SitesBLAST
Comparing CCNA_03172 FitnessBrowser__Caulo:CCNA_03172 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)
3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
39% identity, 97% coverage: 6:251/254 of query aligns to 6:249/254 of 3o4rA
- active site: G19 (= G19), S145 (= S147), F155 (≠ I157), Y158 (= Y160), K162 (= K164), K203 (≠ P205)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G15), T17 (≠ S17), D18 (≠ R18), G19 (= G19), I20 (= I20), S39 (= S39), R40 (= R40), K41 (= K41), N44 (≠ P44), H65 (≠ N67), V66 (≠ I68), N92 (= N94), A94 (= A96), S145 (= S147), Y158 (= Y160), K162 (= K164), P188 (= P190), G189 (= G191), L190 (= L192), I191 (= I193), T193 (= T195), F195 (= F197), S196 (≠ A198)
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)
39% identity, 97% coverage: 6:251/254 of query aligns to 30:273/278 of Q9BTZ2
- S176 (≠ N154) 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 (≠ I157) 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 (≠ N173) 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.
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)
38% identity, 97% coverage: 6:251/254 of query aligns to 31:274/279 of Q8WNV7
- 37:61 (vs. 12:36, 56% identical) binding
- F177 (≠ N154) 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 (≠ I157) 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 (= Y160) active site, Proton acceptor
- K187 (= K164) binding
- N196 (= N173) 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)
38% identity, 97% coverage: 6:251/254 of query aligns to 3:246/251 of 2zatA
- active site: G16 (= G19), S142 (= S147), L152 (≠ I157), Y155 (= Y160), K159 (= K164), K200 (≠ P205)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A12 (≠ G15), T14 (≠ S17), D15 (≠ R18), G16 (= G19), I17 (= I20), S36 (= S39), R37 (= R40), K38 (= K41), N41 (≠ E47), H62 (≠ N67), N89 (= N94), A91 (= A96), V140 (≠ I145), S142 (= S147), Y155 (= Y160), K159 (= K164), P185 (= P190), G186 (= G191), I188 (= I193), T190 (= T195), F192 (= F197), S193 (≠ A198)
5ojiA Crystal structure of the dehydrogenase/reductase sdr family member 4 (dhrs4) from caenorhabditis elegans (see paper)
37% identity, 97% coverage: 6:251/254 of query aligns to 8:255/260 of 5ojiA
- active site: G21 (= G19), S148 (= S147), Y161 (= Y160), K165 (= K164)
- binding isatin: S148 (= S147), S150 (≠ G149), Y161 (= Y160), V193 (≠ L192), S199 (≠ A198), L202 (= L201)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A17 (≠ G15), T19 (≠ S17), I22 (= I20), S41 (= S39), R42 (= R40), N43 (≠ K41), N46 (≠ P44), I69 (= I68), N95 (= N94), H96 (≠ A95), G97 (≠ A96), N146 (≠ I145), S148 (= S147), Y161 (= Y160), K165 (= K164), G192 (= G191), I194 (= I193), T196 (= T195), M198 (≠ F197)
5ojgA Crystal structure of the dehydrogenase/reductase sdr family member 4 (dhrs4) from caenorhabditis elegans (see paper)
37% identity, 97% coverage: 6:251/254 of query aligns to 8:255/260 of 5ojgA
- active site: G21 (= G19), S148 (= S147), Y161 (= Y160), K165 (= K164)
- binding butane-2,3-dione: S148 (= S147), Y161 (= Y160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A17 (≠ G15), T19 (≠ S17), G21 (= G19), I22 (= I20), S41 (= S39), R42 (= R40), N43 (≠ K41), N46 (≠ P44), I69 (= I68), N95 (= N94), H96 (≠ A95), G97 (≠ A96), N146 (≠ I145), S148 (= S147), Y161 (= Y160), K165 (= K164), P191 (= P190), I194 (= I193), T196 (= T195), M198 (≠ F197)
1vl8B Crystal structure of gluconate 5-dehydrogenase (tm0441) from thermotoga maritima at 2.07 a resolution
35% identity, 99% coverage: 3:253/254 of query aligns to 1:250/252 of 1vl8B
- active site: G17 (= G19), S143 (≠ G150), I154 (= I157), Y157 (= Y160), K161 (= K164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G15), R16 (= R18), G17 (= G19), L18 (≠ I20), S37 (= S39), R38 (= R40), C63 (≠ A66), D64 (≠ N67), V65 (≠ I68), A91 (= A95), A92 (= A96), G93 (≠ S97), I94 (≠ N98), V114 (≠ N118), I141 (= I148), S143 (≠ G150), Y157 (= Y160), K161 (= K164), P187 (= P190), G188 (= G191), Y190 (≠ I193), T192 (= T195), M194 (≠ F197), T195 (≠ A198)
Q9S9W2 Short-chain dehydrogenase/reductase SDRA; Protein INDOLE-3-BUTYRIC ACID RESPONSE 1; Short-chain dehydrogenase/reductase A; EC 1.1.-.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 97% coverage: 6:251/254 of query aligns to 9:249/254 of Q9S9W2
- R43 (= R40) mutation to C: In ibr1-1; resistance to the inhibitory effect of intermediate levels of indole-3-butyric acid (IBA) on root elongation.
- S140 (= S141) mutation to F: In ibr1-8; resistance to the inhibitory effect of intermediate levels of indole-3-butyric acid (IBA) on root elongation.
1ahhA 7 alpha-hydroxysteroid dehydrogenase complexed with NAD+ (see paper)
40% identity, 97% coverage: 6:251/254 of query aligns to 9:249/253 of 1ahhA
- active site: G22 (= G19), S146 (= S147), M156 (≠ I157), Y159 (= Y160), K163 (= K164)
- binding nicotinamide-adenine-dinucleotide: G18 (= G15), A21 (≠ R18), D42 (≠ S39), I43 (≠ R40), C67 (≠ A66), D68 (≠ N67), I69 (= I68), N95 (= N94), G97 (≠ A96), T145 (≠ S146), Y159 (= Y160), K163 (= K164), P189 (= P190), G190 (= G191), I192 (= I193)
1ahiA 7 alpha-hydroxysteroid dehydrogenase complexed with nadh and 7-oxo glycochenodeoxycholic acid (see paper)
40% identity, 97% coverage: 6:251/254 of query aligns to 9:249/255 of 1ahiA
- active site: G22 (= G19), S146 (= S147), M156 (≠ I157), Y159 (= Y160), K163 (= K164)
- binding glycochenodeoxycholic acid: S146 (= S147), A148 (≠ G149), N151 (≠ R152), Y159 (= Y160), A196 (≠ F197), V200 (≠ L201)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G18 (= G15), A21 (≠ R18), G22 (= G19), I23 (= I20), D42 (≠ S39), I43 (≠ R40), D68 (≠ N67), I69 (= I68), N95 (= N94), Y159 (= Y160), K163 (= K164), P189 (= P190), G190 (= G191), I192 (= I193), T194 (= T195), A196 (≠ F197)
Sites not aligning to the query:
P0AET8 7alpha-hydroxysteroid dehydrogenase; 7alpha-HSDH; NAD-dependent 7alpha-hydroxysteroid dehydrogenase; EC 1.1.1.159 from Escherichia coli (strain K12) (see 2 papers)
40% identity, 97% coverage: 6:251/254 of query aligns to 9:249/255 of P0AET8
- I23 (= I20) binding
- DI 42:43 (≠ SR 39:40) binding
- DI 68:69 (≠ NI 67:68) binding
- N95 (= N94) binding
- G99 (vs. gap) binding
- S146 (= S147) binding ; mutation S->A,H: Reduction of the catalytic efficiency by over 65%. No effect on the affinity for cholate and NAD.
- N151 (≠ R152) binding
- Y159 (= Y160) binding ; binding ; mutation to F: Loss of activity.; mutation to H: Reduction of the catalytic efficiency by 87.7%. No effect on the affinity for cholate and NAD.
- K163 (= K164) binding ; mutation to I: Reduction of the catalytic efficiency by 95%. No effect on the affinity for cholate and NAD.; mutation to R: Reduction of the catalytic efficiency by 35%. No effect on the affinity for cholate and NAD.
- ILT 192:194 (≠ IKT 193:195) binding
7do7A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NAD and l-rhamnose bound-form) (see paper)
37% identity, 97% coverage: 6:251/254 of query aligns to 3:250/256 of 7do7A
- active site: G16 (= G19), S146 (= S147), Y159 (= Y160)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), R15 (= R18), G16 (= G19), I17 (= I20), S37 (≠ R40), D66 (≠ N67), A67 (≠ I68), N93 (= N94), A94 (= A95), G95 (≠ A96), I96 (≠ S97), V144 (≠ I145), S145 (= S146), S146 (= S147), Y159 (= Y160), K163 (= K164), P189 (= P190), G190 (= G191), I192 (= I193), T194 (= T195), I196 (≠ F197)
- binding beta-L-rhamnopyranose: F99 (≠ Y100), S146 (= S147), S148 (≠ G149), Q156 (≠ I157), Y159 (= Y160), N197 (≠ A198), D235 (≠ K236), M236 (≠ A237), R238 (≠ S239)
7b81A Crystal structure of azotobacter vinelandii l-rhamnose 1-dehydrogenase (NAD bound-form) (see paper)
37% identity, 97% coverage: 6:251/254 of query aligns to 3:250/256 of 7b81A
- active site: G16 (= G19), S146 (= S147), Y159 (= Y160)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), S14 (= S17), R15 (= R18), I17 (= I20), D66 (≠ N67), A67 (≠ I68), N93 (= N94), A94 (= A95), G95 (≠ A96), I96 (≠ S97), T116 (≠ N118), V144 (≠ I145), S146 (= S147), Y159 (= Y160), K163 (= K164), P189 (= P190), G190 (= G191), I192 (= I193), T194 (= T195), I196 (≠ F197)
7krmC Putative fabg bound to nadh from acinetobacter baumannii
35% identity, 98% coverage: 6:254/254 of query aligns to 3:243/244 of 7krmC
- active site: G18 (= G19), S140 (= S147), Y155 (= Y160)
- binding nicotinamide-adenine-dinucleotide: G12 (= G15), S15 (= S16), G18 (= G19), I19 (= I20), D38 (≠ S39), L39 (≠ R40), A60 (= A66), N61 (= N67), V62 (≠ I68), N88 (= N94), V111 (≠ N118), S140 (= S147), Y155 (= Y160), K159 (= K164), I188 (= I193), T190 (= T195)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
35% identity, 98% coverage: 4:251/254 of query aligns to 1:240/244 of 6t77A
- active site: G16 (= G19), S138 (= S147), Y151 (= Y160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G15), S14 (= S17), R15 (= R18), T37 (≠ R40), L58 (≠ I62), N59 (= N67), V60 (≠ I68), A87 (= A95), G88 (≠ A96), I89 (≠ S97)
5fffA Noroxomaritidine/norcraugsodine reductase in complex with NADP+ and piperonal (see paper)
35% identity, 100% coverage: 1:254/254 of query aligns to 1:255/257 of 5fffA
- active site: K206 (≠ P205)
- binding 1,3-benzodioxole-5-carbaldehyde: Y100 (≠ P99), H158 (≠ N154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G15), T20 (≠ S17), G22 (= G19), I23 (= I20), R43 (= R40), C67 (≠ A63), D68 (≠ N67), V69 (≠ I68), N96 (≠ A95), I146 (= I145), Y161 (= Y160), K165 (= K164), P191 (= P190), A193 (≠ L192), I194 (= I193), T196 (= T195), G198 (≠ F197), T199 (≠ A198)
5ff9B Noroxomaritidine/norcraugsodine reductase in complex with NADP+ and tyramine (see paper)
35% identity, 100% coverage: 1:254/254 of query aligns to 1:255/257 of 5ff9B
- active site: K206 (≠ P205)
- binding 4-(2-aminoethyl)phenol: Y100 (≠ P99), I155 (≠ L151), H158 (≠ N154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G15), T20 (≠ S17), K21 (≠ R18), I23 (= I20), S42 (= S39), R43 (= R40), C67 (≠ A63), D68 (≠ N67), V69 (≠ I68), N96 (≠ A95), I146 (= I145), S148 (= S147), Y161 (= Y160), K165 (= K164), P191 (= P190), A193 (≠ L192), I194 (= I193), T196 (= T195), G198 (≠ F197), T199 (≠ A198)
A0A1A9TAK5 Noroxomaritidine/norcraugsodine reductase; NorRed; EC 1.1.1.- from Narcissus pseudonarcissus (Daffodil) (see paper)
35% identity, 100% coverage: 1:254/254 of query aligns to 1:255/257 of A0A1A9TAK5
A7DY56 Tropinone reductase; EC 1.1.1.206; EC 1.1.1.236 from Cochlearia officinalis (Common scurvygrass) (see paper)
33% identity, 100% coverage: 2:254/254 of query aligns to 12:262/273 of A7DY56
- Y209 (≠ L201) mutation to S: Loss of tropinone or nortropinone reduction, but faster reduction of cyclohexanones.
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)
35% identity, 98% coverage: 3:251/254 of query aligns to 3:243/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G15), S17 (= S17), R18 (= R18), I20 (= I20), T40 (≠ R40), N62 (= N67), V63 (≠ I68), N89 (= N94), A90 (= A95), I92 (≠ S97), V139 (≠ I145), S141 (= S147), Y154 (= Y160), K158 (= K164), P184 (= P190), G185 (= G191), I187 (= I193), T189 (= T195), M191 (≠ F197)
Query Sequence
>CCNA_03172 FitnessBrowser__Caulo:CCNA_03172
MSLFDLTGKVAIITGSSRGIGKAIAERMAEHGAKVVISSRKAGPCEEVASELNAKHGAGT
AIAVPANIASKDELQNLVDETRKAFGKIDICVCNAASNPYYGPLAGIADDQFRKILDNNI
ISNHWLIGMVAPEMQARKDGSIIIISSIGGLRGNAIIGAYNISKAADFQLARNLAHEFGP
DNVRVNCIAPGLIKTDFAKALWDNPETLKRSTTAVPLRRIGEPDEIAGAAVYLASKAGSF
MTGQAMVVDGGATI
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