SitesBLAST
Comparing 3607132 FitnessBrowser__Dino:3607132 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)
5jo9A Structural characterization of the thermostable bradyrhizobium japonicum d-sorbitol dehydrogenase (see paper)
51% identity, 99% coverage: 3:241/241 of query aligns to 1:239/239 of 5jo9A
4nbuB Crystal structure of fabg from bacillus sp (see paper)
34% identity, 94% coverage: 1:226/241 of query aligns to 2:229/244 of 4nbuB
- active site: G18 (= G17), N111 (= N111), S139 (= S139), Q149 (≠ E149), Y152 (= Y152), K156 (= K156)
- binding acetoacetyl-coenzyme a: D93 (≠ G93), K98 (≠ A98), S139 (= S139), N146 (≠ V146), V147 (= V147), Q149 (≠ E149), Y152 (= Y152), F184 (≠ P184), M189 (≠ L189), K200 (≠ Q200)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), N17 (≠ S16), G18 (= G17), I19 (= I18), D38 (= D37), F39 (≠ R38), V59 (≠ T59), D60 (= D60), V61 (≠ L61), N87 (= N87), A88 (= A88), G89 (= G89), I90 (≠ A90), T137 (= T137), S139 (= S139), Y152 (= Y152), K156 (= K156), P182 (= P182), F184 (≠ P184), T185 (≠ V185), T187 (= T187), M189 (≠ L189)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
32% identity, 96% coverage: 4:235/241 of query aligns to 3:241/248 of 6ixmC
- active site: G16 (= G17), S142 (= S139), Y155 (= Y152), K159 (= K156)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S15 (= S16), G16 (= G17), I17 (= I18), D36 (= D37), I37 (≠ R38), A61 (≠ T59), D62 (= D60), T63 (≠ L61), N89 (= N87), A90 (= A88), M140 (≠ T137), S142 (= S139), Y155 (= Y152), K159 (= K156), P185 (= P182), A186 (≠ G183), Y187 (≠ P184), I188 (≠ V185), L192 (= L189)
8cwlA Cryo-em structure of human 15-pgdh in complex with small molecule sw222746 (see paper)
34% identity, 80% coverage: 4:197/241 of query aligns to 2:197/255 of 8cwlA
- binding 1,4-dihydronicotinamide adenine dinucleotide: G11 (= G13), Q14 (≠ S16), G15 (= G17), I16 (= I18), D35 (= D37), W36 (≠ R38), C62 (≠ T59), V64 (≠ L61), N90 (= N87), G92 (= G89), V93 (≠ A98), S137 (= S139), Y150 (= Y152), K154 (= K156), G183 (= G183), V185 (= V185), T187 (= T187), I189 (≠ L189)
- binding 2-methyl-6-[7-(piperidine-1-carbonyl)quinoxalin-2-yl]isoquinolin-1(2H)-one: S137 (= S139), L138 (≠ V140), A139 (= A141), M142 (≠ I144), Q147 (≠ E149), Y150 (= Y152), F184 (≠ P184), I193 (≠ W193)
Sites not aligning to the query:
8cvnA Cryo-em structure of human 15-pgdh in complex with small molecule sw209415 (see paper)
34% identity, 80% coverage: 4:197/241 of query aligns to 3:198/256 of 8cvnA
- binding 1,4-dihydronicotinamide adenine dinucleotide: Q15 (≠ S16), I17 (= I18), D36 (= D37), W37 (≠ R38), V65 (≠ L61), N91 (= N87), G93 (= G89), V94 (≠ A98), S138 (= S139), K155 (= K156), P183 (= P182), V186 (= V185), T188 (= T187)
- binding 2-[butyl(oxidanyl)-$l^{3}-sulfanyl]-4-(2,3-dimethylimidazol-4-yl)-6-(1,3-thiazol-2-yl)thieno[2,3-b]pyridin-3-amine: N95 (≠ G99), S138 (= S139), Q148 (≠ E149), Y151 (= Y152), F185 (≠ P184)
Sites not aligning to the query:
P15428 15-hydroxyprostaglandin dehydrogenase [NAD(+)]; 15-PGDH; Eicosanoid/docosanoid dehydrogenase [NAD(+)]; Prostaglandin dehydrogenase 1; Short chain dehydrogenase/reductase family 36C member 1; EC 1.1.1.141; EC 1.1.1.-; EC 1.1.1.232 from Homo sapiens (Human) (see 5 papers)
34% identity, 80% coverage: 4:197/241 of query aligns to 3:198/266 of P15428
- 12:20 (vs. 13:21, 67% identical) binding
- DW 36:37 (≠ DR 37:38) binding
- CDV 63:65 (≠ TDL 59:61) binding
- N91 (= N87) binding
- A140 (= A141) to P: in COA; inactive; dbSNP:rs121434480
- Q148 (≠ E149) mutation to A: Loss of activity.; mutation Q->E,H,N: Reduced affinity for NAD and prostaglandin E2.
- Y151 (= Y152) mutation to A: Loss of activity.; mutation to F: Loss 15-hydroxyprostaglandin dehydrogenase activity.
- YCASK 151:155 (≠ YTASK 152:156) binding
- K155 (= K156) mutation to Q: Loss 15-hydroxyprostaglandin dehydrogenase activity.
- VNT 186:188 (≠ VVT 185:187) binding
2gdzA Crystal structure of 15-hydroxyprostaglandin dehydrogenase type1, complexed with NAD+ (see paper)
34% identity, 80% coverage: 4:197/241 of query aligns to 4:199/266 of 2gdzA
- active site: G17 (= G17), N108 (= N111), S139 (= S139), Y152 (= Y152), K156 (= K156)
- binding nicotinamide-adenine-dinucleotide: G13 (= G13), Q16 (≠ S16), G17 (= G17), I18 (= I18), D37 (= D37), W38 (≠ R38), C64 (≠ T59), D65 (= D60), V66 (≠ L61), N92 (= N87), G94 (= G89), V95 (≠ A98), I107 (≠ L110), S139 (= S139), Y152 (= Y152), K156 (= K156), P184 (= P182), F186 (≠ P184), V187 (= V185), T189 (= T187), I191 (≠ L189)
A0A1U8QWA2 Glycine betaine reductase ATRR; Nonribosomal peptide synthetase-like protein ATRR; EC 1.2.1.-; EC 1.1.1.- from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see paper)
31% identity, 97% coverage: 4:237/241 of query aligns to 1027:1266/1270 of A0A1U8QWA2
- G1036 (= G13) mutation to A: Compromises binding of the cosubstrate NADPH to aldehyde reductase domain R2. Decreases the aldehyde reductase activity by 4,000-fold; when associated with F-1178.
- Y1178 (= Y152) mutation to F: Does not substantially affect carboxylic acid reductase activity but results to a 150-fold loss of aldehyde reductase activity and the accumulation of glycine betaine aldehyde intermediate. Further decreases the aldehyde reductase activity by 4,000-fold; when associated with F-1178.
Sites not aligning to the query:
- 14:418 Adenylation (A) domain
- 643:937 Carboxylic acid reductase domain R1
- 812 Y→F: Abolishes overall carboxylic acid reductase activity but does nor affect aldehyde reductase activity.
- 1026:1256 Aldehyde reductase domain R2
3pk0B Crystal structure of short-chain dehydrogenase/reductase sdr from mycobacterium smegmatis (see paper)
29% identity, 100% coverage: 1:240/241 of query aligns to 5:258/262 of 3pk0B
4bmsF Short chain alcohol dehydrogenase from ralstonia sp. Dsm 6428 in complex with NADPH
30% identity, 94% coverage: 1:226/241 of query aligns to 1:233/249 of 4bmsF
- active site: S137 (= S139), H147 (≠ E149), Y150 (= Y152), K154 (= K156), Q195 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G13), N15 (≠ A15), S16 (= S16), I18 (= I18), R38 (= R38), R39 (≠ N39), A59 (≠ T59), D60 (= D60), V61 (≠ L61), N87 (= N87), S88 (≠ A88), G89 (= G89), V110 (≠ L110), S137 (= S139), Y150 (= Y152), K154 (= K156), G181 (= G183), I183 (≠ V185), T185 (= T187), I187 (≠ L189)
6ihhA Crystal structure of rasadh f12 from ralstonia.Sp in complex with NADPH and a6o
30% identity, 94% coverage: 1:226/241 of query aligns to 1:233/249 of 6ihhA
- binding (2R,3S)-2-ethyl-2-[(2E)-2-(6-methoxy-3,4-dihydro-2H-naphthalen-1-ylidene)ethyl]-3-oxidanyl-cyclopentan-1-one: S137 (= S139), H147 (≠ E149), Y150 (= Y152), L188 (= L190)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G13), N15 (≠ A15), S16 (= S16), G17 (= G17), I18 (= I18), R38 (= R38), R39 (≠ N39), D60 (= D60), V61 (≠ L61), N87 (= N87), S88 (≠ A88), G89 (= G89), V110 (≠ L110), T135 (= T137), S137 (= S139), Y150 (= Y152), K154 (= K156), P180 (= P182), G181 (= G183), A182 (≠ P184), I183 (≠ V185), T185 (= T187), S187 (≠ L189)
Sites not aligning to the query:
8fd8A Human 15-pgdh with nadh bound (see paper)
34% identity, 76% coverage: 4:186/241 of query aligns to 3:187/223 of 8fd8A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I17 (= I18), D36 (= D37), W37 (≠ R38), D64 (= D60), V65 (≠ L61), N91 (= N87), A92 (= A88), G93 (= G89), I106 (≠ L110), K155 (= K156), G184 (= G183), V186 (= V185)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
34% identity, 90% coverage: 4:220/241 of query aligns to 8:231/258 of 4wecA
- active site: G21 (= G17), S143 (= S139), Q154 (≠ P150), Y157 (= Y152), K161 (= K156)
- binding nicotinamide-adenine-dinucleotide: G17 (= G13), A19 (= A15), S20 (= S16), G21 (= G17), I22 (= I18), D41 (= D37), I42 (≠ R38), V61 (≠ I57), D62 (= D60), V63 (≠ L61), N89 (= N87), T141 (= T137), Y157 (= Y152), K161 (= K156), P187 (= P182), P189 (= P184), V190 (= V185)
P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
31% identity, 93% coverage: 1:225/241 of query aligns to 1:229/247 of P73574
- A14 (≠ G14) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ V147) mutation to F: 2.7-fold increase in activity on acetoacetyl-CoA.; mutation to V: 5.7-fold increase in activity on acetoacetyl-CoA.
- K160 (= K156) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ P184) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ P194) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
H9XP47 Meso-2,3-butanediol dehydrogenase; BDH; meso-2,3-BDH; (R,S)-butane-2,3-diol dehydrogenase; NAD(H)-dependent meso-2,3-BDH; SmBdh; EC 1.1.1.- from Serratia marcescens (see paper)
31% identity, 91% coverage: 4:222/241 of query aligns to 3:224/251 of H9XP47
- N15 (≠ S16) binding
- M17 (≠ I18) binding
- D36 (= D37) binding
- D60 (= D60) binding
- V61 (≠ L61) binding
- N87 (= N87) binding
- S138 (= S139) binding ; binding
- V139 (= V140) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ A141) binding
- Y151 (= Y152) binding ; binding ; binding
- K155 (= K156) binding
- V184 (= V185) binding
- T186 (= T187) binding
- RDK 197:199 (≠ KPK 195:197) mutation to SEAAGKPLGYGTET: Mimics longer alpha6 helix. Retains 3% of activity with acetoin as substrate.
Sites not aligning to the query:
- 247 Q→A: Retains 10% of activity with acetoin as substrate. Retains 50% of activity with acetoin as substrate; when associated with Q-139.
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
31% identity, 91% coverage: 4:222/241 of query aligns to 3:224/251 of 6xewA
- active site: G16 (= G17), S138 (= S139), Y151 (= Y152)
- binding r,3-hydroxybutan-2-one: S138 (= S139), S140 (≠ A141), Y151 (= Y152)
- binding s,3-hydroxybutan-2-one: S138 (= S139), Y151 (= Y152), S182 (≠ G183)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ S16), G16 (= G17), M17 (≠ I18), D36 (= D37), W37 (≠ R38), W37 (≠ R38), A38 (≠ N39), I59 (≠ T59), D60 (= D60), V61 (≠ L61), N87 (= N87), A88 (= A88), G89 (= G89), V110 (≠ L110), T136 (= T137), S138 (= S139), Y151 (= Y152), K155 (= K156), S182 (≠ G183), L183 (≠ P184), V184 (= V185), T186 (= T187), N187 (≠ A188), M188 (≠ L189), T189 (≠ L190)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
31% identity, 91% coverage: 4:222/241 of query aligns to 3:224/251 of 6vspA
- active site: G16 (= G17), S138 (= S139), Y151 (= Y152)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ S16), G16 (= G17), M17 (≠ I18), D36 (= D37), W37 (≠ R38), W37 (≠ R38), A38 (≠ N39), I59 (≠ T59), D60 (= D60), V61 (≠ L61), N87 (= N87), A88 (= A88), G89 (= G89), V90 (≠ A90), V110 (≠ L110), T136 (= T137), S138 (= S139), Y151 (= Y152), K155 (= K156), P181 (= P182), S182 (≠ G183), L183 (≠ P184), V184 (= V185), T186 (= T187), N187 (≠ A188), M188 (≠ L189), T189 (≠ L190)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
31% identity, 91% coverage: 4:222/241 of query aligns to 5:226/252 of 6vspB
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
32% identity, 90% coverage: 4:220/241 of query aligns to 5:232/254 of 4fn4A
- active site: G18 (= G17), S144 (= S139), Y157 (= Y152), K161 (= K156), S202 (≠ K197)
- binding nicotinamide-adenine-dinucleotide: G14 (= G13), S17 (= S16), G18 (= G17), I19 (= I18), E38 (≠ I36), L39 (vs. gap), R43 (= R38), A63 (≠ T59), D64 (= D60), V65 (≠ L61), N91 (= N87), G93 (= G89), I94 (≠ A90), T142 (= T137), S144 (= S139), Y157 (= Y152), K161 (= K156), P187 (= P182), V190 (= V185), T192 (= T187), N193 (≠ A188), I194 (≠ L189)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
29% identity, 92% coverage: 2:222/241 of query aligns to 9:246/267 of Q9LBG2
- 17:42 (vs. 10:35, 46% identical) binding
- E103 (≠ A98) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
Query Sequence
>3607132 FitnessBrowser__Dino:3607132
MTDLSGKVVAITGGASGIGLACARACIDAGAKVAIIDRNATALEEVRAELGAQAVPIVTD
LMDKASVAQMLSRILDKAGRLDAFHANAGAYVGGDVLAGDPDEWDHVLNLNINAAFRSVH
AVLPHLAKQGSGDVILTSSVAGVIPVVWEPIYTASKHAVQAFTHSVRRQMSKHGVRVGAI
LPGPVVTALLDDWPKPKMEQALAEGSLMQPKDVADCVVFMLTRPSNVTIRDLVLLPNAVD
L
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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