SitesBLAST
Comparing RR42_RS34980 FitnessBrowser__Cup4G11:RR42_RS34980 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
60% identity, 98% coverage: 4:250/251 of query aligns to 3:244/245 of D4A1J4
- Y147 (= Y148) mutation to F: Loss of function.
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)
58% identity, 98% coverage: 4:250/251 of query aligns to 3:244/245 of Q8JZV9
- Y147 (= Y148) active site, Proton acceptor; mutation to F: Loss of function.
Q9BUT1 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 Homo sapiens (Human) (see 4 papers)
57% identity, 98% coverage: 4:250/251 of query aligns to 3:244/245 of Q9BUT1
2ag5A Crystal structure of human dhrs6 (see paper)
57% identity, 98% coverage: 4:250/251 of query aligns to 3:244/246 of 2ag5A
- active site: S133 (= S134), Y147 (= Y148), K151 (= K152), R192 (= R195)
- binding nicotinamide-adenine-dinucleotide: Q16 (= Q17), G17 (= G18), I18 (= I19), D37 (= D38), I38 (= I39), D58 (= D59), V59 (= V60), V81 (≠ G82), G83 (= G84), L104 (= L105), Y147 (= Y148), K151 (= K152), P177 (= P178), V180 (= V181), T182 (≠ S183), S184 (= S185)
- binding sulfate ion: R144 (= R145), R188 (= R189), F202 (= F208), R205 (= R211)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
38% identity, 97% coverage: 8:250/251 of query aligns to 3:248/250 of 2cfcA
- active site: G13 (= G18), S142 (= S134), Y155 (= Y148), K159 (= K152)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ A142), R152 (= R145), Y155 (= Y148), W195 (≠ Q188), R196 (= R189)
- binding nicotinamide-adenine-dinucleotide: G9 (≠ A14), S12 (≠ Q17), G13 (= G18), N14 (≠ I19), D33 (= D38), L34 (≠ I39), A59 (≠ L58), D60 (= D59), V61 (= V60), N87 (≠ G82), A88 (= A83), G89 (= G84), I140 (≠ M132), P185 (= P178), G186 (= G179), M187 (≠ T180), I188 (≠ V181), T190 (≠ S183), P191 (= P184), M192 (≠ S185), T193 (≠ L186)
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)
38% identity, 97% coverage: 8:250/251 of query aligns to 3:248/250 of Q56840
- SGN 12:14 (≠ QGI 17:19) binding
- D33 (= D38) binding
- DV 60:61 (= DV 59:60) binding
- N87 (≠ G82) binding
- S142 (= S134) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (= R145) 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 (= Y148) mutation Y->E,F: Loss of activity.
- K159 (= K152) mutation to A: Loss of activity.
- R179 (= R172) mutation to A: Loss of activity.
- IETPM 188:192 (≠ VESPS 181:185) binding
- WR 195:196 (≠ QR 188:189) binding
- R196 (= R189) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (≠ E205) mutation to A: Slight decrease in catalytic efficiency.
- R209 (= R211) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
34% identity, 100% coverage: 1:250/251 of query aligns to 1:253/255 of 5itvA
- active site: G18 (= G18), S141 (= S134), Y154 (= Y148), K158 (= K152)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (≠ A14), S17 (≠ Q17), G18 (= G18), I19 (= I19), D38 (= D38), I39 (= I39), T61 (vs. gap), I63 (≠ V60), N89 (≠ G82), G91 (= G84), T139 (≠ M132), S141 (= S134), Y154 (= Y148), K158 (= K152), P184 (= P178), G185 (= G179), I186 (≠ T180), I187 (≠ V181)
6zzsD Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and 3-oxovalerate (see paper)
36% identity, 100% coverage: 1:250/251 of query aligns to 1:259/261 of 6zzsD
- active site: G18 (= G18), S143 (= S134), Y156 (= Y148)
- binding nicotinamide-adenine-dinucleotide: G14 (≠ A14), S17 (≠ Q17), I19 (= I19), D38 (= D38), M39 (≠ I39), D64 (= D59), V65 (= V60), N91 (≠ G82), A92 (= A83), G93 (= G84), M141 (= M132), A142 (= A133), S143 (= S134), Y156 (= Y148), K160 (= K152), P186 (= P178), G187 (= G179), V189 (= V181), T191 (≠ S183), L193 (≠ S185)
- binding 3-oxidanylidenepentanoic acid: Q95 (≠ V86), S143 (= S134), N145 (≠ A136), K153 (≠ R145), Y156 (= Y148), Q197 (≠ R189)
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)
39% identity, 100% coverage: 1:250/251 of query aligns to 1:253/255 of A7IQH5
- I19 (= I19) binding
- D38 (= D38) binding
- DV 64:65 (= DV 59:60) binding
- N91 (≠ G82) binding
- S143 (= S134) binding ; mutation to A: Retains very weak activity.
- Y156 (= Y148) binding ; mutation to A: Retains some activity but with more than 2200-fold decrease in catalytic efficiency.; mutation to F: Loss of activity.
- K160 (= K152) binding ; mutation to A: Loss of activity.
- T188 (= T180) binding
- VTSTG 189:193 (≠ VESPS 181:185) binding
- R211 (≠ F208) 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 (≠ R211) 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 (≠ Q212) binding
7djsD Crystal structure of isopiperitenol dehydrogenase from pseudomonas aeruginosa complexed with NAD
41% identity, 98% coverage: 3:248/251 of query aligns to 1:247/251 of 7djsD
- binding nicotinamide-adenine-dinucleotide: G12 (≠ A14), G16 (= G18), I17 (= I19), D36 (= D38), L37 (≠ I39), C61 (≠ L58), D62 (= D59), V63 (= V60), N89 (≠ G82), A90 (= A83), T140 (≠ M132), S142 (= S134), Y155 (= Y148), K159 (= K152), A186 (≠ G179), V187 (≠ T180)
6zzqA Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and acetoacetate (see paper)
36% identity, 99% coverage: 2:250/251 of query aligns to 1:258/260 of 6zzqA
- active site: G17 (= G18), S142 (= S134), Y155 (= Y148)
- binding acetoacetic acid: Q94 (≠ V86), S142 (= S134), K152 (≠ R145), Y155 (= Y148), Q196 (≠ R189)
- binding nicotinamide-adenine-dinucleotide: G13 (≠ A14), S16 (≠ Q17), G17 (= G18), I18 (= I19), D37 (= D38), M38 (≠ I39), D63 (= D59), V64 (= V60), N90 (≠ G82), A91 (= A83), G92 (= G84), M140 (= M132), A141 (= A133), S142 (= S134), Y155 (= Y148), K159 (= K152), Y187 (≠ T180), V188 (= V181), T190 (≠ S183)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
35% identity, 100% coverage: 1:251/251 of query aligns to 4:252/258 of 4wecA
- active site: G21 (= G18), S143 (= S134), Q154 (≠ R145), Y157 (= Y148), K161 (= K152)
- binding nicotinamide-adenine-dinucleotide: G17 (≠ A14), A19 (≠ G16), S20 (≠ Q17), G21 (= G18), I22 (= I19), D41 (= D38), I42 (= I39), V61 (≠ L58), D62 (= D59), V63 (= V60), N89 (≠ G82), T141 (≠ M132), Y157 (= Y148), K161 (= K152), P187 (= P178), P189 (≠ T180), V190 (= V181)
4gh5A Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) (see paper)
39% identity, 90% coverage: 25:250/251 of query aligns to 23:246/248 of 4gh5A
- active site: N113 (= N106), S141 (= S134), Y154 (= Y148), K158 (= K152)
- binding nicotinamide-adenine-dinucleotide: D36 (= D38), L37 (≠ I39), A61 (≠ L58), D62 (= D59), V63 (= V60), N89 (≠ G82), A90 (= A83), V112 (≠ L105), F139 (≠ M132), S141 (= S134), Y154 (= Y148), K158 (= K152), P184 (= P178), V187 (= V181), T190 (≠ P184), G191 (≠ S185), M192 (≠ L186)
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)
39% identity, 90% coverage: 25:250/251 of query aligns to 23:251/253 of 4ituA
- active site: N113 (= N106), S141 (= S134), Y154 (= Y148), K158 (= K152)
- binding 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonic acid: S141 (= S134), Y154 (= Y148), T186 (= T180), R209 (≠ F208), Y213 (≠ Q212)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D36 (= D38), L37 (≠ I39), D62 (= D59), V63 (= V60), N89 (≠ G82), V112 (≠ L105), F139 (≠ M132), S141 (= S134), Y154 (= Y148), K158 (= K152), P184 (= P178), T186 (= T180), V187 (= V181), T190 (≠ P184), M192 (≠ L186)
Sites not aligning to the query:
6pejA Structure of sorbitol dehydrogenase from sinorhizobium meliloti 1021 bound to sorbitol
38% identity, 98% coverage: 3:249/251 of query aligns to 2:255/257 of 6pejA
2dtxA Structure of thermoplasma acidophilum aldohexose dehydrogenase (aldt) in complex with d-mannose (see paper)
34% identity, 98% coverage: 5:250/251 of query aligns to 5:246/255 of 2dtxA
2dteA Structure of thermoplasma acidophilum aldohexose dehydrogenase (aldt) in complex with nadh (see paper)
34% identity, 98% coverage: 5:250/251 of query aligns to 5:246/255 of 2dteA
- active site: G18 (= G18), S132 (= S134), Y145 (= Y148), S148 (≠ T151), K149 (= K152)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (≠ A14), S16 (≠ G16), M17 (≠ Q17), G18 (= G18), I19 (= I19), S38 (≠ D38), I39 (= I39), C52 (≠ L58), D53 (= D59), V54 (= V60), N80 (≠ G82), A81 (= A83), I130 (≠ M132), S132 (= S134), Y145 (= Y148), K149 (= K152), P174 (= P178), A175 (≠ G179), T176 (= T180), I177 (≠ V181), T179 (≠ S183), P180 (= P184), L181 (≠ S185), V182 (≠ L186)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
34% identity, 98% coverage: 5:250/251 of query aligns to 3:246/248 of 6ixmC
- active site: G16 (= G18), S142 (= S134), Y155 (= Y148), K159 (= K152)
- binding nicotinamide-adenine-dinucleotide: G12 (≠ A14), S15 (≠ Q17), G16 (= G18), I17 (= I19), D36 (= D38), I37 (= I39), A61 (≠ L58), D62 (= D59), T63 (≠ V60), N89 (≠ G82), A90 (= A83), M140 (= M132), S142 (= S134), Y155 (= Y148), K159 (= K152), P185 (= P178), A186 (≠ G179), Y187 (≠ T180), I188 (≠ V181), L192 (≠ S185)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
32% identity, 98% coverage: 4:248/251 of query aligns to 4:241/244 of 4nbuB
- active site: G18 (= G18), N111 (= N106), S139 (= S134), Q149 (≠ R145), Y152 (= Y148), K156 (= K152)
- binding acetoacetyl-coenzyme a: D93 (≠ H88), K98 (≠ E93), S139 (= S134), N146 (≠ A142), V147 (≠ P143), Q149 (≠ R145), Y152 (= Y148), F184 (≠ T180), M189 (vs. gap), K200 (≠ Q193)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (≠ A14), N17 (≠ Q17), G18 (= G18), I19 (= I19), D38 (= D38), F39 (≠ I39), V59 (≠ L58), D60 (= D59), V61 (= V60), N87 (≠ G82), A88 (= A83), G89 (= G84), I90 (≠ F85), T137 (≠ M132), S139 (= S134), Y152 (= Y148), K156 (= K152), P182 (= P178), F184 (≠ T180), T185 (≠ V181), T187 (≠ S183), M189 (vs. gap)
6qheA Alcohol dehydrogenase from arthrobacter sp. Ts-15 in complex with NAD+
32% identity, 97% coverage: 8:250/251 of query aligns to 8:255/261 of 6qheA
- binding nicotinamide-adenine-dinucleotide: G14 (≠ A14), M17 (≠ Q17), G18 (= G18), M19 (≠ I19), D38 (= D40), R39 (≠ A41), D63 (= D59), I64 (≠ V60), A90 (≠ G82), A91 (= A83), S142 (= S134), Y156 (= Y148), K160 (= K152), P186 (= P178), G187 (= G179), M189 (≠ V181), T191 (≠ S183), P192 (= P184), M193 (≠ S185)
Query Sequence
>RR42_RS34980 FitnessBrowser__Cup4G11:RR42_RS34980
MTQRLAGKLALVTAAGQGIGRATAEAYLREGARVIAADIDARLLEALAGQPGCTTLRLDV
TDGAAVQAAAKQAGALDILFNGAGFVHHGTILECDEAAFDFSMNLNVRAMYSMMRAFLPA
MVARRRGSIVNMASVAGSIKGAPNRFVYGATKAAVIGMTKSVAADYIGHGIRCNAICPGT
VESPSLRQRIADQARDGGRSLAEVEAAFVARQPMGRIGSAAEIAALAVYLGSDESAFTTG
TAQVIDGGWSN
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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