SitesBLAST
Comparing Ga0059261_2871 FitnessBrowser__Korea:Ga0059261_2871 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)
3ak4A Crystal structure of nadh-dependent quinuclidinone reductase from agrobacterium tumefaciens
42% identity, 97% coverage: 6:252/254 of query aligns to 5:257/258 of 3ak4A
- active site: G18 (= G19), S141 (= S138), L151 (≠ K148), Y154 (= Y151), K158 (= K155), E199 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: K17 (≠ S18), G18 (= G19), I19 (≠ M20), D38 (= D39), L39 (= L40), V60 (= V59), D61 (= D60), V62 (= V61), N88 (≠ A87), A89 (= A88), G90 (= G89), T139 (≠ F136), S141 (= S138), Y154 (= Y151), K158 (= K155), G185 (vs. gap), V187 (≠ I183), T189 (= T185), M191 (= M187)
7wbcA Hydroxysteroid dehydrogenase wild-type complexed with NAD+ and (4s)-2- 2-methyl-2,4-pentanediol
35% identity, 98% coverage: 6:254/254 of query aligns to 3:250/250 of 7wbcA
- binding calcium ion: Y115 (≠ T113), P116 (≠ G114), H119 (≠ L117)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), G16 (= G19), I17 (≠ M20), D36 (= D39), V37 (≠ L40), A61 (≠ V59), D62 (= D60), I63 (≠ V61), N89 (≠ A87), F138 (= F136), S140 (= S138), Y153 (= Y151), K157 (= K155), P183 (= P181), F184 (≠ Y188), A185 (≠ D189), T187 (= T191), G189 (≠ S193), V190 (≠ S194)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
33% identity, 96% coverage: 6:249/254 of query aligns to 5:251/255 of 5itvA
- active site: G18 (= G19), S141 (= S138), Y154 (= Y151), K158 (= K155)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), S17 (= S18), G18 (= G19), I19 (≠ M20), D38 (= D39), I39 (≠ L40), T61 (≠ V59), I63 (≠ V61), N89 (≠ A87), G91 (= G89), T139 (≠ F136), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), G185 (vs. gap), I186 (≠ T182), I187 (= I183)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
34% identity, 97% coverage: 6:252/254 of query aligns to 5:244/244 of 4nbuB
- active site: G18 (= G19), N111 (= N111), S139 (= S138), Q149 (≠ K148), Y152 (= Y151), K156 (= K155)
- binding acetoacetyl-coenzyme a: D93 (≠ G93), K98 (≠ S98), S139 (= S138), N146 (≠ Y145), V147 (≠ P146), Q149 (≠ K148), Y152 (= Y151), F184 (≠ I183), M189 (= M195), K200 (≠ A206)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G15), N17 (≠ S18), G18 (= G19), I19 (≠ M20), D38 (= D39), F39 (≠ L40), V59 (= V59), D60 (= D60), V61 (= V61), N87 (≠ A87), A88 (= A88), G89 (= G89), I90 (= I90), T137 (≠ F136), S139 (= S138), Y152 (= Y151), K156 (= K155), P182 (= P181), F184 (≠ I183), T185 (= T191), T187 (≠ S193), M189 (= M195)
1iy8A Crystal structure of levodione reductase (see paper)
32% identity, 95% coverage: 9:249/254 of query aligns to 5:253/258 of 1iy8A
- active site: G15 (= G19), S143 (= S138), Q153 (≠ K148), Y156 (= Y151), K160 (= K155)
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), S14 (= S18), G15 (= G19), L16 (≠ M20), D35 (= D39), V36 (≠ L40), A62 (≠ V59), D63 (= D60), V64 (= V61), N90 (≠ A87), G92 (= G89), I93 (= I90), T141 (≠ F136), S143 (= S138), Y156 (= Y151), K160 (= K155), P186 (= P181), G187 (vs. gap), T191 (= T185), P192 (= P186), M193 (= M187)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
33% identity, 95% coverage: 9:249/254 of query aligns to 14:262/267 of Q9LBG2
- 17:42 (vs. 12:37, 38% identical) binding
- E103 (≠ A91) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
37% identity, 96% coverage: 6:249/254 of query aligns to 3:247/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), Q15 (≠ S18), G16 (= G19), I17 (≠ M20), D36 (= D39), V63 (= V61), N89 (≠ A87), A91 (≠ G89), S94 (≠ P92), I142 (≠ F136), S143 (≠ A137), S144 (= S138), Y157 (= Y151), K161 (= K155), P187 (= P181), H188 (≠ T182), I190 (= I183), I194 (≠ M187)
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)
34% identity, 96% coverage: 6:249/254 of query aligns to 3:242/248 of Q9KJF1
- S15 (= S18) binding
- D36 (= D39) binding
- D62 (= D60) binding
- I63 (≠ V61) binding
- N89 (≠ A87) binding
- Y153 (= Y151) binding
- K157 (= K155) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
34% identity, 96% coverage: 6:249/254 of query aligns to 2:241/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), M16 (= M20), D35 (= D39), I36 (≠ L40), I62 (≠ V61), N88 (≠ A87), G90 (= G89), I138 (≠ F136), S140 (= S138), Y152 (= Y151), K156 (= K155), I185 (= I183)
3rwbA Crystal structure of complex of 4pal (4-pyridoxolactone) and pldh (tetrameric pyridoxal 4-dehydrogenase) from mesorhizobium loti
34% identity, 98% coverage: 6:254/254 of query aligns to 4:246/247 of 3rwbA
- active site: G17 (= G19), S140 (= S138), Y153 (= Y151), K157 (= K155)
- binding 7-hydroxy-6-methylfuro[3,4-c]pyridin-1(3H)-one: S140 (= S138), N141 (≠ S139), T142 (≠ A140), M150 (≠ K148), Y153 (= Y151), L185 (≠ I183), H196 (= H203)
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), Q16 (≠ S18), G17 (= G19), I18 (≠ M20), D37 (= D39), I38 (≠ L40), D60 (= D60), I61 (≠ V61), N87 (≠ A87), A88 (= A88), S89 (≠ G89), I138 (≠ F136), S140 (= S138), Y153 (= Y151), K157 (= K155), P183 (= P181), L185 (≠ I183), I186 (≠ M195), S188 (≠ T197), G190 (≠ Q199), V191 (≠ L200)
3ndrA Crystal structure of tetrameric pyridoxal 4-dehydrogenase from mesorhizobium loti
34% identity, 98% coverage: 6:254/254 of query aligns to 4:246/247 of 3ndrA
- active site: G17 (= G19), S140 (= S138), Y153 (= Y151), K157 (= K155)
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), Q16 (≠ S18), G17 (= G19), I18 (≠ M20), D37 (= D39), I38 (≠ L40), D60 (= D60), I61 (≠ V61), N87 (≠ A87), A88 (= A88), S89 (≠ G89), V110 (= V110), I138 (≠ F136), S140 (= S138), Y153 (= Y151), K157 (= K155), P183 (= P181), L185 (≠ I183), I186 (≠ M195), S188 (≠ T197), G190 (≠ Q199), V191 (≠ L200)
5u9pB Crystal structure of a gluconate 5-dehydrogenase from burkholderia cenocepacia j2315 in complex with NADP and tartrate
36% identity, 97% coverage: 3:249/254 of query aligns to 10:256/261 of 5u9pB
- active site: G27 (= G19), S152 (= S138), Y165 (= Y151), K169 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G23 (= G15), R26 (≠ S18), G27 (= G19), I28 (≠ M20), R48 (≠ L40), D73 (= D60), V74 (= V61), N100 (≠ A87), A101 (= A88), I150 (≠ F136), Y165 (= Y151), K169 (= K155), P195 (= P181), F198 (≠ D189), T200 (= T191), L202 (≠ S193), N203 (≠ S194)
6qheA Alcohol dehydrogenase from arthrobacter sp. Ts-15 in complex with NAD+
37% identity, 96% coverage: 6:248/254 of query aligns to 5:252/261 of 6qheA
- binding nicotinamide-adenine-dinucleotide: G14 (= G15), M17 (≠ S18), G18 (= G19), M19 (= M20), D38 (= D39), R39 (≠ L40), D63 (= D60), I64 (≠ V61), A90 (= A87), A91 (= A88), S142 (= S138), Y156 (= Y151), K160 (= K155), P186 (= P181), G187 (vs. gap), M189 (≠ I183), T191 (= T185), P192 (= P186), M193 (= M187)
3pk0B Crystal structure of short-chain dehydrogenase/reductase sdr from mycobacterium smegmatis (see paper)
35% identity, 97% coverage: 6:252/254 of query aligns to 8:253/262 of 3pk0B
P9WGT1 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase; NADH-dependent 3alpha, 20beta-hydroxysteroid dehydrogenase; EC 1.1.1.53 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
36% identity, 99% coverage: 1:251/254 of query aligns to 1:239/260 of P9WGT1
- I6 (≠ L6) mutation to T: Maximal improvement in solubility; when associated with M-47 and K-69.
- RGM 17:19 (≠ SGM 18:20) binding
- D38 (= D39) binding
- V47 (= V48) mutation to M: Maximal improvement in solubility; when associated with T-6 and K-69.
- DV 61:62 (= DV 60:61) binding
- T69 (≠ D68) mutation to K: Maximal improvement in solubility; when associated with T-6 and M-47.
- N88 (≠ A87) binding
- S140 (= S138) mutation to A: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- Y153 (= Y151) binding ; mutation to F: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- K157 (= K155) binding
- 183:191 (vs. 181:188, 44% identical) binding
4ituA Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) bound to s-hpc and nadh (see paper)
37% identity, 86% coverage: 32:249/254 of query aligns to 29:249/253 of 4ituA
- active site: N113 (= N111), S141 (= S138), Y154 (= Y151), K158 (= K155)
- binding 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonic acid: S141 (= S138), Y154 (= Y151), T186 (vs. gap), R209 (≠ D204), Y213 (≠ I211)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D36 (= D39), L37 (= L40), D62 (= D60), V63 (= V61), N89 (≠ A87), V112 (= V110), F139 (= F136), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), T186 (vs. gap), V187 (≠ T182), T190 (= T185), M192 (= M187)
Sites not aligning to the query:
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)
37% identity, 86% coverage: 32:249/254 of query aligns to 31:251/255 of A7IQH5
- D38 (= D39) binding
- DV 64:65 (= DV 60:61) binding
- N91 (≠ A87) binding
- S143 (= S138) binding ; mutation to A: Retains very weak activity.
- Y156 (= Y151) binding ; mutation to A: Retains some activity but with more than 2200-fold decrease in catalytic efficiency.; mutation to F: Loss of activity.
- K160 (= K155) binding ; mutation to A: Loss of activity.
- T188 (vs. gap) binding
- VTSTG 189:193 (≠ TIWTP 182:186) binding
- R211 (≠ D204) 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 (≠ A210) 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 (≠ I211) binding
Sites not aligning to the query:
4gh5A Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) (see paper)
37% identity, 86% coverage: 32:249/254 of query aligns to 29:244/248 of 4gh5A
- active site: N113 (= N111), S141 (= S138), Y154 (= Y151), K158 (= K155)
- binding nicotinamide-adenine-dinucleotide: D36 (= D39), L37 (= L40), A61 (≠ V59), D62 (= D60), V63 (= V61), N89 (≠ A87), A90 (= A88), V112 (= V110), F139 (= F136), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), V187 (≠ W184), T190 (≠ S193), G191 (≠ S194), M192 (= M195)
Sites not aligning to the query:
5jy1A Crystal structure of putative short-chain dehydrogenase/reductase from burkholderia xenovorans lb400 bound to NAD
34% identity, 96% coverage: 5:249/254 of query aligns to 3:248/266 of 5jy1A
- active site: G17 (= G19), S143 (= S138), H153 (≠ K148), Y156 (= Y151), K160 (= K155), P201 (≠ D198)
- binding nicotinamide-adenine-dinucleotide: G13 (= G15), G17 (= G19), I18 (≠ M20), E37 (≠ D39), I38 (≠ L40), T62 (≠ V59), D63 (= D60), V64 (= V61), N90 (≠ A87), A91 (= A88), F92 (≠ G89), V93 (≠ I90), S143 (= S138), Y156 (= Y151), K160 (= K155), P186 (= P181), T187 (= T182), A188 (≠ I183), A191 (≠ P186)
6b9uA Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase from brucella melitensis complexed with nadh
33% identity, 96% coverage: 6:249/254 of query aligns to 2:241/244 of 6b9uA
- active site: G15 (= G19), S142 (= S138), L152 (≠ K148), Y155 (= Y151), K159 (= K155)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G11 (= G15), S14 (= S18), G15 (= G19), F16 (≠ M20), D35 (= D39), R36 (≠ L40), A57 (vs. gap), D58 (= D60), I59 (≠ V61), N85 (≠ A87), A86 (= A88), V140 (≠ F136), S142 (= S138), Y155 (= Y151), K159 (= K155), A187 (vs. gap), G188 (vs. gap), T190 (≠ A180), P191 (= P181), L192 (≠ T182), F196 (≠ P186)
Query Sequence
>Ga0059261_2871 FitnessBrowser__Korea:Ga0059261_2871
MADRMLEGRRIIVTGGASGMGAGLVRALPAMGARVVSLDLNADAGARVAGEAGATFLAVD
VTDKASVDAATNQAVAALDGLDVLIHAAGIAPGAPAESIPPEQWLEAIAVNATGTFLVNQ
AVFPHLKDHGGAIINFASSAGIKGYPGKAAYAAAKGAVVAWVRSIASEWGRYNIRVNAIA
PTIWTPMYDKTRSSMSTDQLAAHDAALKVAIPIGGKLGDIRRDLVPVVAFLASDGAHFMT
GQIIPVDGGALMMR
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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