (≠ M194), N183 (= N195)
P39333 Cyclic-di-GMP-binding biofilm dispersal mediator protein from Escherichia coli (strain K12) (see paper)
50% identity, 98% coverage: 6:248/248 of query aligns to 4:237/237 of P39333
- E50 (≠ S52) mutation E->Q,V: Shows higher affinity for cyclic-di-GMP, increases swimming motility and biofilm dispersal. Biofilm formation is almost completely removed.
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
38% identity, 98% coverage: 4:247/248 of query aligns to 7:253/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G15), S20 (= S17), K21 (≠ R18), G22 (= G19), I23 (= I20), A43 (≠ V40), S44 (= S41), S45 (= S42), G68 (≠ A65), D69 (= D66), V70 (≠ S67), N96 (= N93), S97 (≠ A94), G98 (= G95), Y100 (≠ L97), I144 (= I141), S146 (= S143), Y159 (= Y157), K163 (= K161), P189 (= P187), G190 (= G188), M191 (≠ P189), I192 (≠ V190), T194 (= T192), G196 (≠ M194), T197 (≠ N195)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S143), Y159 (= Y157), M191 (≠ P189), I202 (vs. gap)
7nm8AAA Antimycin pathway standalone ketoreductase, AntM (see paper)
39% identity, 98% coverage: 3:245/248 of query aligns to 1:247/251 of 7nm8AAA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G13 (= G15), S15 (= S17), R16 (= R18), G17 (= G19), I18 (= I20), H36 (≠ T38), Y37 (= Y39), G38 (≠ V40), H39 (≠ S41), L65 (vs. gap), N97 (= N93), G99 (= G95), S147 (≠ T144), Y160 (= Y157), K164 (= K161), G191 (= G188), T193 (≠ V190), T195 (= T192)
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)
39% identity, 97% coverage: 6:246/248 of query aligns to 4:244/247 of P73574
- A14 (≠ G16) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ G152) 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 (= K161) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ P189) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ S199) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
39% identity, 97% coverage: 6:246/248 of query aligns to 3:245/247 of 4jroC
- active site: G16 (= G19), S142 (= S143), Q152 (≠ G154), Y155 (= Y157), K159 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (= S17), R15 (= R18), G16 (= G19), I17 (= I20), N35 (≠ T38), Y36 (= Y39), N37 (≠ V40), G38 (≠ S41), S39 (= S42), N63 (≠ D66), V64 (≠ S67), N90 (= N93), A91 (= A94), I93 (≠ V96), I113 (= I116), S142 (= S143), Y155 (= Y157), K159 (= K161), P185 (= P187), I188 (≠ V190), T190 (= T192)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
38% identity, 96% coverage: 9:246/248 of query aligns to 5:244/246 of 3osuA
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
42% identity, 97% coverage: 6:246/248 of query aligns to 3:237/240 of 4dmmB
- active site: G16 (= G19), S142 (= S143), Q152 (≠ G154), Y155 (= Y157), K159 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (= S17), R15 (= R18), G16 (= G19), I17 (= I20), A37 (≠ V40), S38 (= S41), S39 (= S42), A62 (= A65), D63 (= D66), V64 (≠ S67), N90 (= N93), A91 (= A94), L113 (≠ I116), I140 (= I141), S142 (= S143), Y155 (= Y157), K159 (= K161), P185 (= P187), G186 (= G188), I188 (≠ V190), T190 (= T192), M192 (= M194)
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)
39% identity, 98% coverage: 5:246/248 of query aligns to 5:244/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (= S17), R18 (= R18), I20 (= I20), T40 (≠ S41), N62 (≠ H64), V63 (≠ A65), N89 (= N93), A90 (= A94), I92 (≠ V96), V139 (≠ I141), S141 (= S143), Y154 (= Y157), K158 (= K161), P184 (= P187), G185 (= G188), I187 (≠ V190), T189 (= T192), M191 (= M194)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
37% identity, 96% coverage: 9:246/248 of query aligns to 2:237/239 of 3sj7A
- active site: G12 (= G19), S138 (= S143), Q148 (≠ G154), Y151 (= Y157), K155 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), S10 (= S17), R11 (= R18), I13 (= I20), N31 (≠ T38), Y32 (= Y39), A33 (≠ V40), G34 (≠ S41), S35 (= S42), A58 (= A65), N59 (≠ D66), V60 (≠ S67), N86 (= N93), A87 (= A94), T109 (≠ I116), S138 (= S143), Y151 (= Y157), K155 (= K161), P181 (= P187), G182 (= G188)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
39% identity, 98% coverage: 5:246/248 of query aligns to 5:240/243 of 4i08A
- active site: G19 (= G19), N113 (= N117), S141 (= S143), Q151 (≠ G154), Y154 (= Y157), K158 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (= S17), R18 (= R18), I20 (= I20), T40 (≠ S41), N62 (≠ H64), V63 (≠ A65), N89 (= N93), A90 (= A94), G140 (= G142), S141 (= S143), Y154 (= Y157), K158 (= K161), P184 (= P187), G185 (= G188), T189 (= T192)
3iccA Crystal structure of a putative 3-oxoacyl-(acyl carrier protein) reductase from bacillus anthracis at 1.87 a resolution (see paper)
37% identity, 97% coverage: 6:245/248 of query aligns to 5:252/255 of 3iccA
- active site: G18 (= G19), S148 (= S143), F158 (≠ G154), Y161 (= Y157), K165 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G15), S16 (= S17), R17 (= R18), G18 (= G19), I19 (= I20), H37 (≠ T38), Y38 (= Y39), G39 (≠ V40), L66 (vs. gap), E67 (vs. gap), N98 (= N93), G100 (= G95), I146 (= I141), S148 (= S143), Y161 (= Y157), K165 (= K161), P191 (= P187), G192 (= G188), M198 (= M194), N199 (= N195)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
39% identity, 98% coverage: 5:246/248 of query aligns to 1:240/243 of 1q7bA
- active site: G15 (= G19), E101 (≠ D109), S137 (= S143), Q147 (≠ G154), Y150 (= Y157), K154 (= K161)
- binding calcium ion: E232 (≠ A238), T233 (≠ S239)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (= S17), R14 (= R18), T36 (≠ V40), N58 (≠ H64), V59 (≠ A65), N85 (= N93), A86 (= A94), G87 (= G95), I88 (≠ V96), S137 (= S143), Y150 (= Y157), K154 (= K161), P180 (= P187), G181 (= G188), I183 (≠ V190)
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)
39% identity, 98% coverage: 5:246/248 of query aligns to 2:241/244 of P0AEK2
- GASR 12:15 (≠ GGSR 15:18) binding
- T37 (≠ V40) binding
- NV 59:60 (≠ HA 64:65) binding
- N86 (= N93) binding
- Y151 (= Y157) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YAMSK 157:161) binding
- A154 (≠ S160) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K161) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ V190) binding
- E233 (≠ A238) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
1nfqA Rv2002 gene product from mycobacterium tuberculosis (see paper)
37% identity, 97% coverage: 5:245/248 of query aligns to 3:236/244 of 1nfqA
- active site: G17 (= G19), S139 (= S143), Y152 (= Y157), K156 (= K161)
- binding Androsterone: L91 (= L97), E141 (≠ N145), C149 (≠ G153), Y152 (= Y157), V193 (≠ A202), I197 (= I206), F198 (≠ G207)
- binding 1,4-dihydronicotinamide adenine dinucleotide: R16 (= R18), G17 (= G19), M18 (≠ I20), D37 (≠ Y39), L39 (≠ S41), L59 (≠ A65), D60 (= D66), V61 (≠ S67), N87 (= N93), A88 (= A94), I137 (= I141), S139 (= S143), Y152 (= Y157), K156 (= K161), P182 (= P187), V185 (= V190), T187 (= T192), P188 (≠ D193), M189 (= M194), T190 (≠ S199)
1nffA Crystal structure of rv2002 gene product from mycobacterium tuberculosis (see paper)
37% identity, 97% coverage: 5:245/248 of query aligns to 3:236/244 of 1nffA
- active site: G17 (= G19), S139 (= S143), Y152 (= Y157), K156 (= K161)
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), R16 (= R18), G17 (= G19), M18 (≠ I20), D37 (≠ Y39), I38 (≠ V40), L39 (≠ S41), L59 (≠ A65), D60 (= D66), V61 (≠ S67), N87 (= N93), A88 (= A94), G89 (= G95), I90 (≠ V96), I137 (= I141), S139 (= S143), Y152 (= Y157), K156 (= K161), P182 (= P187), V185 (= V190), T187 (= T192), P188 (≠ D193), M189 (= M194), T190 (≠ S199)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
39% identity, 98% coverage: 5:246/248 of query aligns to 1:240/243 of 1q7cA
- active site: G15 (= G19), S137 (= S143), Q147 (≠ G154), F150 (≠ Y157), K154 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G15), S13 (= S17), R14 (= R18), A35 (≠ Y39), T36 (≠ V40), L57 (≠ I63), N58 (≠ H64), V59 (≠ A65), G87 (= G95), I88 (≠ V96)
Query Sequence
>GFF4128 FitnessBrowser__WCS417:GFF4128
MTTQNLSGKVALIQGGSRGIGAAIVKRLAAQGAAVAFTYVSSVAKAEELQNSVISEGGKA
LAIHADSADAGAIRNAVNATVEAFGRLDILVNNAGVLAIAPLEDFKLEDFDQTLAINVRS
VFIATQEAAKHMADGGRVINIGSTNAERMPFGGGGPYAMSKAALVGLTKGLARDLGPRGI
TINNVQPGPVDTDMNPANSDFAESLIGLMAVGRYGHVEEIASFVAYLAGPEAGYITGASL
TIDGGFSA
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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