SitesBLAST
Comparing HSERO_RS19050 FitnessBrowser__HerbieS:HSERO_RS19050 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)
5jc8D Crystal structure of a putative short-chain dehydrogenase/reductase from burkholderia xenovorans
45% identity, 98% coverage: 5:264/266 of query aligns to 4:261/262 of 5jc8D
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
37% identity, 97% coverage: 5:262/266 of query aligns to 5:253/254 of 4fn4A
- active site: G18 (= G23), S144 (= S148), Y157 (= Y162), K161 (= K166), S202 (= S207)
- binding nicotinamide-adenine-dinucleotide: G14 (= G14), S17 (= S17), G18 (= G23), I19 (≠ N24), E38 (≠ D43), L39 (≠ R44), R43 (≠ A48), A63 (= A68), D64 (= D69), V65 (= V70), N91 (= N96), G93 (= G98), I94 (= I99), T142 (≠ I146), S144 (= S148), Y157 (= Y162), K161 (= K166), P187 (= P192), V190 (≠ M195), T192 (= T197), N193 (≠ P198), I194 (≠ M199)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
36% identity, 97% coverage: 5:262/266 of query aligns to 3:247/247 of 4jroC
- active site: G16 (= G23), S142 (= S148), Q152 (≠ Y159), Y155 (= Y162), K159 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (≠ G16), R15 (≠ S17), G16 (= G23), I17 (≠ N24), N35 (≠ A41), Y36 (≠ V42), N37 (≠ D43), G38 (≠ R44), S39 (= S45), N63 (≠ D69), V64 (= V70), N90 (= N96), A91 (≠ V97), I93 (= I99), I113 (≠ V119), S142 (= S148), Y155 (= Y162), K159 (= K166), P185 (= P192), I188 (≠ M195), T190 (= T197)
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
32% identity, 98% coverage: 1:261/266 of query aligns to 1:251/261 of 1g6kA
- active site: G18 (= G23), S145 (= S148), Y158 (= Y162), K162 (= K166)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ S17), G18 (= G23), L19 (≠ N24), R39 (= R44), D65 (= D69), V66 (= V70), N92 (= N96), A93 (≠ V97), G94 (= G98), M143 (≠ I146), S145 (= S148), Y158 (= Y162), P188 (= P192), G189 (= G193), I191 (≠ M195), T193 (= T197)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
32% identity, 98% coverage: 1:261/266 of query aligns to 1:251/261 of P40288
- 11:35 (vs. 11:40, 30% identical) binding
- E96 (≠ A100) mutation E->A,G,K: Heat stable.
- D108 (≠ S112) mutation to N: Heat stable.
- V112 (≠ L116) mutation to A: Heat stable.
- E133 (= E136) mutation to K: Heat stable.
- V183 (≠ A187) mutation to I: Heat stable.
- P194 (= P198) mutation to Q: Heat stable.
- E210 (≠ N220) mutation to K: Heat stable.
- Y217 (≠ F227) mutation to H: Heat stable.
Sites not aligning to the query:
- 252 Q→L: Heat stable.
- 253 Y→C: Heat stable.
- 258 A→G: Heat stable.
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
37% identity, 95% coverage: 8:261/266 of query aligns to 3:248/250 of 2cfcA
- active site: G13 (= G23), S142 (= S148), Y155 (= Y162), K159 (= K166)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (= F157), R152 (≠ Y159), Y155 (= Y162), W195 (≠ E202), R196 (≠ P203)
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), S12 (= S17), G13 (= G23), N14 (= N24), D33 (= D43), L34 (≠ R44), A59 (= A68), D60 (= D69), V61 (= V70), N87 (= N96), A88 (≠ V97), G89 (= G98), I140 (= I146), P185 (= P192), G186 (= G193), M187 (= M194), I188 (≠ M195), T190 (= T197), P191 (= P198), M192 (= M199), T193 (≠ I200)
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)
37% identity, 95% coverage: 8:261/266 of query aligns to 3:248/250 of Q56840
- S-----GN 12:14 (≠ SVGEGWGN 17:24) binding
- D33 (= D43) binding
- DV 60:61 (= DV 69:70) binding
- N87 (= N96) binding
- S142 (= S148) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ Y159) 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 (= Y162) mutation Y->E,F: Loss of activity.
- K159 (= K166) mutation to A: Loss of activity.
- R179 (= R186) mutation to A: Loss of activity.
- IETPM 188:192 (≠ MDTPM 195:199) binding
- WR 195:196 (≠ EP 202:203) binding
- R196 (≠ P203) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (= R216) mutation to A: Slight decrease in catalytic efficiency.
- R209 (≠ Q222) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q8JZV9 Dehydrogenase/reductase SDR family member 6; (R)-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate dehydrogenase type 2; 4-oxo-L-proline reductase; Oxidoreductase UCPA; Short chain dehydrogenase/reductase family 15C member 1; EC 1.1.1.-; EC 1.1.1.30; EC 1.1.1.104 from Mus musculus (Mouse) (see paper)
36% identity, 97% coverage: 5:262/266 of query aligns to 4:245/245 of Q8JZV9
- Y147 (= Y162) active site, Proton acceptor; mutation to F: Loss of function.
D4A1J4 Dehydrogenase/reductase SDR family member 6; (R)-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate dehydrogenase type 2; 4-oxo-L-proline reductase; Oxidoreductase UCPA; Short chain dehydrogenase/reductase family 15C member 1; EC 1.1.1.-; EC 1.1.1.30; EC 1.1.1.104 from Rattus norvegicus (Rat) (see paper)
34% identity, 97% coverage: 5:262/266 of query aligns to 4:245/245 of D4A1J4
- Y147 (= Y162) mutation to F: Loss of function.
7krmC Putative fabg bound to nadh from acinetobacter baumannii
33% identity, 97% coverage: 4:260/266 of query aligns to 2:241/244 of 7krmC
- active site: G18 (= G23), S140 (= S148), Y155 (= Y162)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), S15 (= S17), G18 (= G23), I19 (≠ N24), D38 (= D43), L39 (≠ R44), A60 (= A68), N61 (≠ D69), V62 (= V70), N88 (= N96), V111 (= V119), S140 (= S148), Y155 (= Y162), K159 (= K166), I188 (≠ M195), T190 (= T197)
3ay6B Crystal structure of bacillus megaterium glucose dehydrogenase 4 a258f mutant in complex with nadh and d-glucose (see paper)
31% identity, 97% coverage: 5:261/266 of query aligns to 11:257/267 of 3ay6B
- active site: G24 (= G23), S151 (= S148), Y164 (= Y162), K168 (= K166)
- binding beta-D-glucopyranose: E102 (≠ A100), S151 (= S148), H153 (≠ A150), W158 (≠ F157), Y164 (= Y162), N202 (≠ I200), K205 (≠ P203)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G20 (= G14), T23 (≠ S17), G24 (= G23), L25 (≠ N24), Y45 (≠ D43), D71 (= D69), V72 (= V70), N98 (= N96), A99 (≠ V97), G100 (= G98), V101 (≠ I99), M149 (≠ I146), S151 (= S148), Y164 (= Y162), K168 (= K166), P194 (= P192), G195 (= G193), M197 (= M195), T199 (= T197), P200 (= P198), I201 (≠ M199), N202 (≠ I200)
7do7A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NAD and l-rhamnose bound-form) (see paper)
36% identity, 97% coverage: 3:260/266 of query aligns to 1:251/256 of 7do7A
- active site: G16 (= G23), S146 (= S148), Y159 (= Y162)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), R15 (≠ W22), G16 (= G23), I17 (≠ N24), S37 (vs. gap), D66 (= D69), A67 (≠ V70), N93 (= N96), A94 (≠ V97), G95 (= G98), I96 (= I99), V144 (≠ I146), S145 (= S147), S146 (= S148), Y159 (= Y162), K163 (= K166), P189 (= P192), G190 (= G193), I192 (≠ M195), T194 (= T197), I196 (≠ M199)
- binding beta-L-rhamnopyranose: F99 (≠ V102), S146 (= S148), S148 (≠ A150), Q156 (≠ Y159), Y159 (= Y162), N197 (≠ I200), D235 (= D244), M236 (≠ H245), R238 (= R247)
7b81A Crystal structure of azotobacter vinelandii l-rhamnose 1-dehydrogenase (NAD bound-form) (see paper)
36% identity, 97% coverage: 3:260/266 of query aligns to 1:251/256 of 7b81A
- active site: G16 (= G23), S146 (= S148), Y159 (= Y162)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), S14 (≠ G16), R15 (≠ W22), I17 (≠ N24), D66 (= D69), A67 (≠ V70), N93 (= N96), A94 (≠ V97), G95 (= G98), I96 (= I99), T116 (≠ V119), V144 (≠ I146), S146 (= S148), Y159 (= Y162), K163 (= K166), P189 (= P192), G190 (= G193), I192 (≠ M195), T194 (= T197), I196 (≠ M199)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
32% identity, 97% coverage: 5:261/266 of query aligns to 5:253/255 of 5itvA
- active site: G18 (= G23), S141 (= S148), Y154 (= Y162), K158 (= K166)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), S17 (= S17), G18 (= G23), I19 (≠ N24), D38 (= D43), I39 (= I46), T61 (≠ A68), I63 (≠ V70), N89 (= N96), G91 (= G98), T139 (≠ I146), S141 (= S148), Y154 (= Y162), K158 (= K166), P184 (= P192), G185 (= G193), I186 (≠ M194), I187 (≠ M195)
4ituA Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) bound to s-hpc and nadh (see paper)
34% identity, 86% coverage: 34:261/266 of query aligns to 27:251/253 of 4ituA
- active site: N113 (= N120), S141 (= S148), Y154 (= Y162), K158 (= K166)
- binding 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonic acid: S141 (= S148), Y154 (= Y162), T186 (≠ M194), R209 (= R219), Y213 (≠ C223)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D36 (= D43), L37 (≠ R44), D62 (= D69), V63 (= V70), N89 (= N96), V112 (= V119), F139 (≠ I146), S141 (= S148), Y154 (= Y162), K158 (= K166), P184 (= P192), T186 (≠ M194), V187 (≠ M195), T190 (≠ P198), M192 (≠ I200)
Sites not aligning to the query:
A7IQH5 2-(S)-hydroxypropyl-CoM dehydrogenase 3; S-HPCDH 3; 2-[(S)-2-hydroxypropylthio]ethanesulfonate dehydrogenase 3; Aliphatic epoxide carboxylation component IV; Epoxide carboxylase component IV; SHPCDH3; EC 1.1.1.269 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 2 papers)
34% identity, 86% coverage: 34:261/266 of query aligns to 29:253/255 of A7IQH5
- D38 (= D43) binding
- DV 64:65 (= DV 69:70) binding
- N91 (= N96) binding
- S143 (= S148) binding ; mutation to A: Retains very weak activity.
- Y156 (= Y162) binding ; mutation to A: Retains some activity but with more than 2200-fold decrease in catalytic efficiency.; mutation to F: Loss of activity.
- K160 (= K166) binding ; mutation to A: Loss of activity.
- T188 (≠ M194) binding
- VTSTG 189:193 (≠ MDTPM 195:199) binding
- R211 (= R219) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
- K214 (≠ Q222) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
- Y215 (≠ C223) binding
Sites not aligning to the query:
2dtxA Structure of thermoplasma acidophilum aldohexose dehydrogenase (aldt) in complex with d-mannose (see paper)
34% identity, 97% coverage: 5:263/266 of query aligns to 5:248/255 of 2dtxA
2dteA Structure of thermoplasma acidophilum aldohexose dehydrogenase (aldt) in complex with nadh (see paper)
34% identity, 97% coverage: 5:263/266 of query aligns to 5:248/255 of 2dteA
- active site: G18 (= G23), S132 (= S148), Y145 (= Y162), S148 (≠ T165), K149 (= K166)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), S16 (≠ G16), M17 (≠ W22), G18 (= G23), I19 (≠ N24), S38 (= S45), I39 (= I46), C52 (≠ A68), D53 (= D69), V54 (= V70), N80 (= N96), A81 (≠ V97), I130 (= I146), S132 (= S148), Y145 (= Y162), K149 (= K166), P174 (= P192), A175 (≠ G193), T176 (≠ M194), I177 (≠ M195), T179 (= T197), P180 (= P198), L181 (≠ M199), V182 (≠ I200)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
32% identity, 97% coverage: 4:261/266 of query aligns to 2:246/248 of 6ixmC
- active site: G16 (= G23), S142 (= S148), Y155 (= Y162), K159 (= K166)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), S15 (= S17), G16 (= G23), I17 (≠ N24), D36 (= D43), I37 (≠ R44), A61 (= A68), D62 (= D69), T63 (≠ V70), N89 (= N96), A90 (≠ V97), M140 (≠ I146), S142 (= S148), Y155 (= Y162), K159 (= K166), P185 (= P192), A186 (≠ G193), Y187 (≠ M194), I188 (≠ M195), L192 (≠ M199)
4gh5A Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) (see paper)
34% identity, 86% coverage: 34:261/266 of query aligns to 27:246/248 of 4gh5A
- active site: N113 (= N120), S141 (= S148), Y154 (= Y162), K158 (= K166)
- binding nicotinamide-adenine-dinucleotide: D36 (= D43), L37 (≠ R44), A61 (= A68), D62 (= D69), V63 (= V70), N89 (= N96), A90 (≠ V97), V112 (= V119), F139 (≠ I146), S141 (= S148), Y154 (= Y162), K158 (= K166), P184 (= P192), V187 (≠ M195), T190 (≠ P198), G191 (≠ M199), M192 (≠ I200)
Sites not aligning to the query:
Query Sequence
>HSERO_RS19050 FitnessBrowser__HerbieS:HSERO_RS19050
MDKLMQGKAIIVTGAGSVGEGWGNGKAAAVLYAREGGRVLAVDRSIEAALQTQDIIRSEG
GVCEVLAADVSRNTEVKAIAEAAMDHFGRVDVLHNNVGIADVGGPVETSEESWNRLVAVN
QTSLFLTHKHVLPIMEKQRKGAIVNISSLAALRWIGFPYLGYTATKAAILAFTKNVAMQY
APMGIRANCVLPGMMDTPMIREPLKASYGGDIEQMRAKRNAQCPMGFMGDAWDVAHASLF
LASDHARYITGLDMIVDGGLSLRCAG
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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