SitesBLAST
Comparing SMc01635 FitnessBrowser__Smeli:SMc01635 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)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
37% identity, 100% coverage: 2:253/253 of query aligns to 2:248/248 of 6ixmC
- active site: G16 (= G16), S142 (= S141), Y155 (= Y154), K159 (= K158)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (= S15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (≠ R37), A61 (≠ V61), D62 (= D62), T63 (≠ V63), N89 (≠ H89), A90 (= A90), M140 (≠ T139), S142 (= S141), Y155 (= Y154), K159 (= K158), P185 (= P184), A186 (≠ G185), Y187 (≠ W186), I188 (≠ V187), L192 (≠ F191)
6zzsD Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and 3-oxovalerate (see paper)
36% identity, 99% coverage: 2:251/253 of query aligns to 4:259/261 of 6zzsD
- active site: G18 (= G16), S143 (= S141), Y156 (= Y154)
- binding nicotinamide-adenine-dinucleotide: G14 (= G12), S17 (= S15), I19 (= I17), D38 (= D36), M39 (≠ R37), D64 (= D62), V65 (= V63), N91 (≠ H89), A92 (= A90), G93 (= G91), M141 (≠ T139), A142 (≠ S140), S143 (= S141), Y156 (= Y154), K160 (= K158), P186 (= P184), G187 (= G185), V189 (= V187), T191 (= T189), L193 (≠ F191)
- binding 3-oxidanylidenepentanoic acid: Q95 (= Q93), S143 (= S141), N145 (≠ S143), K153 (≠ M151), Y156 (= Y154), Q197 (≠ F195)
6zzqA Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and acetoacetate (see paper)
36% identity, 99% coverage: 2:251/253 of query aligns to 3:258/260 of 6zzqA
- active site: G17 (= G16), S142 (= S141), Y155 (= Y154)
- binding acetoacetic acid: Q94 (= Q93), S142 (= S141), K152 (≠ M151), Y155 (= Y154), Q196 (≠ F195)
- binding nicotinamide-adenine-dinucleotide: G13 (= G12), S16 (= S15), G17 (= G16), I18 (= I17), D37 (= D36), M38 (≠ R37), D63 (= D62), V64 (= V63), N90 (≠ H89), A91 (= A90), G92 (= G91), M140 (≠ T139), A141 (≠ S140), S142 (= S141), Y155 (= Y154), K159 (= K158), Y187 (≠ W186), V188 (= V187), T190 (= T189)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
34% identity, 99% coverage: 1:251/253 of query aligns to 3:253/255 of 5itvA
- active site: G18 (= G16), S141 (= S141), Y154 (= Y154), K158 (= K158)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), S17 (= S15), G18 (= G16), I19 (= I17), D38 (= D36), I39 (≠ R37), T61 (≠ V61), I63 (≠ V63), N89 (≠ H89), G91 (= G91), T139 (= T139), S141 (= S141), Y154 (= Y154), K158 (= K158), P184 (= P184), G185 (= G185), I186 (≠ W186), I187 (≠ V187)
1iy8A Crystal structure of levodione reductase (see paper)
34% identity, 98% coverage: 3:251/253 of query aligns to 2:255/258 of 1iy8A
- active site: G15 (= G16), S143 (= S141), Q153 (≠ M151), Y156 (= Y154), K160 (= K158)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (≠ I17), D35 (= D36), V36 (≠ R37), A62 (vs. gap), D63 (= D62), V64 (= V63), N90 (≠ H89), G92 (= G91), I93 (≠ A92), T141 (= T139), S143 (= S141), Y156 (= Y154), K160 (= K158), P186 (= P184), G187 (= G185), T191 (= T189), P192 (= P190), M193 (≠ F191)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
34% identity, 98% coverage: 3:251/253 of query aligns to 11:264/267 of Q9LBG2
- 17:42 (vs. 9:34, 50% identical) binding
- E103 (≠ Q93) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
5jc8D Crystal structure of a putative short-chain dehydrogenase/reductase from burkholderia xenovorans
36% identity, 98% coverage: 3:249/253 of query aligns to 4:256/262 of 5jc8D
4nbuB Crystal structure of fabg from bacillus sp (see paper)
35% identity, 98% coverage: 3:249/253 of query aligns to 5:241/244 of 4nbuB
- active site: G18 (= G16), N111 (= N113), S139 (= S141), Q149 (≠ M151), Y152 (= Y154), K156 (= K158)
- binding acetoacetyl-coenzyme a: D93 (≠ A95), K98 (≠ E100), S139 (= S141), N146 (≠ D148), V147 (≠ R149), Q149 (≠ M151), Y152 (= Y154), F184 (≠ W186), M189 (≠ F191), K200 (≠ Q198)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ S15), G18 (= G16), I19 (= I17), D38 (= D36), F39 (≠ R37), V59 (= V61), D60 (= D62), V61 (= V63), N87 (≠ H89), A88 (= A90), G89 (= G91), I90 (≠ A92), T137 (= T139), S139 (= S141), Y152 (= Y154), K156 (= K158), P182 (= P184), F184 (≠ W186), T185 (≠ V187), T187 (= T189), M189 (≠ F191)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
34% identity, 98% coverage: 3:249/253 of query aligns to 8:249/258 of 4wecA
- active site: G21 (= G16), S143 (= S141), Q154 (≠ M151), Y157 (= Y154), K161 (= K158)
- binding nicotinamide-adenine-dinucleotide: G17 (= G12), A19 (≠ G14), S20 (= S15), G21 (= G16), I22 (= I17), D41 (= D36), I42 (vs. gap), V61 (= V61), D62 (= D62), V63 (= V63), N89 (≠ H89), T141 (= T139), Y157 (= Y154), K161 (= K158), P187 (= P184), P189 (= P190), V190 (≠ F191)
3uf0A Crystal structure of a putative NAD(p) dependent gluconate 5- dehydrogenase from beutenbergia cavernae(efi target efi-502044) with bound NADP (low occupancy)
39% identity, 98% coverage: 3:249/253 of query aligns to 5:245/249 of 3uf0A
- active site: G18 (= G16), S141 (= S141), V151 (≠ M151), Y154 (= Y154), K158 (= K158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G12), S17 (= S15), G18 (= G16), I19 (= I17), R39 (= R37), D63 (= D62), L64 (≠ V63), N89 (≠ H89), G91 (= G91), I92 (≠ A92), I139 (≠ T139), A140 (≠ S140), S141 (= S141), Y154 (= Y154), K158 (= K158), P184 (= P184), G185 (= G185), V187 (= V187), T189 (= T189), N191 (≠ F191), T192 (≠ N192)
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)
35% identity, 99% coverage: 1:251/253 of query aligns to 1:242/251 of H9XP47
- N15 (≠ S15) binding
- M17 (≠ I17) binding
- D36 (= D36) binding
- D60 (= D62) binding
- V61 (= V63) binding
- N87 (≠ H89) binding
- S138 (= S141) binding ; binding
- V139 (≠ S142) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (= S143) binding
- Y151 (= Y154) binding ; binding ; binding
- K155 (= K158) binding
- V184 (= V187) binding
- T186 (= T189) binding
- RDK 197:199 (≠ EAY 206:208) 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.
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
35% identity, 98% coverage: 3:251/253 of query aligns to 5:244/252 of 6vspB
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
35% identity, 98% coverage: 3:251/253 of query aligns to 3:242/251 of 6xewA
- active site: G16 (= G16), S138 (= S141), Y151 (= Y154)
- binding r,3-hydroxybutan-2-one: S138 (= S141), S140 (= S143), Y151 (= Y154)
- binding s,3-hydroxybutan-2-one: S138 (= S141), Y151 (= Y154), S182 (≠ G185)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), N15 (≠ S15), G16 (= G16), M17 (≠ I17), D36 (= D36), W37 (≠ R37), W37 (≠ R37), A38 (≠ S38), I59 (≠ V61), D60 (= D62), V61 (= V63), N87 (≠ H89), A88 (= A90), G89 (= G91), V110 (≠ L112), T136 (= T139), S138 (= S141), Y151 (= Y154), K155 (= K158), S182 (≠ G185), L183 (≠ W186), V184 (= V187), T186 (= T189), N187 (≠ P190), M188 (≠ F191), T189 (≠ N192)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
35% identity, 98% coverage: 3:251/253 of query aligns to 3:242/251 of 6vspA
- active site: G16 (= G16), S138 (= S141), Y151 (= Y154)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), N15 (≠ S15), G16 (= G16), M17 (≠ I17), D36 (= D36), W37 (≠ R37), W37 (≠ R37), A38 (≠ S38), I59 (≠ V61), D60 (= D62), V61 (= V63), N87 (≠ H89), A88 (= A90), G89 (= G91), V90 (≠ A92), V110 (≠ L112), T136 (= T139), S138 (= S141), Y151 (= Y154), K155 (= K158), P181 (= P184), S182 (≠ G185), L183 (≠ W186), V184 (= V187), T186 (= T189), N187 (≠ P190), M188 (≠ F191), T189 (≠ N192)
3o03A Quaternary complex structure of gluconate 5-dehydrogenase from streptococcus suis type 2 (see paper)
34% identity, 98% coverage: 3:249/253 of query aligns to 9:245/254 of 3o03A
- active site: G22 (= G16), S147 (= S141), V157 (≠ M151), Y160 (= Y154), K164 (= K158)
- binding calcium ion: S147 (= S141), M148 (≠ S142), P190 (= P184)
- binding D-gluconic acid: I99 (≠ Q93), R101 (≠ A95), S147 (= S141), M149 (≠ S143), R154 (≠ D148), Y160 (= Y154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G12), Y21 (≠ S15), G22 (= G16), I23 (= I17), D42 (= D36), I43 (≠ R37), L47 (≠ A41), D68 (= D62), V69 (= V63), N95 (≠ H89), A96 (= A90), G97 (= G91), I145 (≠ T139), Y160 (= Y154), K164 (= K158), P190 (= P184)
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)
34% identity, 98% coverage: 3:249/253 of query aligns to 4:242/245 of Q8JZV9
- Y147 (= Y154) active site, Proton acceptor; mutation to F: Loss of function.
4nbwA Crystal structure of fabg from plesiocystis pacifica (see paper)
37% identity, 98% coverage: 5:252/253 of query aligns to 1:251/253 of 4nbwA
- active site: G12 (= G16), S146 (= S141), Y159 (= Y154), K163 (= K158)
- binding nicotinamide-adenine-dinucleotide: G8 (= G12), N11 (≠ S15), G12 (= G16), I13 (= I17), D32 (= D36), L33 (≠ R37), V57 (= V61), D58 (= D62), V59 (= V63), N85 (≠ H89), A86 (= A90), G87 (= G91), S146 (= S141), Y159 (= Y154), K163 (= K158), I192 (≠ V187), T194 (= T189)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
35% identity, 98% coverage: 5:253/253 of query aligns to 2:250/250 of 2cfcA
- active site: G13 (= G16), S142 (= S141), Y155 (= Y154), K159 (= K158)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ D148), R152 (≠ M151), Y155 (= Y154), W195 (≠ P194), R196 (≠ F195)
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), S12 (= S15), G13 (= G16), N14 (≠ I17), D33 (= D36), L34 (≠ R37), A59 (≠ V61), D60 (= D62), V61 (= V63), N87 (≠ H89), A88 (= A90), G89 (= G91), I140 (≠ T139), P185 (= P184), G186 (= G185), M187 (≠ W186), I188 (≠ V187), T190 (= T189), P191 (= P190), M192 (≠ F191), T193 (≠ N192)
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, 98% coverage: 5:253/253 of query aligns to 2:250/250 of Q56840
- SGN 12:14 (≠ SGI 15:17) binding
- D33 (= D36) binding
- DV 60:61 (= DV 62:63) binding
- N87 (≠ H89) binding
- S142 (= S141) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ M151) 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 (= Y154) mutation Y->E,F: Loss of activity.
- K159 (= K158) mutation to A: Loss of activity.
- R179 (= R178) mutation to A: Loss of activity.
- IETPM 188:192 (≠ VDTPF 187:191) binding
- WR 195:196 (≠ PF 194:195) binding
- R196 (≠ F195) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (= R202) mutation to A: Slight decrease in catalytic efficiency.
- R209 (= R212) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
34% identity, 98% coverage: 1:249/253 of query aligns to 1:244/247 of 4jroC
- active site: G16 (= G16), S142 (= S141), Q152 (≠ M151), Y155 (= Y154), K159 (= K158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ G14), R15 (≠ S15), G16 (= G16), I17 (= I17), N35 (vs. gap), Y36 (≠ V35), N37 (≠ D36), G38 (≠ R37), S39 (= S38), N63 (≠ D62), V64 (= V63), N90 (≠ H89), A91 (= A90), I93 (≠ A92), I113 (≠ L112), S142 (= S141), Y155 (= Y154), K159 (= K158), P185 (= P184), I188 (≠ V187), T190 (= T189)
Query Sequence
>SMc01635 FitnessBrowser__Smeli:SMc01635
MILNNRIAIVTGAGSGIGRAGAAIMAREGAHVVVVDRSVEAAGDTVAAIAAGGGSAEALA
VDVTDDDALADGIADILYRHGRIDILHNHAGAQVAGDLEEVEVAGFDRSWNLNVRAHFMA
ARLVMPSMKKAGRGVIVNTSSSSGVLYDREMIAYTTTKHAVIAMTRQMAGDYAKYGVRVN
ALCPGWVDTPFNEPFIDQMGGREAIEAYIRERVPLGRWASVDEIAESILFLVSDRSSYMT
GQILVVDGGETVV
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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