SitesBLAST
Comparing BWI76_RS13720 FitnessBrowser__Koxy:BWI76_RS13720 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)
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
35% identity, 99% coverage: 1:254/257 of query aligns to 1:247/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), Q15 (= Q15), G16 (= G16), I17 (= I17), D36 (= D36), V63 (≠ L62), N89 (= N88), A91 (vs. gap), S94 (≠ G91), I142 (= I139), S143 (= S140), S144 (= S141), Y157 (= Y152), K161 (= K156), P187 (= P182), H188 (≠ G183), I190 (vs. gap), I194 (≠ A187)
6qheA Alcohol dehydrogenase from arthrobacter sp. Ts-15 in complex with NAD+
33% identity, 98% coverage: 1:253/257 of query aligns to 3:252/261 of 6qheA
- binding nicotinamide-adenine-dinucleotide: G14 (= G12), M17 (≠ Q15), G18 (= G16), M19 (≠ I17), D38 (= D36), R39 (= R37), D63 (= D61), I64 (≠ L62), A90 (≠ V89), A91 (≠ G90), S142 (= S141), Y156 (= Y152), K160 (= K156), P186 (= P182), G187 (= G183), M189 (≠ T185), T191 (≠ A187), P192 (= P188), M193 (≠ A189)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
34% identity, 98% coverage: 3:254/257 of query aligns to 5:250/254 of 4fn4A
- active site: G18 (= G16), S144 (= S141), Y157 (= Y152), K161 (= K156), S202 (≠ T200)
- binding nicotinamide-adenine-dinucleotide: G14 (= G12), S17 (≠ Q15), G18 (= G16), I19 (= I17), E38 (vs. gap), L39 (= L33), R43 (= R37), A63 (= A60), D64 (= D61), V65 (≠ L62), N91 (= N88), G93 (= G90), I94 (≠ G91), T142 (≠ I139), S144 (= S141), Y157 (= Y152), K161 (= K156), P187 (= P182), V190 (≠ T185), T192 (≠ A187), N193 (≠ P188), I194 (≠ A189)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
36% identity, 98% coverage: 2:254/257 of query aligns to 4:241/244 of 4nbuB
- active site: G18 (= G16), N111 (≠ S113), S139 (= S141), Q149 (≠ R149), Y152 (= Y152), K156 (= K156)
- binding acetoacetyl-coenzyme a: D93 (≠ A95), K98 (≠ E100), S139 (= S141), N146 (vs. gap), V147 (= V147), Q149 (≠ R149), Y152 (= Y152), F184 (≠ G184), M189 (≠ Q202), K200 (≠ Q213)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ Q15), G18 (= G16), I19 (= I17), D38 (= D36), F39 (≠ R37), V59 (≠ A60), D60 (= D61), V61 (≠ L62), N87 (= N88), A88 (≠ V89), G89 (= G90), I90 (≠ G91), T137 (≠ I139), S139 (= S141), Y152 (= Y152), K156 (= K156), P182 (= P182), F184 (≠ G184), T185 (= T185), T187 (= T200), M189 (≠ Q202)
1iy8A Crystal structure of levodione reductase (see paper)
35% identity, 98% coverage: 2:254/257 of query aligns to 1:253/258 of 1iy8A
- active site: G15 (= G16), S143 (= S141), Q153 (≠ R149), Y156 (= Y152), K160 (= K156)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (≠ Q15), G15 (= G16), L16 (≠ I17), D35 (= D36), V36 (≠ R37), A62 (= A60), D63 (= D61), V64 (≠ L62), N90 (= N88), G92 (= G90), I93 (≠ G91), T141 (≠ I139), S143 (= S141), Y156 (= Y152), K160 (= K156), P186 (= P182), G187 (= G183), T191 (= T192), P192 (= P193), M193 (≠ R194)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
35% identity, 98% coverage: 2:254/257 of query aligns to 10:262/267 of Q9LBG2
- 17:42 (vs. 9:34, 54% identical) binding
- E103 (≠ T92) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
7krmC Putative fabg bound to nadh from acinetobacter baumannii
35% identity, 100% coverage: 1:256/257 of query aligns to 1:242/244 of 7krmC
- active site: G18 (= G16), S140 (= S141), Y155 (= Y152)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (vs. gap), G18 (= G16), I19 (= I17), D38 (= D36), L39 (≠ R37), A60 (= A60), N61 (≠ D61), V62 (≠ L62), N88 (= N88), V111 (≠ R112), S140 (= S141), Y155 (= Y152), K159 (= K156), I188 (≠ T185), T190 (= T192)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
35% identity, 97% coverage: 5:253/257 of query aligns to 2:245/250 of 2cfcA
- active site: G13 (= G16), S142 (= S141), Y155 (= Y152), K159 (= K156)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ G146), R152 (= R149), Y155 (= Y152), W195 (≠ R194), R196 (≠ N195)
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), S12 (≠ Q15), G13 (= G16), N14 (≠ I17), D33 (= D36), L34 (≠ R37), A59 (= A60), D60 (= D61), V61 (≠ L62), N87 (= N88), A88 (≠ V89), G89 (= G90), I140 (= I139), P185 (= P182), G186 (= G183), M187 (≠ G184), I188 (≠ T185), T190 (≠ A187), P191 (= P188), M192 (≠ L191), T193 (= T192)
Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase; R-HPCDH; 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase; Aliphatic epoxide carboxylation component III; Epoxide carboxylase component III; RHPCDH1; EC 1.1.1.268 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 4 papers)
35% identity, 97% coverage: 5:253/257 of query aligns to 2:245/250 of Q56840
- SGN 12:14 (≠ QGI 15:17) binding
- D33 (= D36) binding
- DV 60:61 (≠ DL 61:62) binding
- N87 (= N88) binding
- S142 (= S141) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (= R149) binding ; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- Y155 (= Y152) mutation Y->E,F: Loss of activity.
- K159 (= K156) mutation to A: Loss of activity.
- R179 (= R176) mutation to A: Loss of activity.
- IETP--M 188:192 (≠ TEAPARL 185:191) binding
- WR 195:196 (≠ RN 194:195) binding
- R196 (≠ N195) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (≠ V211) mutation to A: Slight decrease in catalytic efficiency.
- R209 (≠ S217) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 100% coverage: 1:256/257 of query aligns to 1:246/248 of 4urfB
- active site: G16 (= G16), S142 (= S141), I152 (≠ V150), Y155 (= Y152), K159 (= K156)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (≠ M220), R211 (≠ H221), R212 (= R222)
- binding bicarbonate ion: I92 (≠ G91), G94 (≠ I93), R109 (≠ K108), R179 (= R176), S228 (= S238)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G14 (≠ A14), N15 (≠ Q15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (≠ R37), D62 (= D61), T63 (≠ L62), N89 (= N88), A90 (≠ V89), G91 (= G90), I140 (= I139), Y155 (= Y152), K159 (= K156), P185 (= P188), A186 (= A189), I188 (≠ L191), T190 (≠ P193)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 100% coverage: 1:256/257 of query aligns to 1:246/248 of 4urfA
- active site: G16 (= G16), S142 (= S141), I152 (≠ V150), Y155 (= Y152), K159 (= K156)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (≠ G91), S93 (≠ T92), G94 (≠ I93), E95 (≠ W94), T97 (≠ R96), E101 (= E100), T103 (≠ Q102), Q106 (= Q105), R109 (≠ K108), S175 (≠ A172), G177 (= G174)
- binding magnesium ion: S237 (≠ V247), Y238 (≠ T248)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G14 (≠ A14), N15 (≠ Q15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (≠ R37), W41 (≠ Y40), D62 (= D61), T63 (≠ L62), N89 (= N88), A90 (≠ V89), G91 (= G90), I140 (= I139), Y155 (= Y152), K159 (= K156), P185 (= P188), I188 (≠ L191), T190 (≠ P193)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 100% coverage: 1:256/257 of query aligns to 1:246/248 of 4ureB
- active site: G16 (= G16), S142 (= S141), I152 (≠ V150), Y155 (= Y152), K159 (= K156)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ Q15), G16 (= G16), I17 (= I17), N89 (= N88), G91 (= G90), Y155 (= Y152), P185 (= P188), A186 (= A189)
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)
34% identity, 99% coverage: 1:254/257 of query aligns to 1:240/251 of H9XP47
- N15 (≠ Q15) binding
- M17 (≠ I17) binding
- D36 (= D36) binding
- D60 (= D61) binding
- V61 (≠ L62) binding
- N87 (= N88) binding
- S138 (= S141) binding ; binding
- V139 (= V142) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ A143) binding
- Y151 (= Y152) binding ; binding ; binding
- K155 (= K156) binding
- V184 (≠ T185) binding
- T186 (= T200) binding
- RDK 197:199 (≠ VDQ 211:213) 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.
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
33% identity, 99% coverage: 1:254/257 of query aligns to 1:244/247 of 4jroC
- active site: G16 (= G16), S142 (= S141), Q152 (≠ R149), Y155 (= Y152), K159 (= K156)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ A14), R15 (≠ Q15), G16 (= G16), I17 (= I17), N35 (≠ I35), Y36 (≠ D36), N37 (≠ R37), G38 (≠ S38), S39 (vs. gap), N63 (≠ D61), V64 (≠ L62), N90 (= N88), A91 (≠ V89), I93 (≠ G91), I113 (≠ R112), S142 (= S141), Y155 (= Y152), K159 (= K156), P185 (= P182), I188 (vs. gap), T190 (= T185)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
34% identity, 98% coverage: 2:254/257 of query aligns to 2:240/251 of 6vspA
- active site: G16 (= G16), S138 (= S141), Y151 (= Y152)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), N15 (≠ Q15), G16 (= G16), M17 (≠ I17), D36 (= D36), W37 (≠ R37), W37 (≠ R37), A38 (≠ S38), I59 (≠ A60), D60 (= D61), V61 (≠ L62), N87 (= N88), A88 (≠ V89), G89 (= G90), V90 (≠ G91), V110 (≠ R112), T136 (≠ I139), S138 (= S141), Y151 (= Y152), K155 (= K156), P181 (= P182), S182 (≠ G183), L183 (≠ G184), V184 (≠ T185), T186 (= T200), N187 (≠ A201), M188 (≠ Q202), T189 (≠ E203)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
33% identity, 98% coverage: 2:254/257 of query aligns to 7:249/258 of 4wecA
- active site: G21 (= G16), S143 (= S141), Q154 (≠ R149), Y157 (= Y152), K161 (= K156)
- binding nicotinamide-adenine-dinucleotide: G17 (= G12), A19 (= A14), S20 (≠ Q15), G21 (= G16), I22 (= I17), D41 (= D36), I42 (≠ R37), V61 (≠ A60), D62 (= D61), V63 (≠ L62), N89 (= N88), T141 (≠ I139), Y157 (= Y152), K161 (= K156), P187 (= P182), P189 (≠ G184), V190 (≠ T185)
G9FRD7 7alpha-hydroxysteroid dehydrogenase; 7alpha-HSDH; NADP-dependent 7alpha-hydroxysteroid dehydrogenase; EC 1.1.1.- from Clostridium sardiniense (Clostridium absonum) (see 2 papers)
32% identity, 98% coverage: 2:254/257 of query aligns to 3:248/262 of G9FRD7
- SSTRGI 13:18 (≠ GAAQGI 12:17) binding
- R38 (= R37) binding ; mutation to D: Loss of catalytic activity.
- NA 63:64 (≠ DL 61:62) binding
- N90 (= N88) binding
- T145 (≠ S141) binding
- Y158 (= Y152) binding ; binding
- K162 (= K156) binding
- IGTRA 191:195 (≠ TEAPA 185:189) binding
Sites not aligning to the query:
- 261:262 mutation Missing: 5-fold reduction in catalytic efficiency.
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
34% identity, 98% coverage: 2:254/257 of query aligns to 2:240/251 of 6xewA
- active site: G16 (= G16), S138 (= S141), Y151 (= Y152)
- binding r,3-hydroxybutan-2-one: S138 (= S141), S140 (≠ A143), Y151 (= Y152)
- binding s,3-hydroxybutan-2-one: S138 (= S141), Y151 (= Y152), S182 (≠ G183)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), N15 (≠ Q15), G16 (= G16), M17 (≠ I17), D36 (= D36), W37 (≠ R37), W37 (≠ R37), A38 (≠ S38), I59 (≠ A60), D60 (= D61), V61 (≠ L62), N87 (= N88), A88 (≠ V89), G89 (= G90), V110 (≠ R112), T136 (≠ I139), S138 (= S141), Y151 (= Y152), K155 (= K156), S182 (≠ G183), L183 (≠ G184), V184 (≠ T185), T186 (= T200), N187 (≠ A201), M188 (≠ Q202), T189 (≠ E203)
5epoA The three-dimensional structure of clostridium absonum 7alpha- hydroxysteroid dehydrogenase (see paper)
32% identity, 98% coverage: 2:254/257 of query aligns to 2:247/261 of 5epoA
- active site: G16 (= G16), T144 (≠ S141), I152 (≠ V147), Y157 (= Y152), K161 (= K156), R193 (≠ P188)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S12 (≠ G12), T14 (≠ A14), R15 (≠ Q15), G16 (= G16), I17 (= I17), R37 (= R37), F61 (≠ A60), N62 (≠ D61), N89 (= N88), Y90 (≠ V89), G91 (= G90), Y157 (= Y152), K161 (= K156), P187 (= P182), G188 (= G183), I190 (≠ T185), T192 (≠ A187), R193 (≠ P188), A194 (= A189), A195 (≠ R190)
- binding taurochenodeoxycholic acid: T93 (= T92), T144 (≠ S141), G146 (≠ A143), R154 (= R149), Y157 (= Y152), G188 (= G183), N198 (≠ K205), M199 (≠ W206), F203 (≠ V210)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
34% identity, 98% coverage: 2:254/257 of query aligns to 4:242/252 of 6vspB
Query Sequence
>BWI76_RS13720 FitnessBrowser__Koxy:BWI76_RS13720
MRFSNKVVAITGAAQGIGRQTAEQAAREGARLLLIDRSRYVHELAAALNDSGSEALALEA
DLEQWESTERAFAEGVAHFGRLDVLINNVGGTIWARPFAEYQPQQIEKEIRRSLFPTLWG
CRAALPWMLRQGKGSIVNISSVATAGVNRVPYSAAKGGVNALTRSLALEYSANGIRINAV
APGGTEAPARLTPRNEEQPTAQEQKWYQQVVDQTVASSLMHRYGTLAEQANAILFLASDE
ASYITGVTLPVAGGDLG
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