SitesBLAST
Comparing WP_052665079.1 NCBI__GCF_000969705.1:WP_052665079.1 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)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
53% identity, 99% coverage: 1:255/257 of query aligns to 6:256/258 of 4wecA
- active site: G21 (= G16), S143 (= S143), Q154 (= Q154), Y157 (= Y157), K161 (= K161)
- binding nicotinamide-adenine-dinucleotide: G17 (= G12), A19 (= A14), S20 (≠ G15), G21 (= G16), I22 (= I17), D41 (= D36), I42 (≠ L37), V61 (= V61), D62 (= D62), V63 (= V63), N89 (= N89), T141 (= T141), Y157 (= Y157), K161 (= K161), P187 (= P187), P189 (= P189), V190 (≠ L190)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
38% identity, 97% coverage: 3:251/257 of query aligns to 3:247/248 of 6ixmC
- active site: G16 (= G16), S142 (= S143), Y155 (= Y157), K159 (= K161)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), S15 (≠ G15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (≠ L37), A61 (≠ V61), D62 (= D62), T63 (≠ V63), N89 (= N89), A90 (= A90), M140 (≠ T141), S142 (= S143), Y155 (= Y157), K159 (= K161), P185 (= P187), A186 (≠ G188), Y187 (≠ P189), I188 (≠ L190), L192 (= L194)
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
42% identity, 97% coverage: 1:249/257 of query aligns to 1:248/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), Q15 (≠ G15), G16 (= G16), I17 (= I17), D36 (= D36), V63 (= V63), N89 (= N89), A91 (≠ G91), S94 (vs. gap), I142 (≠ T141), S143 (≠ A142), S144 (= S143), Y157 (= Y157), K161 (= K161), P187 (= P187), H188 (≠ G188), I190 (≠ L190), I194 (≠ L194)
8y83A Crystal structure of a ketoreductase from sphingobacterium siyangense sy1 with co-enzyme (see paper)
40% identity, 97% coverage: 3:251/257 of query aligns to 4:248/249 of 8y83A
- binding nicotinamide-adenine-dinucleotide: G13 (= G12), S16 (≠ G15), G17 (= G16), I18 (= I17), D37 (= D36), I38 (≠ L37), A62 (≠ V61), D63 (= D62), S64 (≠ V63), N90 (= N89), M141 (≠ T141), Y156 (= Y157), K160 (= K161), P186 (= P187), G187 (= G188), Y188 (≠ P189), I189 (≠ L190), L193 (= L194)
7djsD Crystal structure of isopiperitenol dehydrogenase from pseudomonas aeruginosa complexed with NAD
43% identity, 97% coverage: 3:251/257 of query aligns to 3:250/251 of 7djsD
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G16 (= G16), I17 (= I17), D36 (= D36), L37 (= L37), C61 (≠ V61), D62 (= D62), V63 (= V63), N89 (= N89), A90 (= A90), T140 (= T141), S142 (= S143), Y155 (= Y157), K159 (= K161), A186 (≠ G188), V187 (≠ P189)
5jc8D Crystal structure of a putative short-chain dehydrogenase/reductase from burkholderia xenovorans
37% identity, 97% coverage: 2:251/257 of query aligns to 3:259/262 of 5jc8D
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
37% identity, 98% coverage: 2:253/257 of query aligns to 10:267/267 of Q9LBG2
- 17:42 (vs. 9:34, 58% identical) binding NAD(+)
- E103 (vs. gap) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
1iy8A Crystal structure of levodione reductase (see paper)
37% identity, 98% coverage: 2:253/257 of query aligns to 1:258/258 of 1iy8A
- active site: G15 (= G16), S143 (= S143), Q153 (= Q154), Y156 (= Y157), K160 (= K161)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), S14 (≠ G15), G15 (= G16), L16 (≠ I17), D35 (= D36), V36 (≠ L37), A62 (≠ V61), D63 (= D62), V64 (= V63), N90 (= N89), G92 (= G91), I93 (= I92), T141 (= T141), S143 (= S143), Y156 (= Y157), K160 (= K161), P186 (= P187), G187 (= G188), T191 (= T192), P192 (≠ E193), M193 (≠ L194)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)- hydroxypropylethane thiosulfonate dehydrogenases (see paper)
39% identity, 96% coverage: 6:251/257 of query aligns to 3:249/250 of 2cfcA
- active site: G13 (= G16), S142 (= S143), Y155 (= Y157), K159 (= K161)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ A151), R152 (≠ Q154), Y155 (= Y157), W195 (≠ K197), R196 (≠ F198)
- binding nicotinamide-adenine-dinucleotide: G9 (= G12), S12 (≠ G15), G13 (= G16), N14 (≠ I17), D33 (= D36), L34 (= L37), A59 (≠ V61), D60 (= D62), V61 (= V63), N87 (= N89), A88 (= A90), G89 (= G91), I140 (≠ T141), P185 (= P187), G186 (= G188), M187 (≠ P189), I188 (≠ L190), T190 (= T192), P191 (≠ E193), M192 (≠ L194), T193 (≠ L195)
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)
39% identity, 96% coverage: 6:251/257 of query aligns to 3:249/250 of Q56840
- SGN 12:14 (≠ GGI 15:17) binding NAD(+)
- D33 (= D36) binding NAD(+)
- DV 60:61 (= DV 62:63) binding NAD(+)
- N87 (= N89) binding NAD(+)
- S142 (= S143) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ Q154) binding 2-oxopropyl-coenzyme M; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- Y155 (= Y157) mutation Y->E,F: Loss of activity.
- K159 (= K161) mutation to A: Loss of activity.
- R179 (= R181) mutation to A: Loss of activity.
- IETPM 188:192 (≠ LHTEL 190:194) binding NAD(+)
- WR 195:196 (≠ KF 197:198) binding 2-oxopropyl-coenzyme M
- R196 (≠ F198) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (≠ K205) mutation to A: Slight decrease in catalytic efficiency.
- R209 (≠ H211) 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)
36% identity, 96% coverage: 1:248/257 of query aligns to 1:244/248 of 4urfB
- active site: G16 (= G16), S142 (= S143), I152 (≠ A151), Y155 (= Y157), K159 (= K161)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (≠ M214), R211 (≠ G215), R212 (= R216)
- binding bicarbonate ion: I92 (= I92), G94 (≠ H94), R109 (≠ L110), R179 (= R181), S228 (= S232)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G14 (≠ A14), N15 (≠ G15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (≠ L37), D62 (= D62), T63 (≠ V63), N89 (= N89), A90 (= A90), G91 (= G91), I140 (≠ T141), Y155 (= Y157), K159 (= K161), P185 (= P187), A186 (≠ G188), I188 (≠ L190), T190 (= T192)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
36% identity, 96% coverage: 1:248/257 of query aligns to 1:244/248 of 4urfA
- active site: G16 (= G16), S142 (= S143), I152 (≠ A151), Y155 (= Y157), K159 (= K161)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (= I92), S93 (≠ M93), G94 (≠ H94), E95 (≠ P95), T97 (≠ D97), E101 (≠ I101), T103 (= T103), Q106 (≠ T107), R109 (≠ L110), S175 (≠ R177), G177 (≠ N179)
- binding magnesium ion: S237 (= S241), Y238 (≠ T242)
- binding nicotinamide-adenine-dinucleotide: G12 (= G12), G14 (≠ A14), N15 (≠ G15), G16 (= G16), I17 (= I17), D36 (= D36), I37 (≠ L37), W41 (≠ G41), D62 (= D62), T63 (≠ V63), N89 (= N89), A90 (= A90), G91 (= G91), I140 (≠ T141), Y155 (= Y157), K159 (= K161), P185 (= P187), I188 (≠ L190), T190 (= T192)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
36% identity, 96% coverage: 1:248/257 of query aligns to 1:244/248 of 4ureB
- active site: G16 (= G16), S142 (= S143), I152 (≠ A151), Y155 (= Y157), K159 (= K161)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ G15), G16 (= G16), I17 (= I17), N89 (= N89), G91 (= G91), Y155 (= Y157), P185 (= P187), A186 (≠ G188)
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)
36% identity, 97% coverage: 1:250/257 of query aligns to 1:244/248 of Q9KJF1
- M1 (= M1) modified: Initiator methionine, Removed
- S15 (≠ G15) binding NAD(+)
- D36 (= D36) binding NAD(+)
- D62 (= D62) binding NAD(+)
- I63 (≠ V63) binding NAD(+)
- N89 (= N89) binding NAD(+)
- Y153 (= Y157) binding NAD(+)
- K157 (= K161) binding NAD(+)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
39% identity, 98% coverage: 1:251/257 of query aligns to 3:254/255 of 5itvA
- active site: G18 (= G16), S141 (= S143), Y154 (= Y157), K158 (= K161)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), S17 (≠ G15), G18 (= G16), I19 (= I17), D38 (= D36), I39 (≠ L37), T61 (≠ V61), I63 (≠ V63), N89 (= N89), G91 (= G91), T139 (= T141), S141 (= S143), Y154 (= Y157), K158 (= K161), P184 (= P187), G185 (= G188), I186 (≠ P189), I187 (≠ L190)
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
36% identity, 96% coverage: 3:250/257 of query aligns to 2:243/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), M16 (≠ I17), D35 (= D36), I36 (≠ L37), I62 (≠ V63), N88 (= N89), G90 (= G91), I138 (≠ T141), S140 (= S143), Y152 (= Y157), K156 (= K161), I185 (≠ L190)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
36% identity, 96% coverage: 2:249/257 of query aligns to 4:242/244 of 4nbuB
- active site: G18 (= G16), N111 (= N115), S139 (= S143), Q149 (= Q154), Y152 (= Y157), K156 (= K161)
- binding acetoacetyl-coenzyme a: D93 (≠ P95), K98 (≠ A100), S139 (= S143), N146 (≠ A150), V147 (≠ A151), Q149 (= Q154), Y152 (= Y157), F184 (≠ P189), M189 (≠ L194), K200 (= K205)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G12), N17 (≠ G15), G18 (= G16), I19 (= I17), D38 (= D36), F39 (≠ L37), V59 (= V61), D60 (= D62), V61 (= V63), N87 (= N89), A88 (= A90), G89 (= G91), I90 (= I92), T137 (= T141), S139 (= S143), Y152 (= Y157), K156 (= K161), P182 (= P187), F184 (≠ P189), T185 (≠ L190), T187 (= T192), M189 (≠ L194)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
35% identity, 96% coverage: 3:250/257 of query aligns to 5:252/254 of 4fn4A
- active site: G18 (= G16), S144 (= S143), Y157 (= Y157), K161 (= K161), S202 (≠ D202)
- binding nicotinamide-adenine-dinucleotide: G14 (= G12), S17 (≠ G15), G18 (= G16), I19 (= I17), E38 (≠ D36), L39 (= L37), R43 (≠ G41), A63 (≠ V61), D64 (= D62), V65 (= V63), N91 (= N89), G93 (= G91), I94 (= I92), T142 (= T141), S144 (= S143), Y157 (= Y157), K161 (= K161), P187 (= P187), V190 (≠ L190), T192 (= T192), N193 (≠ E193), I194 (≠ L194)
5epoA The three-dimensional structure of clostridium absonum 7alpha- hydroxysteroid dehydrogenase (see paper)
36% identity, 97% coverage: 2:250/257 of query aligns to 2:249/261 of 5epoA
- active site: G16 (= G16), T144 (≠ V147), I152 (vs. gap), Y157 (= Y157), K161 (= K161), R193 (≠ E193)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S12 (≠ G12), T14 (≠ A14), R15 (≠ G15), G16 (= G16), I17 (= I17), R37 (≠ L37), F61 (≠ V61), N62 (≠ D62), N89 (= N89), Y90 (≠ A90), G91 (= G91), Y157 (= Y157), K161 (= K161), P187 (= P187), G188 (= G188), I190 (≠ L190), T192 (= T192), R193 (≠ E193), A194 (≠ L194), A195 (≠ L195)
- binding taurochenodeoxycholic acid: T93 (≠ M93), T144 (≠ V147), G146 (= G149), R154 (≠ Q154), Y157 (= Y157), G188 (= G188), N198 (≠ F198), M199 (≠ L199), F203 (≠ K204)
G9FRD7 7alpha-hydroxysteroid dehydrogenase; 7alpha-HSDH; NADP-dependent 7alpha-hydroxysteroid dehydrogenase; EC 1.1.1.- from Clostridium sardiniense (Clostridium absonum) (see 2 papers)
36% identity, 97% coverage: 2:250/257 of query aligns to 3:250/262 of G9FRD7
- SSTRGI 13:18 (≠ GAAGGI 12:17) binding NADP(+)
- R38 (≠ L37) binding NADP(+); mutation to D: Loss of catalytic activity.
- NA 63:64 (≠ DV 62:63) binding NADP(+)
- N90 (= N89) binding NADP(+)
- T145 (≠ V147) binding taurochenodeoxycholate
- Y158 (= Y157) binding NADP(+); binding taurochenodeoxycholate
- K162 (= K161) binding NADP(+)
- IGTRA 191:195 (≠ LHTEL 190:194) binding NADP(+)
Sites not aligning to the query:
- 261:262 mutation Missing: 5-fold reduction in catalytic efficiency.
Query Sequence
>WP_052665079.1 NCBI__GCF_000969705.1:WP_052665079.1
MRLQDKVALITGAAGGIGRASALRFAAEGALVTCADLDGDGAQRTADAVTGAGGRALAVT
VDVSRSEDCERMVAATEDAFGRLDVLFNNAGIMHPADDDAIATDESTWDLTMAVNVKGVY
LGCKHGIPALRRAGGGSIINTASFVAVMGAATPQLAYTASKGAVLALSRELGVLHARENI
RVNALCPGPLHTELLMKFLDTDEKKQRRLVHLPMGRFGEAAEMADAALYLASDESSYVNA
STFLVDGGLSSAYVTAE
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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