SitesBLAST
Comparing Dsui_2312 FitnessBrowser__PS:Dsui_2312 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)
2ztlA Closed conformation of d-3-hydroxybutyrate dehydrogenase complexed with NAD+ and l-3-hydroxybutyrate (see paper)
55% identity, 100% coverage: 1:260/260 of query aligns to 1:260/260 of 2ztlA
- active site: G15 (= G15), N114 (= N114), S142 (= S142), Y155 (= Y155), K159 (= K159), L200 (≠ Q200)
- binding (3s)-3-hydroxybutanoic acid: Q94 (= Q94), S142 (= S142), H144 (= H144), K152 (= K152), Y155 (= Y155), Q196 (= Q196)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), G15 (= G15), I16 (= I16), F36 (≠ S36), L64 (= L64), N90 (= N90), A91 (= A91), G92 (= G92), L113 (≠ I113), Y155 (= Y155), K159 (= K159), P185 (= P185), W187 (≠ Y187), V188 (= V188), T190 (= T190), V193 (= V193)
1wmbA Crystal structure of NAD dependent d-3-hydroxybutylate dehydrogenase (see paper)
55% identity, 100% coverage: 1:260/260 of query aligns to 1:260/260 of 1wmbA
2q2qD Structure of d-3-hydroxybutyrate dehydrogenase from pseudomonas putida (see paper)
55% identity, 100% coverage: 2:260/260 of query aligns to 2:255/255 of 2q2qD
- active site: G15 (= G15), S138 (= S142), Y151 (= Y155), K155 (= K159), R196 (≠ Q200)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), T13 (= T13), S14 (= S14), G15 (= G15), I16 (= I16), F36 (≠ S36), D59 (= D63), L60 (= L64), N86 (= N90), G88 (= G92), L109 (≠ I113), I136 (= I140), S138 (= S142), Y151 (= Y155), K155 (= K159), P181 (= P185), G182 (= G186), W183 (≠ Y187), V184 (= V188), T186 (= T190), L188 (= L192), V189 (= V193)
5b4tA Crystal structure of d-3-hydroxybutyrate dehydrogenase from alcaligenes faecalis complexed with NAD+ and a substrate d-3- hydroxybutyrate (see paper)
53% identity, 100% coverage: 1:260/260 of query aligns to 1:260/260 of 5b4tA
- active site: G15 (= G15), N114 (= N114), S142 (= S142), Y155 (= Y155), K159 (= K159), I200 (≠ Q200)
- binding (3R)-3-hydroxybutanoic acid: Q94 (= Q94), S142 (= S142), H144 (= H144), K152 (= K152), Y155 (= Y155), W187 (≠ Y187), Q196 (= Q196)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), T13 (= T13), G15 (= G15), I16 (= I16), F36 (≠ S36), D63 (= D63), L64 (= L64), N90 (= N90), G92 (= G92), L113 (≠ I113), I140 (= I140), Y155 (= Y155), K159 (= K159), P185 (= P185), G186 (= G186), W187 (≠ Y187), V188 (= V188), T190 (= T190), L192 (= L192), V193 (= V193)
3w8dA Crystal structure of d-3-hydroxybutyrate dehydrogenase from alcaligenes faecalis complexed with NAD+ and an inhibitor methylmalonate
53% identity, 100% coverage: 1:260/260 of query aligns to 1:260/260 of 3w8dA
- active site: G15 (= G15), N114 (= N114), S142 (= S142), Y155 (= Y155), K159 (= K159), I200 (≠ Q200)
- binding methylmalonic acid: Q94 (= Q94), S142 (= S142), H144 (= H144), K152 (= K152), Y155 (= Y155), W187 (≠ Y187), Q196 (= Q196), W257 (= W257)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), T13 (= T13), S14 (= S14), G15 (= G15), I16 (= I16), F36 (≠ S36), A62 (= A62), D63 (= D63), L64 (= L64), N90 (= N90), A91 (= A91), G92 (= G92), L113 (≠ I113), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), G186 (= G186), W187 (≠ Y187), V188 (= V188), T190 (= T190), L192 (= L192), V193 (= V193)
3vdrA Crystal structure of d-3-hydroxybutyrate dehydrogenase, prepared in the presence of the substrate d-3-hydroxybutyrate and NAD(+) (see paper)
53% identity, 100% coverage: 1:260/260 of query aligns to 1:260/260 of 3vdrA
- active site: G15 (= G15), N114 (= N114), S142 (= S142), Y155 (= Y155), K159 (= K159), I200 (≠ Q200)
- binding (3R)-3-hydroxybutanoic acid: Q94 (= Q94), H144 (= H144), K152 (= K152), Y155 (= Y155), W187 (≠ Y187), Q196 (= Q196), W257 (= W257)
- binding acetoacetic acid: Q94 (= Q94), H144 (= H144), K152 (= K152), Y155 (= Y155), W187 (≠ Y187), Q196 (= Q196), W257 (= W257)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), T13 (= T13), I16 (= I16), F36 (≠ S36), D63 (= D63), L64 (= L64), N90 (= N90), A91 (= A91), G92 (= G92), L113 (≠ I113), K159 (= K159), G186 (= G186), V188 (= V188), T190 (= T190), L192 (= L192), V193 (= V193)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G11 (= G11), T13 (= T13), I16 (= I16), F36 (≠ S36), D63 (= D63), L64 (= L64), N90 (= N90), A91 (= A91), G92 (= G92), L113 (≠ I113), S142 (= S142), Y155 (= Y155), K159 (= K159), G186 (= G186), V188 (= V188), T190 (= T190), L192 (= L192), V193 (= V193)
3vdqA Crystal structure of alcaligenes faecalis d-3-hydroxybutyrate dehydrogenase in complex with NAD(+) and acetate (see paper)
53% identity, 100% coverage: 1:260/260 of query aligns to 1:260/260 of 3vdqA
- active site: G15 (= G15), N114 (= N114), S142 (= S142), Y155 (= Y155), K159 (= K159), I200 (≠ Q200)
- binding acetate ion: Q94 (= Q94), H144 (= H144), K152 (= K152), W187 (≠ Y187), L192 (= L192), Q196 (= Q196)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), S14 (= S14), I16 (= I16), F36 (≠ S36), D63 (= D63), L64 (= L64), N90 (= N90), A91 (= A91), G92 (= G92), L113 (≠ I113), I140 (= I140), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), G186 (= G186), W187 (≠ Y187), V188 (= V188), T190 (= T190), L192 (= L192), V193 (= V193)
5yssB Crystal structure of aminocaproic acid cyclase in complex with NAD (+) (see paper)
51% identity, 100% coverage: 2:260/260 of query aligns to 2:255/255 of 5yssB
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), T13 (= T13), S14 (= S14), G15 (= G15), I16 (= I16), G35 (= G35), F36 (≠ S36), L60 (= L64), N86 (= N90), G88 (= G92), I89 (= I93), A137 (= A141), Y151 (= Y155), K155 (= K159), P181 (= P185), G182 (= G186), V184 (= V188), T186 (= T190)
1x1tA Crystal structure of d-3-hydroxybutyrate dehydrogenase from pseudomonas fragi complexed with NAD+ (see paper)
52% identity, 100% coverage: 1:260/260 of query aligns to 1:236/236 of 1x1tA
- active site: G15 (= G15), N114 (= N114), S142 (= S142), Y155 (= Y155), K159 (= K159)
- binding cacodylate ion: S142 (= S142), H144 (= H144), Y155 (= Y155), W187 (≠ Y187), W233 (= W257)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), T13 (= T13), S14 (= S14), G15 (= G15), I16 (= I16), G35 (= G35), F36 (≠ S36), D63 (= D63), L64 (= L64), N90 (= N90), G92 (= G92), L113 (≠ I113), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), W187 (≠ Y187), V188 (= V188), T190 (= T190)
6zzsD Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and 3-oxovalerate (see paper)
43% identity, 100% coverage: 1:260/260 of query aligns to 4:261/261 of 6zzsD
- active site: G18 (= G15), S143 (= S142), Y156 (= Y155)
- binding nicotinamide-adenine-dinucleotide: G14 (= G11), S17 (= S14), I19 (= I16), D38 (vs. gap), M39 (≠ L33), D64 (= D63), V65 (≠ L64), N91 (= N90), A92 (= A91), G93 (= G92), M141 (≠ I140), A142 (= A141), S143 (= S142), Y156 (= Y155), K160 (= K159), P186 (= P185), G187 (= G186), V189 (= V188), T191 (= T190), L193 (= L192)
- binding 3-oxidanylidenepentanoic acid: Q95 (= Q94), S143 (= S142), N145 (≠ H144), K153 (= K152), Y156 (= Y155), Q197 (= Q196)
6zzqA Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and acetoacetate (see paper)
43% identity, 100% coverage: 1:260/260 of query aligns to 3:260/260 of 6zzqA
- active site: G17 (= G15), S142 (= S142), Y155 (= Y155)
- binding acetoacetic acid: Q94 (= Q94), S142 (= S142), K152 (= K152), Y155 (= Y155), Q196 (= Q196)
- binding nicotinamide-adenine-dinucleotide: G13 (= G11), S16 (= S14), G17 (= G15), I18 (= I16), D37 (vs. gap), M38 (≠ L33), D63 (= D63), V64 (≠ L64), N90 (= N90), A91 (= A91), G92 (= G92), M140 (≠ I140), A141 (= A141), S142 (= S142), Y155 (= Y155), K159 (= K159), Y187 (= Y187), V188 (= V188), T190 (= T190)
P16544 Putative ketoacyl reductase; EC 1.3.1.- from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) (see 2 papers)
41% identity, 97% coverage: 5:256/260 of query aligns to 7:257/261 of P16544
- 11:39 (vs. 9:41, 45% identical) binding
- D63 (= D63) binding
- K161 (= K159) binding
2rh4B Actinorhodin ketoreductase, actkr, with NADPH and inhibitor emodin (see paper)
41% identity, 97% coverage: 5:256/260 of query aligns to 14:264/268 of 2rh4B
- active site: G24 (= G15), N121 (= N114), S151 (= S142), Y164 (= Y155), K168 (= K159), Y209 (≠ Q200)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G11), T22 (= T13), S23 (= S14), I25 (= I16), A44 (= A39), R45 (≠ A40), G46 (≠ E41), C69 (≠ A62), D70 (= D63), V71 (≠ L64), N97 (= N90), S151 (= S142), Y164 (= Y155), K168 (= K159), G195 (= G186), V197 (= V188), T199 (= T190), M201 (≠ L192)
2rh4A Actinorhodin ketoreductase, actkr, with NADPH and inhibitor emodin (see paper)
41% identity, 97% coverage: 5:256/260 of query aligns to 3:253/257 of 2rh4A
- active site: G13 (= G15), N110 (= N114), S140 (= S142), Y153 (= Y155), K157 (= K159), Y198 (≠ Q200)
- binding 3-methyl-1,6,8-trihydroxyanthraquinone: T141 (≠ A143), Q145 (≠ V147), V147 (≠ S149), Y153 (= Y155), F185 (≠ Y187)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G11), T11 (= T13), S12 (= S14), G13 (= G15), I14 (= I16), A33 (= A39), R34 (≠ A40), G35 (≠ E41), C58 (≠ A62), D59 (= D63), V60 (≠ L64), N86 (= N90), G88 (= G92), S140 (= S142), Y153 (= Y155), K157 (= K159), P183 (= P185), G184 (= G186), V186 (= V188), T188 (= T190), M190 (≠ L192)
Sites not aligning to the query:
1w4zA Structure of actinorhodin polyketide (actiii) reductase (see paper)
41% identity, 97% coverage: 5:256/260 of query aligns to 5:255/259 of 1w4zA
- active site: G15 (= G15), N112 (= N114), S142 (= S142), Y155 (= Y155), K159 (= K159), Y200 (≠ Q200)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G11), T13 (= T13), S14 (= S14), G15 (= G15), I16 (= I16), R36 (≠ A40), G37 (≠ E41), D61 (= D63), V62 (≠ L64), N88 (= N90), G90 (= G92), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), G186 (= G186), V188 (= V188), T190 (= T190)
1xr3A Actinorhodin polyketide ketoreductase with NADP and the inhibitor isoniazid bound (see paper)
41% identity, 97% coverage: 5:256/260 of query aligns to 2:252/256 of 1xr3A
- active site: G12 (= G15), N109 (= N114), S139 (= S142), Y152 (= Y155), K156 (= K159), Y197 (≠ Q200)
- binding 4-(diazenylcarbonyl)pyridine: T140 (≠ A143), G141 (≠ H144), V146 (≠ S149)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G11), T10 (= T13), S11 (= S14), G12 (= G15), I13 (= I16), A32 (= A39), R33 (≠ A40), G34 (≠ E41), C57 (≠ A62), D58 (= D63), V59 (≠ L64), N85 (= N90), A86 (= A91), G87 (= G92), S139 (= S142), Y152 (= Y155), K156 (= K159), G183 (= G186), V185 (= V188), T187 (= T190), P188 (= P191)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
41% identity, 98% coverage: 5:259/260 of query aligns to 3:249/250 of 2cfcA
- active site: G13 (= G15), S142 (= S142), Y155 (= Y155), K159 (= K159)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ S149), R152 (≠ K152), Y155 (= Y155), W195 (≠ K195), R196 (≠ Q196)
- binding nicotinamide-adenine-dinucleotide: G9 (= G11), S12 (= S14), G13 (= G15), N14 (≠ I16), D33 (≠ N34), L34 (≠ G35), A59 (= A62), D60 (= D63), V61 (≠ L64), N87 (= N90), A88 (= A91), G89 (= G92), I140 (= I140), P185 (= P185), G186 (= G186), M187 (≠ Y187), I188 (≠ V188), T190 (= T190), P191 (= P191), M192 (≠ L192), T193 (≠ V193)
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)
41% identity, 98% coverage: 5:259/260 of query aligns to 3:249/250 of Q56840
- SGN 12:14 (≠ SGI 14:16) binding
- D33 (≠ N34) binding
- DV 60:61 (≠ DL 63:64) binding
- N87 (= N90) binding
- S142 (= S142) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ K152) 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 (= Y155) mutation Y->E,F: Loss of activity.
- K159 (= K159) mutation to A: Loss of activity.
- R179 (≠ T179) mutation to A: Loss of activity.
- IETPM 188:192 (≠ VRTPL 188:192) binding
- WR 195:196 (≠ KQ 195:196) binding
- R196 (≠ Q196) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (= R213) mutation to A: Slight decrease in catalytic efficiency.
- R209 (≠ A219) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3sjuA Hedamycin polyketide ketoreductase bound to NADPH (see paper)
41% identity, 97% coverage: 5:256/260 of query aligns to 1:251/255 of 3sjuA
- active site: G11 (= G15), S138 (= S142), Y151 (= Y155), K155 (= K159), Y196 (≠ Q200)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G7 (= G11), S10 (= S14), A31 (vs. gap), R32 (≠ L33), D33 (≠ N34), C56 (≠ A62), D57 (= D63), V58 (≠ L64), S84 (≠ N90), A85 (= A91), G86 (= G92), I136 (= I140), Y151 (= Y155), K155 (= K159), P181 (= P185), G182 (= G186), Y183 (= Y187), V184 (= V188), T186 (= T190), M188 (≠ L192)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
36% identity, 100% coverage: 1:259/260 of query aligns to 2:247/248 of 6ixmC
- active site: G16 (= G15), S142 (= S142), Y155 (= Y155), K159 (= K159)
- binding nicotinamide-adenine-dinucleotide: G12 (= G11), S15 (= S14), G16 (= G15), I17 (= I16), D36 (vs. gap), I37 (≠ L33), A61 (= A62), D62 (= D63), T63 (≠ L64), N89 (= N90), A90 (= A91), M140 (≠ I140), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), A186 (≠ G186), Y187 (= Y187), I188 (≠ V188), L192 (= L192)
Query Sequence
>Dsui_2312 FitnessBrowser__PS:Dsui_2312
MLSGKIALVTGSTSGIGLAVARALARNGAAVMLNGSRPAAEAEGLRAAMAAEFGVKVAYT
SADLADAASVRALAAAAEKQLGVVDILVNNAGIQHVAAVDEFPEEKWDQLIAINLSSVFH
ATKAVLPGMKARNWGRIVNIASAHGLVASPFKAPYTASKHAVVGFSKAVALEVAETGITC
NAVCPGYVRTPLVEKQVAAQAKVHNLPEDQVIRDVILAAQPNKRFLEADDLAEFVLFLCS
PAGAGMTGAALPMDGAWTAR
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