SitesBLAST
Comparing Ga0059261_2792 FitnessBrowser__Korea:Ga0059261_2792 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)
2d1yA Crystal structure of tt0321 from thermus thermophilus hb8 (see paper)
43% identity, 98% coverage: 3:244/246 of query aligns to 3:237/240 of 2d1yA
- active site: G16 (= G16), S135 (= S136), N145 (≠ G146), Y148 (= Y150), K152 (= K154)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), R15 (≠ S15), I17 (= I17), D36 (= D36), L37 (≠ R37), R38 (≠ S38), V55 (≠ A56), D56 (= D57), L57 (= L58), N83 (≠ G84), A84 (= A85), A85 (≠ G86), I86 (= I87), V133 (≠ I134), S135 (= S136), Y148 (= Y150), K152 (= K154), P178 (= P179), G179 (= G180), I181 (≠ V182), T183 (= T184), A185 (≠ G189), V186 (= V190)
5t5qC Crystal structure of short-chain dehydrogenase/reductase sdr:glucose/ribitol dehydrogenase from brucella melitensis
39% identity, 98% coverage: 1:242/246 of query aligns to 3:241/245 of 5t5qC
- active site: G18 (= G16), S140 (= S136), N150 (≠ I147), Y153 (= Y150), K157 (= K154)
- binding nicotinamide-adenine-dinucleotide: N16 (≠ A14), G17 (≠ S15), G18 (= G16), I19 (= I17), D38 (= D36), L39 (≠ R37), D63 (vs. gap), A64 (vs. gap), S90 (≠ G84), I113 (= I107), Y153 (= Y150), K157 (= K154), P182 (= P179), I185 (≠ V182), T187 (= T184), M189 (= M186)
7xqmB Indel-mutant short chain dehydrogenase bound to sah (see paper)
40% identity, 98% coverage: 3:244/246 of query aligns to 4:243/253 of 7xqmB
- binding s-adenosyl-l-homocysteine: G13 (= G12), I16 (= I17), D34 (= D36), L35 (≠ R37), R36 (≠ S38), V53 (≠ A56), L55 (= L58), N81 (≠ G84), A82 (= A85), A83 (≠ G86), Y146 (= Y150)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
36% identity, 96% coverage: 9:244/246 of query aligns to 9:246/248 of 6ixmC
- active site: G16 (= G16), S142 (= S136), Y155 (= Y150), K159 (= K154)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (= S15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (≠ R37), A61 (= A56), D62 (= D57), T63 (≠ L58), N89 (≠ G84), A90 (= A85), M140 (≠ I134), S142 (= S136), Y155 (= Y150), K159 (= K154), P185 (= P179), A186 (≠ G180), Y187 (≠ I181), I188 (≠ V182), L192 (≠ M186)
6d9yB Crystal structure of a short chain dehydrogenase/reductase sdr from burkholderia phymatum with partially occupied NAD
39% identity, 99% coverage: 1:243/246 of query aligns to 5:248/251 of 6d9yB
- active site: G20 (= G16), S145 (= S136), Y158 (= Y150)
- binding nicotinamide-adenine-dinucleotide: G16 (= G12), R19 (≠ S15), G20 (= G16), D40 (= D36), L41 (≠ R37), V64 (≠ A56), D65 (= D57), Q66 (≠ L58), A93 (= A85), S145 (= S136), Y158 (= Y150), K162 (= K154), P188 (= P179), A189 (≠ G180), A190 (≠ I181), A191 (≠ V182), T193 (= T184)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
32% identity, 99% coverage: 1:244/246 of query aligns to 3:253/255 of 5itvA
- active site: G18 (= G16), S141 (= S136), Y154 (= Y150), K158 (= K154)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), S17 (= S15), G18 (= G16), I19 (= I17), D38 (= D36), I39 (≠ R37), T61 (≠ A56), I63 (≠ L58), N89 (≠ G84), G91 (= G86), T139 (≠ I134), S141 (= S136), Y154 (= Y150), K158 (= K154), P184 (= P179), G185 (= G180), I186 (= I181), I187 (≠ V182)
2q2qD Structure of d-3-hydroxybutyrate dehydrogenase from pseudomonas putida (see paper)
38% identity, 98% coverage: 3:242/246 of query aligns to 2:251/255 of 2q2qD
- active site: G15 (= G16), S138 (= S136), Y151 (= Y150), K155 (= K154), R196 (≠ Y194)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), T13 (≠ A14), S14 (= S15), G15 (= G16), I16 (= I17), F36 (≠ R37), D59 (= D57), L60 (= L58), N86 (≠ G84), G88 (= G86), L109 (≠ I107), I136 (= I134), S138 (= S136), Y151 (= Y150), K155 (= K154), P181 (= P179), G182 (= G180), W183 (≠ I181), V184 (= V182), T186 (= T184), L188 (≠ M186), V189 (= V187)
3toxA Crystal structure of a short chain dehydrogenase in complex with NAD(p) from sinorhizobium meliloti 1021
39% identity, 98% coverage: 2:242/246 of query aligns to 2:249/254 of 3toxA
- active site: G16 (= G16), S142 (= S136), V153 (≠ I147), Y156 (= Y150), K160 (= K154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (≠ A14), S15 (= S15), G16 (= G16), I17 (= I17), A36 (≠ D36), R37 (= R37), N38 (≠ S38), V63 (≠ L58), N89 (≠ G84), A90 (= A85), G91 (= G86), T140 (≠ I134), S142 (= S136), Y156 (= Y150), K160 (= K154), P186 (= P179), G188 (≠ I181), T189 (≠ V182), T191 (= T184)
5itvD Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
32% identity, 99% coverage: 1:244/246 of query aligns to 3:225/227 of 5itvD
- active site: G18 (= G16), S141 (= S136), Y154 (= Y150), K158 (= K154)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), S17 (= S15), G18 (= G16), I19 (= I17), D38 (= D36), I39 (≠ R37), T61 (≠ A56), D62 (= D57), I63 (≠ L58), N89 (≠ G84), T139 (≠ I134), S141 (= S136), Y154 (= Y150), K158 (= K154), P184 (= P179), G185 (= G180), I187 (≠ V182)
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)
40% identity, 89% coverage: 27:244/246 of query aligns to 29:253/255 of A7IQH5
- D38 (= D36) binding
- DV 64:65 (≠ DL 57:58) binding
- N91 (≠ G84) binding
- S143 (= S136) binding ; mutation to A: Retains very weak activity.
- Y156 (= Y150) binding ; mutation to A: Retains some activity but with more than 2200-fold decrease in catalytic efficiency.; mutation to F: Loss of activity.
- K160 (= K154) binding ; mutation to A: Loss of activity.
- T188 (≠ I181) binding
- VTSTG 189:193 (≠ V-DTP 182:185) binding
- R211 (vs. gap) 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 (≠ Q205) 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 (= Y206) binding
Sites not aligning to the query:
4ituA Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) bound to s-hpc and nadh (see paper)
40% identity, 89% coverage: 27:244/246 of query aligns to 27:251/253 of 4ituA
- active site: N113 (= N108), S141 (= S136), Y154 (= Y150), K158 (= K154)
- binding 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonic acid: S141 (= S136), Y154 (= Y150), T186 (≠ I181), R209 (vs. gap), Y213 (= Y206)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D36 (= D36), L37 (≠ R37), D62 (= D57), V63 (≠ L58), N89 (≠ G84), V112 (≠ I107), F139 (≠ I134), S141 (= S136), Y154 (= Y150), K158 (= K154), P184 (= P179), T186 (≠ I181), V187 (= V182), T190 (= T184), M192 (= M186)
Sites not aligning to the query:
4nbuB Crystal structure of fabg from bacillus sp (see paper)
34% identity, 98% coverage: 2:242/246 of query aligns to 4:241/244 of 4nbuB
- active site: G18 (= G16), N111 (= N108), S139 (= S136), Q149 (≠ I147), Y152 (= Y150), K156 (= K154)
- binding acetoacetyl-coenzyme a: D93 (≠ S90), K98 (≠ A95), S139 (= S136), N146 (= N143), V147 (≠ A144), Q149 (≠ I147), Y152 (= Y150), F184 (≠ I181), M189 (= M186), K200 (≠ P201)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ S15), G18 (= G16), I19 (= I17), D38 (= D36), F39 (≠ R37), V59 (≠ A56), D60 (= D57), V61 (≠ L58), N87 (≠ G84), A88 (= A85), G89 (= G86), I90 (= I87), T137 (≠ I134), S139 (= S136), Y152 (= Y150), K156 (= K154), P182 (= P179), F184 (≠ I181), T185 (≠ V182), T187 (= T184), M189 (= M186)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
35% identity, 97% coverage: 6:244/246 of query aligns to 3:248/250 of 2cfcA
- active site: G13 (= G16), S142 (= S136), Y155 (= Y150), K159 (= K154)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ A144), R152 (≠ I147), Y155 (= Y150), W195 (≠ G189), R196 (≠ V190)
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), S12 (= S15), G13 (= G16), N14 (≠ I17), D33 (= D36), L34 (≠ R37), A59 (= A56), D60 (= D57), V61 (≠ L58), N87 (≠ G84), A88 (= A85), G89 (= G86), I140 (= I134), P185 (= P179), G186 (= G180), M187 (≠ I181), I188 (≠ V182), T190 (= T184), P191 (= P185), M192 (= M186), T193 (≠ V187)
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: 6:244/246 of query aligns to 3:248/250 of Q56840
- SGN 12:14 (≠ SGI 15:17) binding
- D33 (= D36) binding
- DV 60:61 (≠ DL 57:58) binding
- N87 (≠ G84) binding
- S142 (= S136) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ I147) 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 (= Y150) mutation Y->E,F: Loss of activity.
- K159 (= K154) mutation to A: Loss of activity.
- R179 (= R173) mutation to A: Loss of activity.
- IETPM 188:192 (≠ VDTPM 182:186) binding
- WR 195:196 (≠ GV 189:190) binding
- R196 (≠ V190) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (≠ Q204) mutation to A: Slight decrease in catalytic efficiency.
- R209 (= R210) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
37% identity, 98% coverage: 2:242/246 of query aligns to 7:249/258 of 4wecA
- active site: G21 (= G16), S143 (= S136), Q154 (≠ I147), Y157 (= Y150), K161 (= K154)
- binding nicotinamide-adenine-dinucleotide: G17 (= G12), A19 (= A14), S20 (= S15), G21 (= G16), I22 (= I17), D41 (= D36), I42 (≠ R37), V61 (≠ A56), D62 (= D57), V63 (≠ L58), N89 (≠ G84), T141 (≠ I134), Y157 (= Y150), K161 (= K154), P187 (= P179), P189 (≠ I181), V190 (= V182)
1iy8A Crystal structure of levodione reductase (see paper)
36% identity, 99% coverage: 2:244/246 of query aligns to 1:255/258 of 1iy8A
- active site: G15 (= G16), S143 (= S136), Q153 (≠ A144), Y156 (= Y150), K160 (= K154)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (= S15), G15 (= G16), L16 (≠ I17), D35 (= D36), V36 (≠ R37), A62 (= A56), D63 (= D57), V64 (≠ L58), N90 (≠ G84), G92 (= G86), I93 (= I87), T141 (≠ I134), S143 (= S136), Y156 (= Y150), K160 (= K154), P186 (= P179), G187 (= G180), T191 (= T184), P192 (= P185), M193 (= M186)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
36% identity, 99% coverage: 2:244/246 of query aligns to 10:264/267 of Q9LBG2
- 17:42 (vs. 9:34, 65% identical) binding
- E103 (≠ A88) 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
36% identity, 100% coverage: 1:246/246 of query aligns to 1:244/244 of 7krmC
- active site: G18 (= G16), S140 (= S136), Y155 (= Y150)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (= S15), G18 (= G16), I19 (= I17), D38 (= D36), L39 (≠ R37), A60 (= A56), N61 (≠ D57), V62 (≠ L58), N88 (≠ G84), V111 (≠ I107), S140 (= S136), Y155 (= Y150), K159 (= K154), I188 (≠ V182), T190 (= T184)
5jydB Crystal structure of a putative short chain dehydrogenase from burkholderia cenocepacia
39% identity, 98% coverage: 2:242/246 of query aligns to 44:288/292 of 5jydB
- active site: G58 (= G16), S184 (= S136), L194 (≠ I147), Y197 (= Y150), K201 (= K154), P242 (≠ R196)
- binding magnesium ion: D56 (≠ A14), S57 (= S15), E82 (≠ D36)
- binding nicotinamide-adenine-dinucleotide: G54 (= G12), D56 (≠ A14), S57 (= S15), G58 (= G16), I59 (= I17), L79 (vs. gap), E82 (≠ D36), D106 (= D57), I107 (≠ L58), N133 (≠ G84), A134 (= A85), A135 (= A88), T182 (≠ I134), S184 (= S136), Y197 (= Y150), K201 (= K154), P227 (= P179), G228 (= G180), P229 (≠ I181), Y230 (≠ V182), T232 (= T184), L234 (≠ M186), Q235 (≠ V187)
4gh5A Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) (see paper)
40% identity, 89% coverage: 27:244/246 of query aligns to 27:246/248 of 4gh5A
- active site: N113 (= N108), S141 (= S136), Y154 (= Y150), K158 (= K154)
- binding nicotinamide-adenine-dinucleotide: D36 (= D36), L37 (≠ R37), A61 (= A56), D62 (= D57), V63 (≠ L58), N89 (≠ G84), A90 (= A85), V112 (≠ I107), F139 (≠ I134), S141 (= S136), Y154 (= Y150), K158 (= K154), P184 (= P179), V187 (= V182), T190 (= T184), G191 (≠ P185), M192 (= M186)
Sites not aligning to the query:
Query Sequence
>Ga0059261_2792 FitnessBrowser__Korea:Ga0059261_2792
MKLAGRRILITGAASGIGRATAELFAREGAALALLDRSDDLLRSAAQASGGTAVLADLAD
EAQLLAAVAKAAQAMGGIDGIVNGAGIAGSQPLDALDRESWDRFVAINLTAPYLICRAAL
PHLQVTGNATIVNIASGQALLPNAPGIAAYAATKAGLVAFTKALGAELAPRIRANVVAPG
IVDTPMVQGVLGGYARPDDAPFVQQYAMKRVARPSELAEAILFLSSEASSYVTGTVLAVD
GGRTFH
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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