SitesBLAST
Comparing RR42_RS23420 FitnessBrowser__Cup4G11:RR42_RS23420 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
70% identity, 100% coverage: 2:266/266 of query aligns to 1:262/262 of 5jc8D
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
38% identity, 97% coverage: 5:263/266 of query aligns to 2:244/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G14), M16 (≠ N24), D35 (= D43), I36 (≠ K44), I62 (≠ V70), N88 (= N96), G90 (= G98), I138 (≠ T146), S140 (= S148), Y152 (= Y162), K156 (= K166), I185 (≠ M195)
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)
38% identity, 97% coverage: 5:263/266 of query aligns to 3:245/248 of Q9KJF1
- S15 (≠ C17) binding
- D36 (= D43) binding
- D62 (= D69) binding
- I63 (≠ V70) binding
- N89 (= N96) binding
- Y153 (= Y162) binding
- K157 (= K166) binding
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+
39% identity, 97% coverage: 5:261/266 of query aligns to 3:245/247 of 4jroC
- active site: G16 (= G23), S142 (= S148), Q152 (= Q159), Y155 (= Y162), K159 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (≠ G16), R15 (≠ W22), G16 (= G23), I17 (≠ N24), N35 (≠ D43), Y36 (≠ K44), N37 (= N45), G38 (≠ Q46), S39 (≠ D47), N63 (≠ D69), V64 (= V70), N90 (= N96), A91 (≠ V97), I93 (≠ G99), I113 (≠ F119), S142 (= S148), Y155 (= Y162), K159 (= K166), P185 (= P192), I188 (≠ M195), T190 (= T197)
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, 97% coverage: 4:262/266 of query aligns to 10:264/267 of Q9LBG2
- 17:42 (vs. 11:41, 48% identical) binding
- E103 (≠ S100) 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, 97% coverage: 4:262/266 of query aligns to 1:255/258 of 1iy8A
- active site: G15 (= G23), S143 (= S148), Q153 (= Q159), Y156 (= Y162), K160 (= K166)
- binding nicotinamide-adenine-dinucleotide: G11 (= G14), S14 (≠ C17), G15 (= G23), L16 (≠ N24), D35 (= D43), V36 (≠ K44), A62 (≠ C68), D63 (= D69), V64 (= V70), N90 (= N96), G92 (= G98), I93 (≠ G99), T141 (= T146), S143 (= S148), Y156 (= Y162), K160 (= K166), P186 (= P192), G187 (= G193), T191 (= T197), P192 (= P198), M193 (= M199)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
36% identity, 98% coverage: 3:262/266 of query aligns to 1:246/248 of 6ixmC
- active site: G16 (= G23), S142 (= S148), Y155 (= Y162), K159 (= K166)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), S15 (≠ C17), G16 (= G23), I17 (≠ N24), D36 (= D43), I37 (≠ K44), A61 (≠ C68), D62 (= D69), T63 (≠ V70), N89 (= N96), A90 (≠ V97), M140 (≠ T146), S142 (= S148), Y155 (= Y162), K159 (= K166), P185 (= P192), A186 (≠ G193), Y187 (≠ Q194), I188 (≠ M195), L192 (≠ M199)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
37% identity, 96% coverage: 8:262/266 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 (≠ W154), R152 (≠ S157), Y155 (= Y162), W195 (≠ A202), R196 (= R203)
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), S12 (≠ C17), G13 (= G23), N14 (= N24), D33 (= D43), L34 (≠ K44), A59 (≠ C68), D60 (= D69), V61 (= V70), N87 (= N96), A88 (≠ V97), G89 (= G98), I140 (≠ T146), P185 (= P192), G186 (= G193), M187 (≠ Q194), I188 (≠ M195), T190 (= T197), P191 (= P198), M192 (= M199), T193 (≠ V200)
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, 96% coverage: 8:262/266 of query aligns to 3:248/250 of Q56840
- S-----GN 12:14 (≠ CVGPGWGN 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 (≠ S157) 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 (≠ MHTPM 195:199) binding
- WR 195:196 (≠ AR 202:203) binding
- R196 (= R203) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (≠ L217) mutation to A: Slight decrease in catalytic efficiency.
- R209 (= R223) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
A0R518 Putative short-chain type dehydrogenase/reductase MSMEG_6031/MSMEI_5872; EC 1.1.1.- from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
36% identity, 99% coverage: 1:264/266 of query aligns to 1:279/279 of A0R518
- K65 (≠ A57) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
35% identity, 98% coverage: 1:262/266 of query aligns to 4:251/258 of 4wecA
- active site: G21 (= G19), S143 (= S148), Q154 (= Q159), Y157 (= Y162), K161 (= K166)
- binding nicotinamide-adenine-dinucleotide: G17 (= G14), A19 (≠ C17), S20 (≠ V18), G21 (= G19), I22 (≠ P20), D41 (= D43), I42 (≠ K44), V61 (≠ C68), D62 (= D69), V63 (= V70), N89 (= N96), T141 (= T146), Y157 (= Y162), K161 (= K166), P187 (= P192), P189 (≠ Q194), V190 (≠ M195)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
38% identity, 97% coverage: 5:263/266 of query aligns to 5:253/254 of 4fn4A
- active site: G18 (= G23), S144 (= S148), Y157 (= Y162), K161 (= K166), S202 (≠ Q207)
- binding nicotinamide-adenine-dinucleotide: G14 (= G14), S17 (≠ C17), G18 (= G23), I19 (≠ N24), E38 (≠ D43), L39 (≠ K44), R43 (≠ P48), A63 (≠ C68), D64 (= D69), V65 (= V70), N91 (= N96), G93 (= G98), I94 (≠ G99), T142 (= T146), S144 (= S148), Y157 (= Y162), K161 (= K166), P187 (= P192), V190 (≠ M195), T192 (= T197), N193 (≠ P198), I194 (≠ M199)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
38% identity, 97% coverage: 5:261/266 of query aligns to 2:240/243 of 1q7bA
- active site: G15 (= G23), E101 (≠ D112), S137 (= S148), Q147 (= Q159), Y150 (= Y162), K154 (= K166)
- binding calcium ion: E232 (≠ T253), T233 (≠ E254)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G14), S13 (≠ G16), R14 (≠ W22), T36 (≠ K44), N58 (≠ D69), V59 (= V70), N85 (= N96), A86 (≠ V97), G87 (= G98), I88 (≠ G99), S137 (= S148), Y150 (= Y162), K154 (= K166), P180 (= P192), G181 (= G193), I183 (≠ M195)
P0AEK2 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Escherichia coli (strain K12) (see 2 papers)
38% identity, 97% coverage: 5:261/266 of query aligns to 3:241/244 of P0AEK2
- GAS-----R 12:15 (≠ GAGCVGPGW 14:22) binding
- T37 (≠ K44) binding
- NV 59:60 (≠ DV 69:70) binding
- N86 (= N96) binding
- Y151 (= Y162) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YASAK 162:166) binding
- A154 (= A165) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K166) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ M195) binding
- E233 (≠ T253) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 97% coverage: 4:261/266 of query aligns to 4:242/244 of 4nbuB
- active site: G18 (= G23), N111 (= N120), S139 (= S148), Q149 (= Q159), Y152 (= Y162), K156 (= K166)
- binding acetoacetyl-coenzyme a: D93 (≠ K102), K98 (≠ Q107), S139 (= S148), N146 (≠ G156), V147 (≠ S157), Q149 (= Q159), Y152 (= Y162), F184 (≠ Q194), M189 (= M199), K200 (≠ Q219)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), N17 (≠ C17), G18 (= G23), I19 (≠ N24), D38 (= D43), F39 (≠ K44), V59 (≠ C68), D60 (= D69), V61 (= V70), N87 (= N96), A88 (≠ V97), G89 (= G98), I90 (≠ G99), T137 (= T146), S139 (= S148), Y152 (= Y162), K156 (= K166), P182 (= P192), F184 (≠ Q194), T185 (≠ M195), T187 (= T197), M189 (= M199)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
38% identity, 97% coverage: 5:261/266 of query aligns to 2:240/243 of 1q7cA
- active site: G15 (= G23), S137 (= S148), Q147 (= Q159), F150 (≠ Y162), K154 (= K166)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G14), S13 (≠ G16), R14 (≠ W22), A35 (≠ D43), T36 (≠ K44), L57 (≠ C68), N58 (≠ D69), V59 (= V70), G87 (= G98), I88 (≠ G99)
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
32% identity, 98% coverage: 1:262/266 of query aligns to 1:251/261 of 1g6kA
- active site: G18 (= G23), S145 (= S148), Y158 (= Y162), K162 (= K166)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ C17), G18 (= G23), L19 (≠ N24), R39 (≠ D43), D65 (= D69), V66 (= V70), N92 (= N96), A93 (≠ V97), G94 (= G98), M143 (≠ T146), 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: 1:262/266 of query aligns to 1:251/261 of P40288
- 11:35 (vs. 11:40, 40% identical) binding
- E96 (≠ S100) mutation E->A,G,K: Heat stable.
- D108 (= D112) mutation to N: Heat stable.
- V112 (≠ Q116) mutation to A: Heat stable.
- E133 (= E136) mutation to K: Heat stable.
- V183 (= V187) mutation to I: Heat stable.
- P194 (= P198) mutation to Q: Heat stable.
- E210 (≠ D214) mutation to K: Heat stable.
- Y217 (≠ F228) 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.
3toxA Crystal structure of a short chain dehydrogenase in complex with NAD(p) from sinorhizobium meliloti 1021
40% identity, 98% coverage: 4:263/266 of query aligns to 2:252/254 of 3toxA
- active site: G16 (= G23), S142 (= S148), V153 (≠ Q159), Y156 (= Y162), K160 (= K166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (≠ G16), S15 (≠ C17), G16 (= G23), I17 (≠ N24), A36 (≠ D43), R37 (≠ K44), N38 (= N45), V63 (= V70), N89 (= N96), A90 (≠ V97), G91 (= G98), T140 (= T146), S142 (= S148), Y156 (= Y162), K160 (= K166), P186 (= P192), G188 (≠ Q194), T189 (≠ M195), T191 (= T197)
3op4A Crystal structure of putative 3-ketoacyl-(acyl-carrier-protein) reductase from vibrio cholerae o1 biovar eltor str. N16961 in complex with NADP+ (see paper)
39% identity, 97% coverage: 5:261/266 of query aligns to 6:244/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G14), S17 (≠ G16), R18 (≠ W22), I20 (≠ N24), T40 (≠ K44), N62 (≠ D69), V63 (= V70), N89 (= N96), A90 (≠ V97), I92 (≠ G99), V139 (≠ T146), S141 (= S148), Y154 (= Y162), K158 (= K166), P184 (= P192), G185 (= G193), I187 (≠ M195), T189 (= T197), M191 (= M199)
Query Sequence
>RR42_RS23420 FitnessBrowser__Cup4G11:RR42_RS23420
MAGRLEGKVVIVTGAGCVGPGWGNGRAVAVRFAEEGAKVFAVDKNQDPMVETLDRLAAVG
GEFASHLCDVTDSAAVGAMVEACVERFGRVDILVNNVGGSAKGGPVQLSEEDWDRQLNFN
LKSVFLTCKHVLPHMEKQGSGAIVNTASTSGIRWTGSAQVGYASAKAAIIQFSRVVAVEY
AKKNVRVNTVVPGQMHTPMVEARLAGQRAGGDVDTLLAQRQARIPLGFMGDGRDTANAAL
FLASDEARFVTGTEIVVDGGMSVRCD
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