SitesBLAST
Comparing WP_038208119.1 NCBI__GCF_000745855.1:WP_038208119.1 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)
40% identity, 99% coverage: 1:253/255 of query aligns to 2:244/244 of 4nbuB
- active site: G18 (= G17), N111 (= N114), S139 (= S142), Q149 (≠ E152), Y152 (= Y155), K156 (= K159)
- binding acetoacetyl-coenzyme a: D93 (≠ F96), K98 (≠ R101), S139 (= S142), N146 (≠ S149), V147 (≠ S150), Q149 (≠ E152), Y152 (= Y155), F184 (≠ P187), M189 (≠ L192), K200 (≠ A209)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), N17 (≠ G16), G18 (= G17), I19 (= I18), D38 (= D37), F39 (≠ L38), V59 (≠ C62), D60 (= D63), V61 (≠ I64), N87 (= N90), A88 (= A91), G89 (= G92), I90 (≠ W93), T137 (≠ I140), S139 (= S142), Y152 (= Y155), K156 (= K159), P182 (= P185), F184 (≠ P187), T185 (= T188), T187 (= T190), M189 (≠ L192)
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, 98% coverage: 3:253/255 of query aligns to 5:247/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G13), R18 (≠ G16), G19 (= G17), I20 (= I18), D39 (= D37), R40 (≠ L38), C63 (= C62), I65 (= I64), N91 (= N90), G93 (= G92), I94 (≠ W93), V114 (= V113), Y155 (= Y155), K159 (= K159), I188 (≠ T188), T190 (= T190), T193 (≠ R197)
H9XP47 Meso-2,3-butanediol dehydrogenase; BDH; meso-2,3-BDH; (R,S)-butane-2,3-diol dehydrogenase; NAD(H)-dependent meso-2,3-BDH; SmBdh; EC 1.1.1.- from Serratia marcescens (see paper)
38% identity, 98% coverage: 2:252/255 of query aligns to 1:242/251 of H9XP47
- N15 (≠ G16) binding NAD(+)
- M17 (≠ I18) binding NAD(+)
- D36 (= D37) binding NAD(+)
- D60 (= D63) binding NAD(+)
- V61 (≠ I64) binding NAD(+)
- N87 (= N90) binding NAD(+)
- S138 (= S142) binding (R)-acetoin; binding (S)-acetoin
- V139 (≠ D143) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ A144) binding (R)-acetoin
- Y151 (= Y155) binding (R)-acetoin; binding (S)-acetoin; binding NAD(+)
- K155 (= K159) binding NAD(+)
- V184 (≠ T188) binding NAD(+)
- T186 (= T190) binding NAD(+)
- RDK 197:199 (≠ MEA 207:209) mutation to SEAAGKPLGYGTET: Mimics longer alpha6 helix. Retains 3% of activity with acetoin as substrate.
Sites not aligning to the query:
- 247 Q→A: Retains 10% of activity with acetoin as substrate. Retains 50% of activity with acetoin as substrate; when associated with Q-139.
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
38% identity, 98% coverage: 3:252/255 of query aligns to 2:242/251 of 6xewA
- active site: G16 (= G17), S138 (= S142), Y151 (= Y155)
- binding r,3-hydroxybutan-2-one: S138 (= S142), S140 (≠ A144), Y151 (= Y155)
- binding s,3-hydroxybutan-2-one: S138 (= S142), Y151 (= Y155), S182 (≠ G186)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ G16), G16 (= G17), M17 (≠ I18), D36 (= D37), W37 (≠ L38), W37 (≠ L38), A38 (≠ N39), I59 (≠ C62), D60 (= D63), V61 (≠ I64), N87 (= N90), A88 (= A91), G89 (= G92), V110 (= V113), T136 (≠ I140), S138 (= S142), Y151 (= Y155), K155 (= K159), S182 (≠ G186), L183 (≠ P187), V184 (≠ T188), T186 (= T190), N187 (≠ A191), M188 (≠ L192), T189 (≠ F193)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
38% identity, 98% coverage: 3:252/255 of query aligns to 4:244/252 of 6vspB
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
38% identity, 98% coverage: 3:252/255 of query aligns to 2:242/251 of 6vspA
- active site: G16 (= G17), S138 (= S142), Y151 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ G16), G16 (= G17), M17 (≠ I18), D36 (= D37), W37 (≠ L38), W37 (≠ L38), A38 (≠ N39), I59 (≠ C62), D60 (= D63), V61 (≠ I64), N87 (= N90), A88 (= A91), G89 (= G92), V90 (≠ W93), V110 (= V113), T136 (≠ I140), S138 (= S142), Y151 (= Y155), K155 (= K159), P181 (= P185), S182 (≠ G186), L183 (≠ P187), V184 (≠ T188), T186 (= T190), N187 (≠ A191), M188 (≠ L192), T189 (≠ F193)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
37% identity, 99% coverage: 1:252/255 of query aligns to 2:253/255 of 5itvA
- active site: G18 (= G17), S141 (= S142), Y154 (= Y155), K158 (= K159)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), S17 (≠ G16), G18 (= G17), I19 (= I18), D38 (= D37), I39 (≠ L38), T61 (≠ C62), I63 (= I64), N89 (= N90), G91 (= G92), T139 (≠ I140), S141 (= S142), Y154 (= Y155), K158 (= K159), P184 (= P185), G185 (= G186), I186 (≠ P187), I187 (≠ T188)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
38% identity, 98% coverage: 4:253/255 of query aligns to 3:247/247 of 4jroC
- active site: G16 (= G17), S142 (= S142), Q152 (≠ E152), Y155 (= Y155), K159 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (≠ G15), R15 (≠ G16), G16 (= G17), I17 (= I18), N35 (≠ D37), Y36 (≠ L38), N37 (= N39), G38 (vs. gap), S39 (vs. gap), N63 (≠ D63), V64 (≠ I64), N90 (= N90), A91 (= A91), I93 (≠ W93), I113 (≠ V113), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), I188 (≠ T188), T190 (= T190)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
38% identity, 98% coverage: 4:253/255 of query aligns to 2:242/243 of 7emgB
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
37% identity, 98% coverage: 4:253/255 of query aligns to 2:244/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G13), M16 (≠ I18), D35 (= D37), I36 (≠ L38), I62 (= I64), N88 (= N90), G90 (= G92), I138 (= I140), S140 (= S142), Y152 (= Y155), K156 (= K159), I185 (≠ T188)
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: 4:253/255 of query aligns to 3:245/248 of Q9KJF1
- S15 (≠ G16) binding NAD(+)
- D36 (= D37) binding NAD(+)
- D62 (= D63) binding NAD(+)
- I63 (= I64) binding NAD(+)
- N89 (= N90) binding NAD(+)
- Y153 (= Y155) binding NAD(+)
- K157 (= K159) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6zzsD Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and 3-oxovalerate (see paper)
37% identity, 99% coverage: 1:252/255 of query aligns to 1:259/261 of 6zzsD
- active site: G18 (= G17), S143 (= S142), Y156 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G14 (= G13), S17 (≠ G16), I19 (= I18), D38 (= D37), M39 (≠ L38), D64 (= D63), V65 (≠ I64), N91 (= N90), A92 (= A91), G93 (= G92), M141 (≠ I140), A142 (= A141), S143 (= S142), Y156 (= Y155), K160 (= K159), P186 (= P185), G187 (= G186), V189 (≠ T188), T191 (= T190), L193 (= L192)
- binding 3-oxidanylidenepentanoic acid: Q95 (≠ D94), S143 (= S142), N145 (≠ A144), K153 (≠ E152), Y156 (= Y155), Q197 (vs. gap)
6zzqA Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and acetoacetate (see paper)
36% identity, 98% coverage: 2:252/255 of query aligns to 2:258/260 of 6zzqA
- active site: G17 (= G17), S142 (= S142), Y155 (= Y155)
- binding acetoacetic acid: Q94 (≠ D94), S142 (= S142), K152 (≠ E152), Y155 (= Y155), Q196 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: G13 (= G13), S16 (≠ G16), G17 (= G17), I18 (= I18), D37 (= D37), M38 (≠ L38), D63 (= D63), V64 (≠ I64), N90 (= N90), A91 (= A91), G92 (= G92), M140 (≠ I140), A141 (= A141), S142 (= S142), Y155 (= Y155), K159 (= K159), Y187 (≠ P187), V188 (≠ T188), T190 (= T190)
Q48436 Diacetyl reductase [(S)-acetoin forming]; Acetoin(diacetyl) reductase; AR; Meso-2,3-butanediol dehydrogenase; EC 1.1.1.304 from Klebsiella pneumoniae (see paper)
38% identity, 97% coverage: 7:253/255 of query aligns to 3:255/256 of Q48436
- 6:33 (vs. 10:37, 46% identical) binding NAD(+)
- D59 (= D63) binding NAD(+)
- K156 (= K159) binding NAD(+)
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)
36% identity, 98% coverage: 4:253/255 of query aligns to 3:243/244 of P0AEK2
- GASR 12:15 (≠ GGGG 13:16) binding NADP(+)
- T37 (≠ L38) binding NADP(+)
- NV 59:60 (≠ DI 63:64) binding NADP(+)
- N86 (= N90) binding NADP(+)
- Y151 (= Y155) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YAACK 155:159) binding NADP(+)
- A154 (≠ C158) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K159) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ T188) binding NADP(+)
- E233 (≠ Q243) 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)
36% identity, 98% coverage: 4:253/255 of query aligns to 2:242/243 of 1q7bA
- active site: G15 (= G17), E101 (≠ D106), S137 (= S142), Q147 (≠ E152), Y150 (= Y155), K154 (= K159)
- binding calcium ion: E232 (≠ Q243), T233 (≠ V244)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G13), S13 (≠ G15), R14 (≠ G16), T36 (≠ L38), N58 (≠ D63), V59 (≠ I64), N85 (= N90), A86 (= A91), G87 (= G92), I88 (≠ W93), S137 (= S142), Y150 (= Y155), K154 (= K159), P180 (= P185), G181 (= G186), I183 (≠ T188)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
35% identity, 98% coverage: 4:253/255 of query aligns to 3:243/244 of 6t77A
- active site: G16 (= G17), S138 (= S142), Y151 (= Y155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (≠ G15), R15 (≠ G16), T37 (≠ L38), L58 (≠ C62), N59 (≠ D63), V60 (≠ I64), A87 (= A91), G88 (= G92), I89 (≠ W93)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
36% identity, 98% coverage: 4:253/255 of query aligns to 2:242/243 of 1q7cA
- active site: G15 (= G17), S137 (= S142), Q147 (≠ E152), F150 (≠ Y155), K154 (= K159)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G13), S13 (≠ G15), R14 (≠ G16), A35 (≠ D37), T36 (≠ L38), L57 (≠ C62), N58 (≠ D63), V59 (≠ I64), G87 (= G92), I88 (≠ W93)
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)
35% identity, 98% coverage: 4:253/255 of query aligns to 3:243/244 of P0A2C9
- M125 (= M129) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A233) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S234) 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.
1gegE Cryatal structure analysis of meso-2,3-butanediol dehydrogenase (see paper)
38% identity, 97% coverage: 7:253/255 of query aligns to 3:255/256 of 1gegE
- active site: G13 (= G17), S139 (= S142), Y152 (= Y155), K156 (= K159), V197 (vs. gap)
- binding alpha-D-glucopyranose: R63 (= R67), D64 (≠ A68), F67 (≠ D71), E123 (≠ P127)
- binding nicotinamide-adenine-dinucleotide: G9 (= G13), Q12 (≠ G16), I14 (= I18), D33 (= D37), Y34 (≠ L38), V58 (≠ C62), D59 (= D63), V60 (≠ I64), N86 (= N90), A87 (= A91), I109 (≠ V113), S139 (= S142), Y152 (= Y155), K156 (= K159), P182 (= P185), V185 (≠ T188), T187 (= T190), M189 (≠ L192)
Query Sequence
>WP_038208119.1 NCBI__GCF_000745855.1:WP_038208119.1
MQRFEDRTVVVTGGGGGIGGAACRRFAREGAKVAVFDLNEEAAAQVAGQIREAGGRAEAV
RCDITDRASVDAAVAQAQARLGAIDVLVNNAGWDVFKPFTRTTSADWERLVAVNLTGALH
MHHAVLPGMAARKAGRIVNIASDAARVGSSGEAVYAACKGGLVALSKTLAREHARHGITV
NVVCPGPTDTALFADYREGAGNPEKLMEAFTRSIPLGRIGQPEDLPGAIAFFASDDAAFV
TGQVLSVSGGLTMAG
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