SitesBLAST
Comparing WP_014266681.1 NCBI__GCF_000178955.2:WP_014266681.1 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)
5u9pB Crystal structure of a gluconate 5-dehydrogenase from burkholderia cenocepacia j2315 in complex with NADP and tartrate
41% identity, 94% coverage: 1:252/268 of query aligns to 5:259/261 of 5u9pB
- active site: G27 (= G21), S152 (= S145), Y165 (= Y158), K169 (≠ R162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G23 (= G17), R26 (= R20), G27 (= G21), I28 (≠ L22), R48 (= R42), D73 (= D67), V74 (= V68), N100 (= N93), A101 (= A94), I150 (= I143), Y165 (= Y158), K169 (≠ R162), P195 (= P188), F198 (= F191), T200 (= T193), L202 (≠ Q195), N203 (= N196)
1vl8B Crystal structure of gluconate 5-dehydrogenase (tm0441) from thermotoga maritima at 2.07 a resolution
40% identity, 91% coverage: 5:249/268 of query aligns to 1:248/252 of 1vl8B
- active site: G17 (= G21), S143 (= S145), I154 (≠ L155), Y157 (= Y158), K161 (≠ R162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G17), R16 (= R20), G17 (= G21), L18 (= L22), S37 (= S41), R38 (= R42), C63 (≠ L66), D64 (= D67), V65 (= V68), A91 (≠ N93), A92 (= A94), G93 (= G95), I94 (≠ C96), V114 (≠ T116), I141 (= I143), S143 (= S145), Y157 (= Y158), K161 (≠ R162), P187 (= P188), G188 (= G189), Y190 (≠ F191), T192 (= T193), M194 (≠ Q195), T195 (≠ N196)
4za2D Crystal structure of pectobacterium carotovorum 2-keto-3-deoxy-d- gluconate dehydrogenase complexed with NAD+ (see paper)
38% identity, 93% coverage: 1:249/268 of query aligns to 1:243/247 of 4za2D
- binding nicotinamide-adenine-dinucleotide: G17 (= G17), D19 (≠ S19), L22 (= L22), I42 (vs. gap), D65 (= D67), M66 (≠ V68), N92 (= N93), A93 (= A94), G94 (= G95), L115 (≠ T116), I143 (= I143), S145 (= S145), Y158 (= Y158), K162 (≠ R162), G189 (= G189), M191 (≠ F191), T193 (= T193), N195 (≠ K197)
3o03A Quaternary complex structure of gluconate 5-dehydrogenase from streptococcus suis type 2 (see paper)
36% identity, 91% coverage: 6:250/268 of query aligns to 7:246/254 of 3o03A
- active site: G22 (= G21), S147 (= S145), V157 (≠ L155), Y160 (= Y158), K164 (≠ R162)
- binding calcium ion: S147 (= S145), M148 (≠ V146), P190 (= P188)
- binding D-gluconic acid: I99 (≠ N97), R101 (= R99), S147 (= S145), M149 (≠ T147), R154 (≠ Y152), Y160 (= Y158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G17), Y21 (≠ R20), G22 (= G21), I23 (≠ L22), D42 (≠ S41), I43 (≠ R42), L47 (≠ D46), D68 (= D67), V69 (= V68), N95 (= N93), A96 (= A94), G97 (= G95), I145 (= I143), Y160 (= Y158), K164 (≠ R162), P190 (= P188)
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)
36% identity, 93% coverage: 3:250/268 of query aligns to 1:244/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G17), S17 (= S19), R18 (= R20), I20 (≠ L22), T40 (≠ R42), N62 (≠ D67), V63 (= V68), N89 (= N93), A90 (= A94), I92 (≠ C96), V139 (≠ I143), S141 (= S145), Y154 (= Y158), K158 (≠ R162), P184 (= P188), G185 (= G189), I187 (≠ F191), T189 (= T193), M191 (≠ Q195)
3uf0A Crystal structure of a putative NAD(p) dependent gluconate 5- dehydrogenase from beutenbergia cavernae(efi target efi-502044) with bound NADP (low occupancy)
38% identity, 91% coverage: 6:249/268 of query aligns to 3:245/249 of 3uf0A
- active site: G18 (= G21), S141 (= S145), V151 (≠ L155), Y154 (= Y158), K158 (≠ R162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G17), S17 (≠ R20), G18 (= G21), I19 (≠ L22), R39 (= R42), D63 (= D67), L64 (≠ V68), N89 (= N93), G91 (= G95), I92 (≠ C96), I139 (= I143), A140 (≠ G144), S141 (= S145), Y154 (= Y158), K158 (≠ R162), P184 (= P188), G185 (= G189), V187 (≠ F191), T189 (= T193), N191 (≠ Q195), T192 (≠ N196)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
36% identity, 91% coverage: 6:250/268 of query aligns to 1:241/244 of 6t77A
- active site: G16 (= G21), S138 (= S145), Y151 (= Y158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G17), S14 (= S19), R15 (= R20), T37 (≠ R42), L58 (= L66), N59 (≠ D67), V60 (= V68), A87 (= A94), G88 (= G95), I89 (≠ C96)
7x5jC Acp-dependent oxoacyl reductase
36% identity, 91% coverage: 8:250/268 of query aligns to 2:251/256 of 7x5jC
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G17), S13 (= S19), G15 (= G21), L16 (= L22), N36 (≠ S41), R37 (= R42), N38 (≠ H43), D62 (= D67), V63 (= V68), N89 (= N93), A90 (= A94), A91 (≠ G95), V114 (≠ T116), I141 (= I143), Y156 (= Y158), K160 (≠ R162), L186 (≠ P188), G187 (= G189), V188 (≠ W190), R194 (≠ A194), S197 (≠ K197), S198 (≠ V198)
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
36% identity, 91% coverage: 8:250/268 of query aligns to 3:248/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G17), Q15 (≠ R20), G16 (= G21), I17 (≠ L22), D36 (≠ S41), V63 (= V68), N89 (= N93), A91 (≠ G95), S94 (≠ V98), I142 (= I143), S143 (≠ G144), S144 (= S145), Y157 (= Y158), K161 (≠ R162), P187 (= P188), H188 (≠ G189), I190 (≠ F191), I194 (≠ Q195)
C1DMX5 L-rhamnose 1-dehydrogenase (NAD(P)(+)); RhaDH; AvLRA1; EC 1.1.1.378 from Azotobacter vinelandii (strain DJ / ATCC BAA-1303) (see paper)
38% identity, 91% coverage: 8:250/268 of query aligns to 3:251/256 of C1DMX5
- G12 (= G17) binding NADP(+)
- S14 (= S19) binding NADP(+)
- R15 (= R20) binding NADP(+); mutation to T: Increases specificity toward NAD(+). Shows a strong decrease in catalytic efficiency with NADP(+).
- I17 (≠ L22) binding NADP(+)
- S37 (≠ R42) binding NADP(+); mutation to H: Increases specificity toward NAD(+). Shows a strong decrease in catalytic efficiency with NADP(+) and an increase in catalytic efficiency with NAD(+).
- D66 (= D67) binding NADP(+)
- A67 (≠ V68) binding NADP(+)
- N93 (= N93) binding NADP(+)
- F99 (≠ R99) mutation F->A,Y: Shows a strong decrease in catalytic efficiency with L-rhamnose, L-lyxose and L-mannose.
- S146 (= S145) binding beta-L-rhamnose
- S148 (≠ T147) binding beta-L-rhamnose
- Q156 (≠ L155) binding beta-L-rhamnose; mutation to A: Almost loss of activity with L-rhamnose as substrate.
- Y159 (= Y158) binding beta-L-rhamnose; binding NADP(+)
- K163 (≠ R162) binding NADP(+)
- T191 (≠ W190) binding beta-L-rhamnose; mutation to F: Retains 4% of wild-type activity with L-rhamnose as substrate.
- I192 (≠ F191) binding NADP(+)
- I196 (≠ Q195) mutation to A: Shows a strong decrease in catalytic efficiency with L-rhamnose as substrate, but does not affect catalytic efficiency with L-lyxose and L-mannose.
- N197 (= N196) binding beta-L-rhamnose
- D200 (≠ L199) mutation to A: Retains 16% of wild-type activity with L-rhamnose as substrate.; mutation to H: Retains 22% of wild-type activity with L-rhamnose as substrate.
7do7A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NAD and l-rhamnose bound-form) (see paper)
38% identity, 91% coverage: 8:250/268 of query aligns to 3:251/256 of 7do7A
- active site: G16 (= G21), S146 (= S145), Y159 (= Y158)
- binding nicotinamide-adenine-dinucleotide: G12 (= G17), R15 (= R20), G16 (= G21), I17 (≠ L22), S37 (≠ R42), D66 (= D67), A67 (≠ V68), N93 (= N93), A94 (= A94), G95 (= G95), I96 (≠ C96), V144 (≠ I143), S145 (≠ G144), S146 (= S145), Y159 (= Y158), K163 (≠ R162), P189 (= P188), G190 (= G189), I192 (≠ F191), T194 (= T193), I196 (≠ Q195)
- binding beta-L-rhamnopyranose: F99 (≠ R99), S146 (= S145), S148 (≠ T147), Q156 (≠ L155), Y159 (= Y158), N197 (= N196), D235 (≠ E234), M236 (≠ A235), R238 (= R237)
7b81A Crystal structure of azotobacter vinelandii l-rhamnose 1-dehydrogenase (NAD bound-form) (see paper)
38% identity, 91% coverage: 8:250/268 of query aligns to 3:251/256 of 7b81A
- active site: G16 (= G21), S146 (= S145), Y159 (= Y158)
- binding nicotinamide-adenine-dinucleotide: G12 (= G17), S14 (= S19), R15 (= R20), I17 (≠ L22), D66 (= D67), A67 (≠ V68), N93 (= N93), A94 (= A94), G95 (= G95), I96 (≠ C96), T116 (= T116), V144 (≠ I143), S146 (= S145), Y159 (= Y158), K163 (≠ R162), P189 (= P188), G190 (= G189), I192 (≠ F191), T194 (= T193), I196 (≠ Q195)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
35% identity, 93% coverage: 3:250/268 of query aligns to 1:240/243 of 4i08A
- active site: G19 (= G21), N113 (= N117), S141 (= S145), Q151 (≠ L155), Y154 (= Y158), K158 (≠ R162)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G17), S17 (= S19), R18 (= R20), I20 (≠ L22), T40 (≠ R42), N62 (≠ D67), V63 (= V68), N89 (= N93), A90 (= A94), G140 (= G144), S141 (= S145), Y154 (= Y158), K158 (≠ R162), P184 (= P188), G185 (= G189), T189 (= T193)
P0AEK2 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Escherichia coli (strain K12) (see 2 papers)
35% identity, 91% coverage: 6:250/268 of query aligns to 1:241/244 of P0AEK2
- GASR 12:15 (= GASR 17:20) binding NADP(+)
- T37 (≠ R42) binding NADP(+)
- NV 59:60 (≠ DV 67:68) binding NADP(+)
- N86 (= N93) binding NADP(+)
- Y151 (= Y158) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YGASR 158:162) binding NADP(+)
- A154 (≠ S161) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (≠ R162) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ F191) binding NADP(+)
- E233 (≠ Q242) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
35% identity, 90% coverage: 10:250/268 of query aligns to 4:240/243 of 7emgB
P0A2C9 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
35% identity, 91% coverage: 6:250/268 of query aligns to 1:241/244 of P0A2C9
- M125 (= M132) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A232) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S233) mutation to F: Distorts the local conformation and prevent stacking around Phe-221. The S224F mutation would additionally disrupt the hydrogen bond formed between Ser-224 and Glu-226.
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
35% identity, 91% coverage: 7:250/268 of query aligns to 1:240/243 of 1q7bA