SitesBLAST
Comparing BPHYT_RS28250 FitnessBrowser__BFirm:BPHYT_RS28250 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)
6d9yB Crystal structure of a short chain dehydrogenase/reductase sdr from burkholderia phymatum with partially occupied NAD
89% identity, 100% coverage: 1:250/250 of query aligns to 2:251/251 of 6d9yB
- active site: G20 (= G19), S145 (= S144), Y158 (= Y157)
- binding nicotinamide-adenine-dinucleotide: G16 (= G15), R19 (= R18), G20 (= G19), D40 (= D39), L41 (≠ V40), V64 (= V63), D65 (≠ E64), Q66 (≠ L65), A93 (= A92), S145 (= S144), Y158 (= Y157), K162 (= K161), P188 (= P187), A189 (= A188), A190 (= A189), A191 (= A190), T193 (= T192)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
35% identity, 96% coverage: 6:246/250 of query aligns to 3:244/248 of 6ixmC
- active site: G16 (= G19), S142 (= S144), Y155 (= Y157), K159 (= K161)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), S15 (≠ R18), G16 (= G19), I17 (= I20), D36 (= D39), I37 (≠ V40), A61 (≠ V63), D62 (≠ E64), T63 (≠ L65), N89 (≠ C91), A90 (= A92), M140 (≠ I142), S142 (= S144), Y155 (= Y157), K159 (= K161), P185 (= P187), A186 (= A188), Y187 (≠ A189), I188 (≠ A190), L192 (≠ I194)
5ts3A Crystal structure of a 3-oxoacyl-[acyl-carrier protein] reductase with bound NAD from brucella melitensis
39% identity, 95% coverage: 9:246/250 of query aligns to 20:261/265 of 5ts3A
- active site: G30 (= G19), S158 (= S144), V168 (≠ N153), Y172 (= Y157), K176 (= K161)
- binding nicotinamide-adenine-dinucleotide: G26 (= G15), R29 (= R18), G30 (= G19), I31 (= I20), D50 (= D39), L51 (≠ V40), D77 (≠ E68), V78 (≠ A69), N101 (≠ C91), V129 (= V115), T156 (≠ I142), Y172 (= Y157), K176 (= K161), P202 (= P187), I205 (≠ A190), T207 (= T192)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
37% identity, 96% coverage: 6:246/250 of query aligns to 3:236/239 of 4nbtA
- active site: G16 (= G19), S132 (= S144), Y145 (= Y157), K149 (= K161)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), K15 (≠ R18), G16 (= G19), L17 (≠ I20), D36 (= D39), L37 (≠ V40), L52 (≠ V63), N53 (≠ E64), V54 (≠ L65), N80 (≠ C91), A81 (= A92), G82 (= G93), I130 (= I142), S132 (= S144), Y145 (= Y157), K149 (= K161), P177 (= P187), G178 (≠ A188), I180 (≠ A190), T182 (= T192)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
35% identity, 96% coverage: 6:246/250 of query aligns to 3:244/247 of 4jroC
- active site: G16 (= G19), S142 (= S144), Q152 (≠ A154), Y155 (= Y157), K159 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (≠ A17), R15 (= R18), G16 (= G19), I17 (= I20), N35 (vs. gap), Y36 (≠ W38), N37 (≠ D39), G38 (≠ V40), S39 (≠ D41), N63 (≠ E64), V64 (≠ L65), N90 (≠ C91), A91 (= A92), I93 (= I94), I113 (≠ V115), S142 (= S144), Y155 (= Y157), K159 (= K161), P185 (= P187), I188 (≠ A190), T190 (= T192)
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)
35% identity, 98% coverage: 6:250/250 of query aligns to 3:246/248 of Q9KJF1
- S15 (≠ R18) binding
- D36 (= D39) binding
- D62 (≠ E64) binding
- I63 (≠ L65) binding
- N89 (≠ C91) binding
- Y153 (= Y157) binding
- K157 (= K161) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
35% identity, 98% coverage: 6:250/250 of query aligns to 2:245/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), M16 (≠ I20), D35 (= D39), I36 (≠ V40), I62 (≠ L65), N88 (≠ C91), G90 (= G93), I138 (= I142), S140 (= S144), Y152 (= Y157), K156 (= K161), I185 (≠ A190)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
35% identity, 96% coverage: 6:246/250 of query aligns to 5:241/244 of 4nbuB
- active site: G18 (= G19), N111 (= N116), S139 (= S144), Q149 (≠ A154), Y152 (= Y157), K156 (= K161)
- binding acetoacetyl-coenzyme a: D93 (≠ N98), K98 (≠ E103), S139 (= S144), N146 (= N151), V147 (≠ P152), Q149 (≠ A154), Y152 (= Y157), F184 (≠ A189), M189 (≠ I194), K200 (≠ Y205)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), N17 (≠ R18), G18 (= G19), I19 (= I20), D38 (= D39), F39 (≠ V40), V59 (= V63), D60 (≠ E64), V61 (≠ L65), N87 (≠ C91), A88 (= A92), G89 (= G93), I90 (= I94), T137 (≠ I142), S139 (= S144), Y152 (= Y157), K156 (= K161), P182 (= P187), F184 (≠ A189), T185 (≠ A190), T187 (= T192), M189 (≠ I194)
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)
38% identity, 98% coverage: 6:250/250 of query aligns to 4:247/247 of P73574
- A14 (≠ G16) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (= P152) 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 (≠ A189) 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.
P14697 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) (see 2 papers)
37% identity, 95% coverage: 9:246/250 of query aligns to 4:242/246 of P14697
- GGI 13:15 (≠ RGI 18:20) binding
- G35 (≠ L45) binding
- R40 (= R50) binding
- Q47 (≠ K57) mutation to L: 2.4-fold increase in activity. 2-fold decrease in affinity for NADPH and 2.8-fold decrease in affinity for acetoacetyl-CoA.
- GNV 60:62 (≠ AAV 69:71) binding
- NAGIT 88:92 (≠ CAGIT 91:95) binding
- D94 (≠ N98) mutation to A: About 6% of wild-type activity.
- K99 (≠ E103) mutation to A: Nearly loss of activity.
- Q147 (≠ N151) mutation to A: About 30% of wild-type activity.
- F148 (≠ P152) mutation to A: About 30% of wild-type activity.
- Q150 (≠ A154) mutation to A: About 20% of wild-type activity.
- T173 (= T177) mutation to S: 3.5-fold increase in activity. 4-fold decrease in affinity for NADPH and 2.4-fold decrease in affinity for acetoacetyl-CoA.
- PGYI 183:186 (≠ PAAA 187:190) binding
- Y185 (≠ A189) mutation to A: Nearly loss of activity.
- R195 (≠ S199) mutation to A: Nearly loss of activity.
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
35% identity, 94% coverage: 13:246/250 of query aligns to 9:243/246 of 3osuA
6ci9D Rmm microcompartment-associated aminopropanol dehydrogenase NADP + aminoacetone holo-structure (see paper)
35% identity, 97% coverage: 6:247/250 of query aligns to 7:249/259 of 6ci9D
- active site: G20 (= G19), S145 (= S144), Y159 (= Y157)
- binding 1-aminopropan-2-one: F97 (≠ T95), S145 (= S144), T147 (≠ A146), W156 (≠ A154), Y159 (= Y157), G190 (≠ A188)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G16 (= G15), S18 (≠ A17), G20 (= G19), I21 (= I20), G40 (≠ D39), R41 (≠ V40), N42 (≠ D41), D66 (≠ E64), V67 (≠ L65), N93 (≠ C91), G95 (= G93), T143 (≠ I142), S145 (= S144), Y159 (= Y157), K163 (= K161), P189 (= P187), N191 (≠ A189), I192 (≠ A190), T194 (= T192), G196 (≠ I194), L197 (≠ F195)
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
37% identity, 95% coverage: 9:246/250 of query aligns to 7:245/249 of 3vzsB
- active site: N115 (= N116), S143 (= S144), Y156 (= Y157), K160 (= K161)
- binding acetoacetyl-coenzyme a: D97 (≠ N98), Q150 (≠ N151), F151 (≠ P152), Q153 (≠ A154), Y156 (= Y157), G187 (≠ A188), Y188 (≠ A189), R198 (≠ S199)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G15), I18 (= I20), G38 (≠ L45), R43 (= R50), G63 (≠ A69), N64 (≠ A70), V65 (= V71), G93 (= G93), I94 (= I94), T95 (= T95), P186 (= P187), I189 (≠ A190), M193 (≠ I194), V194 (≠ F195)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
32% identity, 97% coverage: 4:246/250 of query aligns to 1:240/244 of 6t77A
- active site: G16 (= G19), S138 (= S144), Y151 (= Y157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (≠ A17), R15 (= R18), T37 (≠ D41), L58 (≠ V63), N59 (≠ E64), V60 (≠ L65), A87 (= A92), G88 (= G93), I89 (= I94)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
35% identity, 95% coverage: 9:246/250 of query aligns to 3:241/245 of 5vmlA
- active site: G13 (= G19), N111 (= N116), S139 (= S144), Y152 (= Y157), K156 (= K161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G15), G12 (≠ R18), G13 (= G19), I14 (= I20), C33 (≠ W38), G34 (≠ D39), R39 (= R44), G59 (≠ V63), N60 (≠ E64), V61 (≠ L65), N87 (≠ C91), G89 (= G93), I90 (= I94), S139 (= S144), Y152 (= Y157), K156 (= K161), P182 (= P187), G183 (≠ A188), I185 (≠ A190)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
34% identity, 96% coverage: 6:246/250 of query aligns to 2:239/243 of 7emgB
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
35% identity, 94% coverage: 13:246/250 of query aligns to 6:236/239 of 3sj7A
- active site: G12 (= G19), S138 (= S144), Q148 (≠ A154), Y151 (= Y157), K155 (= K161)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G15), S10 (≠ A17), R11 (= R18), I13 (= I20), N31 (≠ W38), Y32 (≠ D39), A33 (≠ V40), G34 (≠ D41), S35 (≠ A42), A58 (≠ L65), N59 (≠ T66), V60 (≠ Q67), N86 (≠ C91), A87 (= A92), T109 (≠ V115), S138 (= S144), Y151 (= Y157), K155 (= K161), P181 (= P187), G182 (≠ A188)
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)
32% identity, 97% coverage: 4:246/250 of query aligns to 4:243/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (≠ A17), R18 (= R18), I20 (= I20), T40 (≠ D41), N62 (≠ E64), V63 (≠ L65), N89 (≠ C91), A90 (= A92), I92 (= I94), V139 (≠ I142), S141 (= S144), Y154 (= Y157), K158 (= K161), P184 (= P187), G185 (≠ A188), I187 (≠ A190), T189 (= T192), M191 (≠ I194)
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)
32% identity, 97% coverage: 4:246/250 of query aligns to 1:240/244 of P0A2C9
- M125 (= M131) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (≠ S229) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S230) 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.
1zemA Crystal structure of NAD+-bound xylitol dehydrogenase (see paper)
32% identity, 96% coverage: 6:246/250 of query aligns to 3:260/260 of 1zemA
- active site: N16 (≠ G19), S142 (= S144), Y155 (= Y157), K159 (= K161), D212 (≠ M198)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), G15 (≠ R18), N16 (≠ G19), I17 (= I20), D36 (= D39), M37 (≠ V40), D62 (≠ E64), V63 (≠ L65), N89 (≠ C91), A90 (= A92), G91 (= G93), T140 (≠ I142), S142 (= S144), Y155 (= Y157), K159 (= K161), P185 (= P187), M188 (vs. gap)
Query Sequence
>BPHYT_RS28250 FitnessBrowser__BFirm:BPHYT_RS28250
MNRIDLEGRVVAITGGARGIGYAVAQRALNSGSSVALWDVDAERLARSQRELSELGKVTA
VCVELTQEAAVAQAVAQTVADHGAIDVLINCAGITGGNGTTWELEPDVWRRVIDVNLIGP
YLTCRAVVPQMLKQGYGRIVNIASVAGKEGNPNASHYSASKAGLIGLTKSLGKELATKNI
LVNAVTPAAAKTEIFDSMSQQHIDYMLSKIPMNRFLMPEEAASLILWLSSEDCAFSTGSV
FDLSGGRATY
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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