SitesBLAST
Comparing SM_b21111 FitnessBrowser__Smeli:SM_b21111 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)
55% identity, 98% coverage: 5:244/244 of query aligns to 4:245/245 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)
54% identity, 98% coverage: 5:244/244 of query aligns to 4:245/245 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)
55% identity, 98% coverage: 5:244/244 of query aligns to 4:245/245 of Q9BUT1
2ag5A Crystal structure of human dhrs6 (see paper)
55% identity, 98% coverage: 5:244/244 of query aligns to 4:245/246 of 2ag5A
- active site: S133 (= S134), Y147 (= Y148), K151 (= K152), R192 (≠ Q193)
- binding nicotinamide-adenine-dinucleotide: Q16 (= Q17), G17 (= G18), I18 (= I19), D37 (= D38), I38 (= I39), D58 (= D59), V59 (= V60), V81 (≠ C82), G83 (= G84), L104 (= L105), Y147 (= Y148), K151 (= K152), P177 (= P178), V180 (= V181), T182 (≠ S183), S184 (= S185)
- binding sulfate ion: R144 (= R145), R188 (= R189), F202 (= F203), R205 (= R206)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
40% identity, 97% coverage: 8:243/244 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 (≠ V142), R152 (= R145), Y155 (= Y148), W195 (≠ S188), 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 (≠ C82), 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)
40% identity, 97% coverage: 8:243/244 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 (≠ C82) 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 (≠ SR 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 (= R200) mutation to A: Slight decrease in catalytic efficiency.
- R209 (= R206) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
38% identity, 98% coverage: 5:243/244 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 (≠ C82), A90 (= A83), M140 (= M132), S142 (= S134), Y155 (= Y148), K159 (= K152), P185 (= P178), A186 (≠ G179), Y187 (≠ T180), I188 (≠ V181), L192 (≠ S185)
5yssB Crystal structure of aminocaproic acid cyclase in complex with NAD (+) (see paper)
35% identity, 98% coverage: 4:242/244 of query aligns to 1:252/255 of 5yssB
- binding nicotinamide-adenine-dinucleotide: G11 (≠ A14), T13 (≠ A16), S14 (≠ Q17), G15 (= G18), I16 (= I19), G35 (vs. gap), F36 (vs. gap), L60 (≠ V60), N86 (≠ C82), G88 (= G84), I89 (≠ F85), A137 (= A133), Y151 (= Y148), K155 (= K152), P181 (= P178), G182 (= G179), V184 (= V181), T186 (≠ S183)
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)
35% identity, 98% coverage: 4:241/244 of query aligns to 5:243/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (≠ A14), S17 (≠ A16), R18 (≠ Q17), I20 (= I19), T40 (vs. gap), N62 (≠ D59), V63 (= V60), N89 (≠ C82), A90 (= A83), I92 (≠ F85), V139 (≠ M132), S141 (= S134), Y154 (= Y148), K158 (= K152), P184 (= P178), G185 (= G179), I187 (≠ V181), T189 (≠ S183), M191 (≠ R189)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
34% identity, 98% coverage: 4:241/244 of query aligns to 5:239/243 of 4i08A
- active site: G19 (= G18), N113 (= N106), S141 (= S134), Q151 (≠ R145), Y154 (= Y148), K158 (= K152)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (≠ A14), S17 (≠ A16), R18 (≠ Q17), I20 (= I19), T40 (vs. gap), N62 (≠ D59), V63 (= V60), N89 (≠ C82), A90 (= A83), G140 (≠ A133), S141 (= S134), Y154 (= Y148), K158 (= K152), P184 (= P178), G185 (= G179), T189 (≠ S183)
6qheA Alcohol dehydrogenase from arthrobacter sp. Ts-15 in complex with NAD+
33% identity, 99% coverage: 4:244/244 of query aligns to 4:256/261 of 6qheA
- binding nicotinamide-adenine-dinucleotide: G14 (≠ A14), M17 (≠ Q17), G18 (= G18), M19 (≠ I19), D38 (= D38), R39 (vs. gap), D63 (= D59), I64 (≠ V60), A90 (≠ C82), A91 (= A83), S142 (= S134), Y156 (= Y148), K160 (= K152), P186 (= P178), G187 (= G179), M189 (≠ V181), T191 (≠ S183), P192 (= P184), M193 (≠ S185)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
33% identity, 100% coverage: 1:243/244 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 (≠ L58), I63 (≠ V60), N89 (≠ C82), G91 (= G84), T139 (≠ M132), S141 (= S134), Y154 (= Y148), K158 (= K152), P184 (= P178), G185 (= G179), I186 (≠ T180), I187 (≠ V181)
2q2qD Structure of d-3-hydroxybutyrate dehydrogenase from pseudomonas putida (see paper)
35% identity, 98% coverage: 5:242/244 of query aligns to 2:252/255 of 2q2qD
- active site: G15 (= G18), S138 (= S134), Y151 (= Y148), K155 (= K152), R196 (= R189)
- binding nicotinamide-adenine-dinucleotide: G11 (≠ A14), T13 (≠ A16), S14 (≠ Q17), G15 (= G18), I16 (= I19), F36 (≠ I39), D59 (= D59), L60 (≠ V60), N86 (≠ C82), G88 (= G84), L109 (= L105), I136 (≠ M132), S138 (= S134), Y151 (= Y148), K155 (= K152), P181 (= P178), G182 (= G179), W183 (≠ T180), V184 (= V181), T186 (≠ S183), L188 (vs. gap), V189 (vs. gap)
2dtxA Structure of thermoplasma acidophilum aldohexose dehydrogenase (aldt) in complex with d-mannose (see paper)
34% identity, 99% coverage: 3:244/244 of query aligns to 3:247/255 of 2dtxA
2dteA Structure of thermoplasma acidophilum aldohexose dehydrogenase (aldt) in complex with nadh (see paper)
34% identity, 99% coverage: 3:244/244 of query aligns to 3:247/255 of 2dteA
- active site: G18 (= G18), S132 (= S134), Y145 (= Y148), S148 (≠ T151), K149 (= K152)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (≠ A14), S16 (≠ A16), M17 (≠ Q17), G18 (= G18), I19 (= I19), S38 (≠ D38), I39 (= I39), C52 (≠ L58), D53 (= D59), V54 (= V60), N80 (≠ C82), 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)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
34% identity, 98% coverage: 4:241/244 of query aligns to 1:239/243 of 1q7bA
- active site: G15 (= G18), E101 (≠ D98), S137 (= S134), Q147 (≠ R145), Y150 (= Y148), K154 (= K152)
- binding calcium ion: E232 (≠ Q234), T233 (≠ A235)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (≠ A14), S13 (≠ A16), R14 (≠ Q17), T36 (vs. gap), N58 (≠ D59), V59 (= V60), N85 (≠ C82), A86 (= A83), G87 (= G84), I88 (≠ F85), S137 (= S134), Y150 (= Y148), K154 (= K152), P180 (= P178), G181 (= G179), I183 (≠ V181)
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)
34% identity, 98% coverage: 4:241/244 of query aligns to 2:240/244 of P0AEK2
- GASR 12:15 (≠ AAAQ 14:17) binding
- T37 (vs. gap) binding
- NV 59:60 (≠ DV 59:60) binding
- N86 (≠ C82) binding
- Y151 (= Y148) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YGVTK 148:152) binding
- A154 (≠ T151) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K152) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ V181) binding
- E233 (≠ Q234) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
32% identity, 98% coverage: 5:244/244 of query aligns to 2:244/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (≠ A14), M16 (≠ I19), D35 (= D38), I36 (= I39), I62 (≠ V60), N88 (≠ C82), G90 (= G84), I138 (≠ M132), S140 (= S134), Y152 (= Y148), K156 (= K152), I185 (≠ V181)
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)
32% identity, 98% coverage: 5:244/244 of query aligns to 3:245/248 of Q9KJF1
- S15 (≠ Q17) binding
- D36 (= D38) binding
- D62 (= D59) binding
- I63 (≠ V60) binding
- N89 (≠ C82) binding
- Y153 (= Y148) binding
- K157 (= K152) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5b4tA Crystal structure of d-3-hydroxybutyrate dehydrogenase from alcaligenes faecalis complexed with NAD+ and a substrate d-3- hydroxybutyrate (see paper)
34% identity, 98% coverage: 5:243/244 of query aligns to 2:258/260 of 5b4tA
- active site: G15 (= G18), N114 (= N106), S142 (= S134), Y155 (= Y148), K159 (= K152), I200 (≠ Q193)
- binding (3R)-3-hydroxybutanoic acid: Q94 (≠ V86), S142 (= S134), H144 (≠ A136), K152 (≠ R145), Y155 (= Y148), W187 (≠ T180), Q196 (≠ R189)
- binding nicotinamide-adenine-dinucleotide: G11 (≠ A14), T13 (≠ A16), G15 (= G18), I16 (= I19), F36 (vs. gap), D63 (= D59), L64 (≠ V60), N90 (≠ C82), G92 (= G84), L113 (= L105), I140 (≠ M132), Y155 (= Y148), K159 (= K152), P185 (= P178), G186 (= G179), W187 (≠ T180), V188 (= V181), T190 (≠ S183), L192 (≠ S185), V193 (≠ L186)
Query Sequence
>SM_b21111 FitnessBrowser__Smeli:SM_b21111
MTANLAGKVVLVTAAAQGIGRATALAFAKAGAKVHATDINADAVGSLEGEAGISTHRLDV
LDTAAVEALVAEIGAVDVLFNCAGFVHAGSVLTMKDEDLDFAFDLNVKSMIRTIRAVLPG
MIARKDGSIVNMASVASSIKGVPNRFAYGVTKAAVIGLTKAVAADYVGDGIRCNAICPGT
VESPSLESRMRAQGDYETARAAFISRQPMGRLGTPEEIADLAVYLAGATYTSGQAYAIDG
GWTI
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