SitesBLAST
Comparing WP_110805876.1 NCBI__GCF_003217355.1:WP_110805876.1 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)
3m4rA Structure of the n-terminal class ii aldolase domain of a conserved protein from thermoplasma acidophilum
39% identity, 32% coverage: 2:215/677 of query aligns to 2:205/213 of 3m4rA
8ijgC Crystal structure of alcohol dehydrogenase m5 from burkholderia gladioli with NADP
34% identity, 29% coverage: 418:610/677 of query aligns to 4:185/250 of 8ijgC
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G427), T15 (≠ A429), S16 (≠ G430), I18 (= I432), R38 (= R452), R39 (≠ P453), D60 (= D474), V61 (≠ I475), N87 (= N501), G89 (= G503), R110 (≠ L524), N135 (= N560), A137 (≠ S562), Y150 (= Y575), K154 (= K579), P180 (≠ A605), G181 (≠ D606), T183 (≠ I608), T185 (≠ S610)
Sites not aligning to the query:
3ai3C The crystal structure of l-sorbose reductase from gluconobacter frateurii complexed with NADPH and l-sorbose (see paper)
32% identity, 38% coverage: 418:673/677 of query aligns to 5:261/263 of 3ai3C
- active site: G18 (≠ A431), S144 (= S562), Y157 (= Y575), K161 (= K579)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G14 (= G427), S16 (≠ A429), S17 (≠ G430), G18 (≠ A431), I19 (= I432), A38 (≠ D451), R39 (= R452), Q40 (≠ P453), R43 (≠ V456), D65 (= D474), V66 (≠ I475), N92 (= N501), G94 (= G503), N142 (= N560), Y157 (= Y575), K161 (= K579), P187 (≠ A605), G188 (≠ D606), I190 (= I608), T192 (= T614), W195 (≠ M617)
- binding alpha-L-sorbopyranose: A252 (≠ V664), F254 (≠ T666)
- binding L-sorbose: G96 (= G508), E154 (≠ F572), Y157 (= Y575), W195 (≠ M617)
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, 38% coverage: 418:673/677 of query aligns to 5:261/263 of 3ai3A
- active site: G18 (≠ A431), S144 (= S562), Y157 (= Y575), K161 (= K579)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G14 (= G427), S16 (≠ A429), S17 (≠ G430), G18 (≠ A431), I19 (= I432), A38 (≠ D451), R39 (= R452), Q40 (≠ P453), R43 (≠ V456), V64 (≠ C473), D65 (= D474), V66 (≠ I475), N92 (= N501), G94 (= G503), N142 (= N560), S144 (= S562), Y157 (= Y575), K161 (= K579), P187 (≠ A605), G188 (≠ D606), I190 (= I608), T192 (= T614), W195 (≠ M617)
- binding L-sorbose: G96 (= G508), S144 (= S562), L151 (≠ G569), E154 (≠ F572), Y157 (= Y575), G188 (≠ D606)
3ai2A The crystal structure of l-sorbose reductase from gluconobacter frateurii complexed with NADPH (see paper)
31% identity, 38% coverage: 418:673/677 of query aligns to 5:261/263 of 3ai2A
- active site: G18 (≠ A431), S144 (= S562), Y157 (= Y575), K161 (= K579)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G14 (= G427), S16 (≠ A429), S17 (≠ G430), G18 (≠ A431), I19 (= I432), A38 (≠ D451), R39 (= R452), Q40 (≠ P453), V64 (≠ C473), D65 (= D474), V66 (≠ I475), N92 (= N501), G94 (= G503), N142 (= N560), Y157 (= Y575), K161 (= K579), P187 (≠ A605), I190 (= I608), T192 (= T614), W195 (≠ M617)
P47227 Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase; 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase; 2,3-dihydroxy-4-phenylhexa-4,6-diene dehydrogenase; Biphenyl-2,3-dihydro-2,3-diol dehydrogenase; Biphenyl-cis-diol dehydrogenase; EC 1.3.1.56 from Paraburkholderia xenovorans (strain LB400) (see paper)
30% identity, 37% coverage: 418:670/677 of query aligns to 3:254/277 of P47227
- 9:36 (vs. 424:451, 43% identical) binding NAD(+)
- D59 (= D474) binding NAD(+)
- K159 (= K579) binding NAD(+)
2ewmB Crystal structure of the (s)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain ebn1 (see paper)
29% identity, 38% coverage: 418:672/677 of query aligns to 3:245/247 of 2ewmB
- active site: G16 (≠ A431), S139 (= S562), Y149 (≠ F572), Y152 (= Y575), K156 (= K579)
- binding nicotinamide-adenine-dinucleotide: G12 (= G427), N15 (≠ G430), G16 (≠ A431), I17 (= I432), D36 (= D451), L37 (≠ R452), C59 (= C473), D60 (= D474), V61 (≠ I475), N87 (= N501), S139 (= S562), Y152 (= Y575), K156 (= K579), P182 (≠ A605), S183 (≠ D606), L184 (≠ R607), V185 (≠ I608), T189 (≠ L612)
Q5P5I4 (S)-1-Phenylethanol dehydrogenase; EC 1.1.1.311 from Aromatoleum aromaticum (strain DSM 19018 / LMG 30748 / EbN1) (Azoarcus sp. (strain EbN1)) (see 2 papers)
29% identity, 38% coverage: 418:672/677 of query aligns to 5:247/249 of Q5P5I4
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3pk0B Crystal structure of short-chain dehydrogenase/reductase sdr from mycobacterium smegmatis (see paper)
32% identity, 38% coverage: 418:672/677 of query aligns to 8:252/262 of 3pk0B
A0A3Q8GL18 (+)-cis,trans-nepetalactol synthase NEPS1; Nepetalactol-related short-chain dehydrogenase; Nepetalactol dehydrogenase; Nepetalactol-related short-chain reductase 1; Nepetalactol-related SDR1; NmNEPS1; EC 5.5.1.34; EC 1.1.1.419 from Nepeta racemosa (Catmint) (Raceme catnip) (see paper)
28% identity, 37% coverage: 418:670/677 of query aligns to 15:261/271 of A0A3Q8GL18
- N125 (≠ S533) mutation to A: Strongly reduced cis-trans-nepetalactone levels.
- T152 (≠ N560) mutation to N: Absence of cis-trans-nepetalactone.
- T153 (≠ V561) mutation to A: Almost normal cis-trans-nepetalactone levels.
- T154 (≠ S562) mutation to G: Loss of dehydrogenase activity and strongly enhanced cis-trans-nepetalactol levels associated with a huge increase in Km for cis-trans-nepetalactol.
- P155 (≠ K563) mutation to S: Strongly reduced cis-trans-nepetalactone levels.
- L156 (≠ Q564) mutation to S: Reduced dehydrogenase activity and absence of cis-trans-nepetalactone.
- Y167 (= Y575) mutation to F: Absence of cis-trans-nepetalactone.
- K171 (= K579) mutation to M: Absence of cis-trans-nepetalactone.
- S198 (≠ D606) mutation to M: Absence of cis-trans-nepetalactone.
- V199 (≠ R607) mutation to A: Almost normal cis-trans-nepetalactone levels.
- T202 (vs. gap) mutation to A: Absence of cis-trans-nepetalactone.
1bdbA Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from pseudomonas sp. Lb400 (see paper)
31% identity, 30% coverage: 418:618/677 of query aligns to 3:197/267 of 1bdbA
- active site: G16 (≠ A431), S142 (= S562), Y155 (= Y575), K159 (= K579)
- binding nicotinamide-adenine-dinucleotide: G12 (= G427), S15 (≠ G430), G16 (≠ A431), L17 (≠ I432), D36 (= D451), K37 (≠ R452), D59 (= D474), V60 (≠ I475), N86 (= N501), T140 (≠ N560), S142 (= S562), Y155 (= Y575), K159 (= K579), G185 (≠ D606), I187 (= I608), S189 (= S610), D190 (≠ G611), L191 (= L612)
6zyzA Structure of the borneol dehydrogenases of salvia rosmarinus with NAD+ (see paper)
30% identity, 37% coverage: 418:670/677 of query aligns to 3:245/259 of 6zyzA
- binding nicotinamide-adenine-dinucleotide: G12 (= G427), S15 (≠ G430), G16 (≠ A431), I17 (= I432), D36 (= D451), I37 (≠ R452), Q38 (≠ P453), C58 (= C473), D59 (= D474), V60 (≠ I475), N86 (= N501), A87 (= A502), V90 (≠ I506), I110 (≠ L524), T137 (≠ N560), Y152 (= Y575), K156 (= K579), V185 (≠ I608)
- binding (2S)-1-[3-{[(2R)-2-hydroxypropyl]oxy}-2,2-bis({[(2R)-2-hydroxypropyl]oxy}methyl)propoxy]propan-2-ol: P93 (vs. gap), N94 (vs. gap), S95 (≠ D509), D98 (≠ T512)
F1SWA0 Zerumbone synthase; EC 1.1.1.326 from Zingiber zerumbet (Shampoo ginger) (Amomum zerumbet) (see paper)
31% identity, 37% coverage: 418:670/677 of query aligns to 3:255/267 of F1SWA0
- S142 (= S562) mutation to A: Strong reduction in oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- S144 (≠ Q564) mutation to A: Increased oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- Y155 (= Y575) mutation to A: Strong reduction in oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- K159 (= K579) mutation to A: Abolishes all oxidoreductase activity.
6ci9D Rmm microcompartment-associated aminopropanol dehydrogenase NADP + aminoacetone holo-structure (see paper)
31% identity, 28% coverage: 417:603/677 of query aligns to 6:187/259 of 6ci9D
- active site: G20 (≠ A431), S145 (≠ Q564), Y159 (= Y575)
- binding 1-aminopropan-2-one: F97 (≠ A505), S145 (≠ Q564), T147 (≠ V566), W156 (vs. gap), Y159 (= Y575)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G16 (= G427), S18 (≠ A429), G20 (≠ A431), I21 (= I432), G40 (≠ D451), R41 (= R452), N42 (≠ P453), D66 (= D474), V67 (≠ I475), N93 (= N501), G95 (= G503), T143 (≠ S562), S145 (≠ Q564), Y159 (= Y575), K163 (= K579)
Sites not aligning to the query:
1zemA Crystal structure of NAD+-bound xylitol dehydrogenase (see paper)
32% identity, 29% coverage: 418:613/677 of query aligns to 3:193/260 of 1zemA
- active site: N16 (≠ A431), S142 (= S562), Y155 (= Y575), K159 (= K579)
- binding nicotinamide-adenine-dinucleotide: G12 (= G427), G15 (= G430), N16 (≠ A431), I17 (= I432), D36 (= D451), M37 (≠ R452), D62 (= D474), V63 (≠ I475), N89 (= N501), A90 (= A502), G91 (= G503), T140 (≠ N560), S142 (= S562), Y155 (= Y575), K159 (= K579), P185 (≠ A605), M188 (≠ I608)
Sites not aligning to the query:
7qujA Structure of nsneps2, a 7s-cis-trans nepetalactone synthase (see paper)
30% identity, 37% coverage: 418:670/677 of query aligns to 4:254/259 of 7qujA
- binding nicotinamide-adenine-dinucleotide: G13 (= G427), S16 (≠ G430), G17 (≠ A431), I18 (= I432), D38 (= D451), I39 (≠ R452), Q40 (≠ P453), C61 (= C473), D62 (= D474), I63 (= I475), N89 (= N501), A90 (= A502), G91 (= G503), T145 (≠ N560), S146 (≠ V561), Y160 (= Y575), K164 (= K579), P190 (≠ A605), M191 (≠ D606), A192 (≠ R607), V193 (≠ I608), T195 (vs. gap), L197 (vs. gap), T198 (vs. gap)
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)
28% identity, 31% coverage: 405:612/677 of query aligns to 17:219/278 of Q9BTZ2
- S176 (≠ G569) 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 (= F572) 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 (≠ Q588) 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.
3zv6A Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (bphb) from pandoraea pnomenusa strain b-356 complex with co-enzyme NAD and product analog 4,4'-dihydroxybiphenyl (see paper)
30% identity, 30% coverage: 418:618/677 of query aligns to 3:197/275 of 3zv6A