SitesBLAST
Comparing CA265_RS14445 FitnessBrowser__Pedo557:CA265_RS14445 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)
Q9BTZ2 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; NADPH-dependent retinol dehydrogenase/reductase; NRDR; humNRDR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; SCAD-SRL; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; Short-chain dehydrogenase/reductase family member 4; EC 1.1.1.184 from Homo sapiens (Human) (see 2 papers)
33% identity, 96% coverage: 5:244/250 of query aligns to 30:273/278 of Q9BTZ2
- S176 (vs. gap) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to F: Decreased reduction activity for benzil, isatin and retinal and increased activity for 5beta-Pregnane-3,20-dione and 5beta-Dihydrotestosterone. No change of stereoselectivity in 3-ketosteroids reduction and no change in 3beta-hydroxysteroid oxidation. Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with L-179. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with L-179. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with L-179. Loss of cold catalytic inactivation; when associated with L-179 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with L-179 and N-195.
- F179 (≠ L150) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to L: Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with F-176. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with F-176. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176. Loss of cold catalytic inactivation; when associated with F-176 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and N-195.
- T195 (≠ Q166) mutation to N: Loss of cold catalytic inactivation. Loss of cold catalytic inactivation; when associated with F-176 and L-179. Switch in stereoselective activity from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176 and L-179. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and L-179.
3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
33% identity, 96% coverage: 5:244/250 of query aligns to 6:249/254 of 3o4rA
- active site: G19 (= G18), S145 (= S143), F155 (≠ L150), Y158 (≠ S153), K162 (= K157), K203 (≠ D198)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G14), T17 (≠ S16), D18 (≠ K17), G19 (= G18), I20 (= I19), S39 (≠ G38), R40 (= R39), K41 (≠ N40), N44 (≠ S43), H65 (≠ Q64), V66 (≠ D65), N92 (= N92), A94 (≠ G94), S145 (= S143), Y158 (≠ S153), K162 (= K157), P188 (= P183), G189 (= G184), L190 (= L185), I191 (= I186), T193 (= T188), F195 (≠ N190), S196 (≠ I191)
5vpsA Crystal structure of an sdr from burkholderia ambifaria in complex with NADPH with a tcep adduct (see paper)
34% identity, 100% coverage: 1:250/250 of query aligns to 2:260/260 of 5vpsA
- active site: N138 (= N140), S154 (≠ A156), R158 (vs. gap), A198 (≠ G197)
- binding [(4~{S})-3-aminocarbonyl-1-[(2~{R},3~{R},4~{S},5~{R})-5-[[[[(2~{R},3~{R},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxymethyl]-3,4-bis(oxidanyl)oxolan-2-yl]piperidin-4-yl]-tris(3-hydroxy-3-oxopropyl)phosphanium: A15 (≠ G14), S17 (= S16), G19 (= G18), L20 (≠ I19), A39 (≠ G38), R40 (= R39), T41 (≠ N40), D66 (= D65), I67 (≠ L66), N89 (= N92), A90 (= A93), G91 (= G94), G92 (≠ Q95), S141 (= S143), S142 (≠ T144), L151 (≠ S153), S154 (≠ A156), R158 (vs. gap), P184 (= P183), G185 (= G184), L186 (= L185), F187 (≠ I186), T189 (= T188), R191 (≠ N190), I192 (= I191), T195 (≠ Y194)
Q8WNV7 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; PHCR; NADPH-dependent retinol dehydrogenase/reductase; NDRD; Peroxisomal carbonyl reductase; PerCR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; EC 1.1.1.184; EC 1.1.1.300 from Sus scrofa (Pig) (see 2 papers)
32% identity, 96% coverage: 5:244/250 of query aligns to 31:274/279 of Q8WNV7
- 37:61 (vs. 11:35, 52% identical) binding
- F177 (≠ L147) Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin; mutation to S: Change in stereoselective activity by the reduction of 3-ketosteroids and benzil into 3beta-hydroxysteroid and R-benzoin, respectively; when associated with F-180.
- L180 (= L150) Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin; mutation to F: Change in stereoselective activity by the reduction of 3-ketosteroids and benzil into 3beta-hydroxysteroid and R-benzoin, respectively; when associated with S-177.
- Y183 (≠ S153) active site, Proton acceptor
- K187 (= K157) binding
- N196 (≠ Q166) Important for the maintenance of the quaternary structure, the catalytic activity and cold stability
Sites not aligning to the query:
- 277:279 Peroxisomal targeting signal
2zatA Crystal structure of a mammalian reductase (see paper)
32% identity, 96% coverage: 5:244/250 of query aligns to 3:246/251 of 2zatA
- active site: G16 (= G18), S142 (= S143), L152 (= L150), Y155 (≠ S153), K159 (= K157), K200 (≠ D198)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A12 (≠ G14), T14 (≠ S16), D15 (≠ K17), G16 (= G18), I17 (= I19), S36 (≠ G38), R37 (= R39), K38 (≠ N40), N41 (≠ S43), H62 (≠ Q64), N89 (= N92), A91 (≠ G94), V140 (≠ L141), S142 (= S143), Y155 (≠ S153), K159 (= K157), P185 (= P183), G186 (= G184), I188 (= I186), T190 (= T188), F192 (≠ N190), S193 (≠ I191)
3ai2A The crystal structure of l-sorbose reductase from gluconobacter frateurii complexed with NADPH (see paper)
32% identity, 99% coverage: 1:248/250 of query aligns to 1:262/263 of 3ai2A
- active site: G18 (= G18), S144 (= S143), Y157 (≠ S153), K161 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G14 (= G14), S16 (= S16), S17 (≠ K17), G18 (= G18), I19 (= I19), A38 (≠ G38), R39 (= R39), Q40 (≠ N40), V64 (≠ Q64), D65 (= D65), V66 (≠ L66), N92 (= N92), G94 (= G94), N142 (≠ L141), Y157 (≠ S153), K161 (= K157), P187 (= P183), I190 (= I186), T192 (= T188), W195 (vs. gap)
5jc8D Crystal structure of a putative short-chain dehydrogenase/reductase from burkholderia xenovorans
36% identity, 96% coverage: 5:244/250 of query aligns to 4:256/262 of 5jc8D
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
34% identity, 97% coverage: 3:244/250 of query aligns to 1:244/247 of 4jroC
- active site: G16 (= G18), S142 (= S143), Q152 (≠ N151), Y155 (≠ A154), K159 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (= S16), R15 (≠ K17), G16 (= G18), I17 (= I19), N35 (≠ T37), Y36 (≠ G38), N37 (≠ R39), G38 (≠ N40), S39 (≠ Q41), N63 (≠ P59), V64 (≠ I60), N90 (= N92), A91 (= A93), I93 (≠ Q95), I113 (≠ L114), S142 (= S143), Y155 (≠ A154), K159 (= K157), P185 (= P183), I188 (= I186), T190 (= T188)
5va8A Crystal structure of short-chain dehydrogenase/reductase sdr from burkholderia phymatum in complex with NADP
33% identity, 98% coverage: 1:245/250 of query aligns to 3:256/261 of 5va8A
- active site: S142 (= S143), R159 (≠ V160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A16 (≠ G14), S18 (= S16), K19 (= K17), G20 (= G18), L21 (≠ I19), A40 (≠ G38), R41 (= R39), T42 (≠ N40), D67 (= D65), I68 (≠ L66), N90 (= N92), A91 (= A93), G92 (= G94), G93 (≠ Q95), R159 (≠ V160), P185 (= P183), G186 (= G184), I187 (≠ L185), F188 (≠ I186), T190 (= T188)
- binding 3,3',3''-phosphanetriyltripropanoic acid: S142 (= S143), S143 (≠ T144), I149 (≠ L150), L152 (≠ S153), S155 (≠ A156), R159 (≠ V160), G186 (= G184), T196 (≠ Y194)
3ai3C The crystal structure of l-sorbose reductase from gluconobacter frateurii complexed with NADPH and l-sorbose (see paper)
32% identity, 99% coverage: 1:248/250 of query aligns to 1:262/263 of 3ai3C
- active site: G18 (= G18), S144 (= S143), Y157 (≠ S153), K161 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G14 (= G14), S16 (= S16), S17 (≠ K17), G18 (= G18), I19 (= I19), A38 (≠ G38), R39 (= R39), Q40 (≠ N40), R43 (≠ S43), D65 (= D65), V66 (≠ L66), N92 (= N92), G94 (= G94), N142 (≠ L141), Y157 (≠ S153), K161 (= K157), P187 (= P183), G188 (= G184), I190 (= I186), T192 (= T188), W195 (vs. gap)
- binding alpha-L-sorbopyranose: A252 (≠ V238), F254 (≠ V240)
- binding L-sorbose: G96 (vs. gap), E154 (vs. gap), Y157 (≠ S153), W195 (vs. gap)
Sites not aligning to the query:
3ai3A The crystal structure of l-sorbose reductase from gluconobacter frateurii complexed with NADPH and l-sorbose (see paper)
32% identity, 99% coverage: 1:248/250 of query aligns to 1:262/263 of 3ai3A
- active site: G18 (= G18), S144 (= S143), Y157 (≠ S153), K161 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G14 (= G14), S16 (= S16), S17 (≠ K17), G18 (= G18), I19 (= I19), A38 (≠ G38), R39 (= R39), Q40 (≠ N40), R43 (≠ S43), V64 (≠ Q64), D65 (= D65), V66 (≠ L66), N92 (= N92), G94 (= G94), N142 (≠ L141), S144 (= S143), Y157 (≠ S153), K161 (= K157), P187 (= P183), G188 (= G184), I190 (= I186), T192 (= T188), W195 (vs. gap)
- binding L-sorbose: G96 (vs. gap), S144 (= S143), L151 (= L150), E154 (vs. gap), Y157 (≠ S153), G188 (= G184)
6jhaA Crystal structure of NADPH bound aerf from microcystis aeruginosa (see paper)
32% identity, 100% coverage: 1:249/250 of query aligns to 1:242/242 of 6jhaA
- active site: G18 (= G18), S145 (= S153)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G14 (= G14), S16 (= S16), I19 (= I19), G38 (= G38), R39 (= R39), N40 (= N40), D66 (= D65), V67 (≠ L66), N93 (= N92), S94 (≠ A93), E95 (≠ G94), K114 (≠ D115), I140 (≠ L141), L142 (= L150), P175 (= P183), T180 (= T188), R182 (≠ N190)
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)
32% identity, 97% coverage: 3:244/250 of query aligns to 4:243/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G14), S17 (= S16), R18 (≠ K17), I20 (= I19), T40 (≠ R39), N62 (≠ D65), V63 (≠ L66), N89 (= N92), A90 (= A93), I92 (≠ Q95), V139 (≠ L141), S141 (= S143), Y154 (≠ S153), K158 (= K157), P184 (= P183), G185 (= G184), I187 (= I186), T189 (= T188), M191 (≠ N190)
5idyB Crystal structure of an oxidoreductase from burkholderia vietnamiensis in complex with NADP
33% identity, 100% coverage: 1:250/250 of query aligns to 6:264/264 of 5idyB
- active site: N142 (= N140), S158 (≠ A156), R162 (≠ V160), A202 (≠ G197)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A19 (≠ G14), S21 (= S16), G23 (= G18), L24 (≠ I19), A43 (≠ G38), R44 (= R39), T45 (≠ N40), D70 (= D65), I71 (≠ L66), N93 (= N92), A94 (= A93), G95 (= G94), G96 (≠ Q95), S145 (= S143), R162 (≠ V160), P188 (= P183), G189 (= G184), L190 (= L185), F191 (≠ I186), T193 (= T188), R195 (≠ N190), I196 (= I191)
3tzcA Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg)(y155f) from vibrio cholerae (see paper)
31% identity, 97% coverage: 3:244/250 of query aligns to 4:222/224 of 3tzcA
1xhlB Crystal structure of putative tropinone reductase-ii from caenorhabditis elegans with cofactor and substrate
32% identity, 96% coverage: 5:245/250 of query aligns to 2:258/274 of 1xhlB
- active site: G15 (= G18), F24 (≠ L27), Q30 (≠ K33), N90 (= N91), S144 (= S143), Q150 (≠ S149), Y155 (vs. gap), Y158 (vs. gap), K162 (= K157), E203 (≠ Y194)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G14), S13 (= S16), G15 (= G18), I16 (= I19), R36 (= R39), N37 (= N40), R40 (≠ S43), D64 (= D65), V65 (≠ L66), N91 (= N92), G93 (= G94), L116 (= L114), S144 (= S143), Y158 (vs. gap), K162 (= K157), P188 (= P183), G189 (= G184), A190 (≠ L185), V191 (≠ I186), T193 (= T188), G194 (≠ E189), F195 (≠ N190)
- binding 8-methyl-8-azabicyclo[3,2,1]octan-3-one: A190 (≠ L185), F195 (≠ N190)
1xhlA Crystal structure of putative tropinone reductase-ii from caenorhabditis elegans with cofactor and substrate
32% identity, 96% coverage: 5:245/250 of query aligns to 2:258/274 of 1xhlA
- active site: G15 (= G18), F24 (≠ L27), Q30 (≠ K33), N90 (= N91), S144 (= S143), Q150 (≠ S149), Y155 (vs. gap), Y158 (vs. gap), K162 (= K157), E203 (≠ Y194)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G14), S13 (= S16), G15 (= G18), I16 (= I19), R36 (= R39), N37 (= N40), R40 (≠ S43), D64 (= D65), V65 (≠ L66), N91 (= N92), A92 (= A93), G93 (= G94), L116 (= L114), S144 (= S143), K162 (= K157), P188 (= P183), G189 (= G184), V191 (≠ I186), T193 (= T188), G194 (≠ E189), F195 (≠ N190)
A7DY56 Tropinone reductase; EC 1.1.1.206; EC 1.1.1.236 from Cochlearia officinalis (Common scurvygrass) (see paper)
32% identity, 98% coverage: 5:250/250 of query aligns to 16:265/273 of A7DY56
- Y209 (= Y194) mutation to S: Loss of tropinone or nortropinone reduction, but faster reduction of cyclohexanones.
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
36% identity, 96% coverage: 5:244/250 of query aligns to 9:251/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G14), S20 (= S16), K21 (= K17), G22 (= G18), I23 (= I19), A43 (≠ G38), S44 (≠ R39), S45 (≠ N40), G68 (≠ A63), D69 (≠ Q64), V70 (≠ D65), N96 (= N92), S97 (≠ A93), G98 (= G94), Y100 (vs. gap), I144 (≠ L141), S146 (= S143), Y159 (vs. gap), K163 (= K157), P189 (= P183), G190 (= G184), M191 (≠ L185), I192 (= I186), T194 (= T188), G196 (≠ N190), T197 (≠ I191)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S143), Y159 (vs. gap), M191 (≠ L185), I202 (≠ F195)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
32% identity, 97% coverage: 3:244/250 of query aligns to 4:239/243 of 4i08A
- active site: G19 (= G18), N113 (≠ D115), S141 (= S143), Q151 (≠ L150), Y154 (≠ S153), K158 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G14), S17 (= S16), R18 (≠ K17), I20 (= I19), T40 (≠ R39), N62 (≠ D65), V63 (≠ L66), N89 (= N92), A90 (= A93), G140 (≠ T142), S141 (= S143), Y154 (≠ S153), K158 (= K157), P184 (= P183), G185 (= G184), T189 (= T188)
Query Sequence
>CA265_RS14445 FitnessBrowser__Pedo557:CA265_RS14445
MDLYLTGKTALVTGASKGIGRAIAKELAKEGVKVFATGRNQQSLDNLFTEIVAEGSPAPI
VFAQDLLASDAPYKIATAALASLGHIDILINNAGQSQPVDVAGPEEPWTRSMALDFERPR
LLTQALLPHFIDRKQGTILNLTSTYELRSLNVSAVAKAAVAMWSKQLAGELGKYGIRVNC
LKPGLIDTENIKPYFPGDERRKYAESEIPLQDFGEVQDMANMAVFLVSPRAKYVTGTVSV
VDGGARRSAF
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