SitesBLAST
Comparing WP_086508208.1 NCBI__GCF_002151265.1:WP_086508208.1 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)
5jydB Crystal structure of a putative short chain dehydrogenase from burkholderia cenocepacia
64% identity, 84% coverage: 54:340/341 of query aligns to 2:288/292 of 5jydB
- active site: G58 (= G110), S184 (= S236), L194 (= L246), Y197 (= Y249), K201 (= K253), P242 (≠ Q294)
- binding magnesium ion: D56 (= D108), S57 (= S109), E82 (= E134)
- binding nicotinamide-adenine-dinucleotide: G54 (= G106), D56 (= D108), S57 (= S109), G58 (= G110), I59 (= I111), L79 (= L131), E82 (= E134), D106 (= D158), I107 (= I159), N133 (= N185), A134 (= A186), A135 (= A187), T182 (≠ V234), S184 (= S236), Y197 (= Y249), K201 (= K253), P227 (= P279), G228 (= G280), P229 (= P281), Y230 (≠ F282), T232 (= T284), L234 (= L286), Q235 (= Q287)
3r3sA Structure of the ygha oxidoreductase from salmonella enterica
54% identity, 84% coverage: 53:340/341 of query aligns to 1:288/292 of 3r3sA
- active site: G58 (= G110), S184 (= S236), L194 (= L246), Y197 (= Y249), K201 (= K253), Q242 (= Q294)
- binding magnesium ion: D56 (= D108), S57 (= S109), E82 (= E134)
- binding nicotinamide-adenine-dinucleotide: D56 (= D108), S57 (= S109), G58 (= G110), I59 (= I111), L79 (= L131), E82 (= E134), D106 (= D158), L107 (≠ I159), V133 (≠ N185), A134 (= A186), G135 (≠ A187), S184 (= S236), Y197 (= Y249), K201 (= K253), P227 (= P279), G228 (= G280), I230 (≠ F282), T232 (= T284), L234 (= L286), Q235 (= Q287)
P0AG84 Uncharacterized oxidoreductase YghA; EC 1.-.-.- from Escherichia coli (strain K12) (see paper)
52% identity, 85% coverage: 51:340/341 of query aligns to 1:290/294 of P0AG84
- K39 (≠ E89) modified: N6-acetyllysine
3ijrF 2.05 angstrom resolution crystal structure of a short chain dehydrogenase from bacillus anthracis str. 'Ames ancestor' in complex with NAD+
46% identity, 81% coverage: 66:341/341 of query aligns to 12:286/290 of 3ijrF
- active site: G57 (= G110), S182 (= S236), L192 (= L246), Y195 (= Y249), K199 (= K253), K240 (≠ Q294)
- binding magnesium ion: D55 (= D108), S56 (= S109), E80 (= E134)
- binding nicotinamide-adenine-dinucleotide: P21 (= P74), D55 (= D108), S56 (= S109), G57 (= G110), I58 (= I111), Y77 (= Y130), L78 (= L131), E80 (= E134), G103 (= G157), D104 (= D158), L105 (≠ I159), N131 (= N185), V132 (≠ A186), A133 (= A187), Q134 (≠ R188), I155 (≠ T209), T180 (≠ V234), S182 (= S236), Y195 (= Y249), K199 (= K253), P225 (= P279), G226 (= G280), P227 (= P281), I228 (≠ F282), T230 (= T284), L232 (= L286)
3i3oA 2.06 angstrom resolution crystal structure of a short chain dehydrogenase from bacillus anthracis str. 'Ames ancestor' in complex with NAD-acetone
46% identity, 81% coverage: 66:341/341 of query aligns to 4:278/282 of 3i3oA
- active site: G49 (= G110), S174 (= S236), L184 (= L246), Y187 (= Y249), K191 (= K253), K232 (≠ Q294)
- binding magnesium ion: D47 (= D108), S48 (= S109), E72 (= E134)
- binding nicotinamide adenine dinucleotide acetone adduct: G45 (= G106), D47 (= D108), S48 (= S109), G49 (= G110), I50 (= I111), Y69 (= Y130), L70 (= L131), E72 (= E134), G95 (= G157), D96 (= D158), L97 (≠ I159), N123 (= N185), V124 (≠ A186), A125 (= A187), Q126 (≠ R188), Q127 (= Q189), I147 (≠ T209), T172 (≠ V234), S174 (= S236), Y187 (= Y249), K191 (= K253), P217 (= P279), G218 (= G280), I220 (≠ F282), T222 (= T284), L224 (= L286)
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
36% identity, 73% coverage: 91:340/341 of query aligns to 3:251/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G106), S20 (≠ D108), K21 (≠ S109), G22 (= G110), I23 (= I111), A43 (≠ L131), S44 (≠ E132), S45 (≠ E134), G68 (= G157), D69 (= D158), V70 (≠ I159), N96 (= N185), S97 (≠ A186), G98 (≠ A187), Y100 (≠ Q189), I144 (≠ V234), S146 (= S236), Y159 (= Y249), K163 (= K253), P189 (= P279), G190 (= G280), M191 (≠ P281), I192 (≠ F282), T194 (= T284), G196 (≠ L286), T197 (≠ Q287)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S236), Y159 (= Y249), M191 (≠ P281), I202 (≠ Q292)
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, 72% coverage: 97:340/341 of query aligns to 30:273/278 of Q9BTZ2
- S176 (≠ P243) 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 (≠ L246) 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 (= T262) 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, 72% coverage: 97:340/341 of query aligns to 6:249/254 of 3o4rA
- active site: G19 (= G110), S145 (= S236), F155 (≠ L246), Y158 (= Y249), K162 (= K253), K203 (≠ Q294)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G106), T17 (≠ D108), D18 (≠ S109), G19 (= G110), I20 (= I111), S39 (≠ Y130), R40 (≠ L131), K41 (≠ E132), N44 (≠ E135), H65 (= H166), V66 (vs. gap), N92 (= N185), A94 (= A187), S145 (= S236), Y158 (= Y249), K162 (= K253), P188 (= P279), G189 (= G280), L190 (≠ P281), I191 (≠ F282), T193 (= T284), F195 (≠ L286), S196 (≠ Q287)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
34% identity, 72% coverage: 97:340/341 of query aligns to 5:249/261 of P40288
- 11:35 (vs. 103:127, 44% identical) binding
- E96 (≠ Q189) mutation E->A,G,K: Heat stable.
- D108 (≠ I202) mutation to N: Heat stable.
- V112 (≠ T206) mutation to A: Heat stable.
- E133 (= E227) mutation to K: Heat stable.
- V183 (= V274) mutation to I: Heat stable.
- P194 (= P285) mutation to Q: Heat stable.
- E210 (≠ G301) mutation to K: Heat stable.
- Y217 (≠ R308) mutation to H: Heat stable.
Sites not aligning to the query:
- 252 Q→L: Heat stable.
- 253 Y→C: Heat stable.
- 258 A→G: Heat stable.
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
34% identity, 72% coverage: 97:340/341 of query aligns to 5:249/261 of 1g6kA
- active site: G18 (= G110), S145 (= S236), Y158 (= Y249), K162 (= K253)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ S109), G18 (= G110), L19 (≠ I111), R39 (≠ E132), D65 (= D158), V66 (≠ I159), N92 (= N185), A93 (= A186), G94 (≠ A187), M143 (≠ V234), S145 (= S236), Y158 (= Y249), P188 (= P279), G189 (= G280), I191 (≠ F282), T193 (= T284)
8bcjB Crystal structure of short-chain dehydrogenase pa3128 from pseudomonas aeruginosa pao1 in complex with NADP+
34% identity, 70% coverage: 103:340/341 of query aligns to 8:249/250 of 8bcjB
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G106), S13 (≠ D108), R14 (≠ S109), G15 (= G110), I16 (= I111), L36 (= L131), R37 (≠ E132), N38 (≠ V133), A61 (≠ G157), D62 (= D158), V63 (≠ I159), N89 (= N185), A90 (= A186), G91 (≠ A187), T113 (= T209), V143 (= V234), S145 (= S236), Y159 (= Y249), K163 (= K253), P189 (= P279), G190 (= G280), I192 (≠ F282), T194 (= T284), I196 (≠ L286), H197 (≠ Q287)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
33% identity, 72% coverage: 96:340/341 of query aligns to 4:241/244 of 4nbuB
- active site: G18 (= G110), N111 (= N210), S139 (= S236), Q149 (≠ L246), Y152 (= Y249), K156 (= K253)
- binding acetoacetyl-coenzyme a: D93 (≠ E193), K98 (vs. gap), S139 (= S236), N146 (≠ P243), V147 (≠ A244), Q149 (≠ L246), Y152 (= Y249), F184 (≠ W283), M189 (≠ P288), K200 (≠ T299)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G106), N17 (≠ S109), G18 (= G110), I19 (= I111), D38 (≠ E132), F39 (≠ V133), V59 (≠ G157), D60 (= D158), V61 (≠ I159), N87 (= N185), A88 (= A186), G89 (≠ A187), I90 (≠ R188), T137 (≠ V234), S139 (= S236), Y152 (= Y249), K156 (= K253), P182 (= P279), F184 (≠ W283), T185 (= T284), T187 (≠ L286), M189 (≠ P288)
6j7uA Crystal structure of blue fluorescent protein from metagenomic library in complex with NADPH (see paper)
34% identity, 72% coverage: 97:340/341 of query aligns to 3:244/247 of 6j7uA
- active site: G16 (= G110), S142 (= S236), Y156 (= Y249)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G106), S14 (≠ D108), R15 (≠ S109), I17 (= I111), Y36 (= Y130), V37 (≠ L131), S38 (≠ E132), S41 (≠ E135), D65 (= D158), S66 (≠ I159), N92 (= N185), A93 (= A186), G94 (≠ A187), I115 (≠ T209), G141 (≠ A235), S142 (= S236), Y156 (= Y249), K160 (= K253), P186 (= P279), T191 (= T284), M193 (≠ L286), N194 (≠ Q287)
3ay6B Crystal structure of bacillus megaterium glucose dehydrogenase 4 a258f mutant in complex with nadh and d-glucose (see paper)
33% identity, 72% coverage: 97:340/341 of query aligns to 11:255/267 of 3ay6B
- active site: G24 (= G110), S151 (= S236), Y164 (= Y249), K168 (= K253)
- binding beta-D-glucopyranose: E102 (≠ Q189), S151 (= S236), H153 (≠ V238), W158 (≠ P243), Y164 (= Y249), N202 (≠ Q287), K205 (≠ Q292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G20 (= G106), T23 (≠ S109), G24 (= G110), L25 (≠ I111), Y45 (≠ L131), D71 (= D158), V72 (≠ I159), N98 (= N185), A99 (= A186), G100 (≠ A187), V101 (≠ R188), M149 (≠ V234), S151 (= S236), Y164 (= Y249), K168 (= K253), P194 (= P279), G195 (= G280), M197 (≠ F282), T199 (= T284), P200 (= P285), I201 (≠ L286), N202 (≠ Q287)
4iqgD Crystal structure of bpro0239 oxidoreductase from polaromonas sp. Js666 in NADP bound form
34% identity, 70% coverage: 103:340/341 of query aligns to 6:247/248 of 4iqgD
- active site: G13 (= G110), N112 (= N210), S143 (= S236), Y154 (≠ L246), Y157 (= Y249), K161 (= K253)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G106), S11 (≠ D108), R12 (≠ S109), G13 (= G110), I14 (= I111), N32 (= N129), A34 (≠ L131), S35 (≠ E132), N36 (≠ E134), A59 (≠ G157), D60 (= D158), V61 (≠ I159), N87 (= N185), A88 (= A186), G89 (≠ A187), V141 (= V234), S143 (= S236), Y157 (= Y249), K161 (= K253), P187 (= P279), G188 (= G280), I190 (≠ F282), T192 (= T284), I194 (≠ L286), H195 (≠ Q287)
6yq3AAA Monooxygenase (see paper)
35% identity, 72% coverage: 96:340/341 of query aligns to 2:248/252 of 6yq3AAA
- active site: G16 (= G110), S146 (= S236), Y159 (= Y249)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G106), S14 (≠ D108), R15 (≠ S109), G16 (= G110), I17 (= I111), H35 (≠ N129), A37 (≠ L131), S38 (≠ E132), N39 (≠ E134), L64 (≠ I159), N96 (= N185), A97 (= A186), A98 (= A187), V119 (≠ T209), I144 (≠ V234), Y159 (= Y249), K163 (= K253), P189 (= P279), G190 (= G280), I191 (≠ L286), T192 (≠ Q287), N194 (≠ S289)
- binding (3~{R})-8-methoxy-3-methyl-3,6-bis(oxidanyl)-2,4-dihydrobenzo[a]anthracene-1,7,12-trione: S146 (= S236), G147 (≠ M237), L148 (≠ V238), Q156 (≠ L246), Y159 (= Y249), I191 (≠ L286)
Sites not aligning to the query:
6ypzAAA Monooxygenase (see paper)
35% identity, 72% coverage: 96:340/341 of query aligns to 2:250/253 of 6ypzAAA
- active site: G16 (= G110), S148 (= S236), Y161 (= Y249)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G106), S14 (≠ D108), R15 (≠ S109), G16 (= G110), I17 (= I111), H35 (≠ N129), A37 (≠ L131), S38 (≠ E132), N39 (≠ E134), L64 (≠ I159), N96 (= N185), A97 (= A186), A98 (= A187), T100 (≠ Q190), I146 (≠ V234), S147 (≠ A235), S148 (= S236), Y161 (= Y249), K165 (= K253), P191 (= P279), G192 (= G280), I193 (≠ L286), T194 (≠ Q287), N196 (≠ S289)
6yq0AAA Monooxygenase (see paper)
35% identity, 72% coverage: 96:340/341 of query aligns to 2:250/254 of 6yq0AAA
- active site: G16 (= G110), S148 (= S236), Y161 (= Y249)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G106), S14 (≠ D108), R15 (≠ S109), G16 (= G110), I17 (= I111), H35 (≠ N129), A37 (≠ L131), S38 (≠ E132), N39 (≠ E134), L64 (≠ I159), N96 (= N185), A97 (= A186), A98 (= A187), T100 (≠ Q190), R117 (≠ D205), I146 (≠ V234), S147 (≠ A235), S148 (= S236), Y161 (= Y249), K165 (= K253), P191 (= P279), G192 (= G280), I193 (≠ L286), T194 (≠ Q287), N196 (≠ S289)
- binding (3~{R})-8-methoxy-3-methyl-3-oxidanyl-2,4-dihydrobenzo[a]anthracene-1,7,12-trione: T100 (≠ Q190), G101 (≠ W191), S148 (= S236), G149 (≠ M237), L150 (≠ V238), C153 (≠ D241), Q158 (≠ L246), Y161 (= Y249), G192 (= G280), I193 (≠ L286)
Sites not aligning to the query:
5u2wA Crystal structure of a short chain dehydrogenase from burkholderia cenocepacia j2315 in complex with NADP
40% identity, 57% coverage: 96:291/341 of query aligns to 3:197/246 of 5u2wA
- active site: G17 (= G110), S141 (= S236), M152 (≠ L246), Y155 (= Y249), K159 (= K253)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G106), S15 (≠ D108), R16 (≠ S109), G17 (= G110), I18 (= I111), Y37 (= Y130), E38 (= E132), K39 (≠ V133), S40 (≠ E134), A63 (≠ G157), D64 (= D158), S65 (≠ I159), N91 (= N185), A92 (= A186), G93 (≠ A187), T139 (≠ V234), Y155 (= Y249), K159 (= K253), P185 (= P279), G186 (= G280), T188 (≠ F282), T190 (= T284), M192 (≠ L286), N193 (≠ Q287)
3a28C Crystal structure of l-2,3-butanediol dehydrogenase (see paper)
32% identity, 71% coverage: 100:340/341 of query aligns to 2:253/257 of 3a28C
- active site: G12 (= G110), S140 (≠ A235), Y153 (= Y249), K157 (= K253), L198 (= L286)
- binding nicotinamide-adenine-dinucleotide: G8 (= G106), Q11 (≠ S109), I13 (= I111), D32 (≠ Y130), L33 (= L131), Q36 (≠ E134), L59 (≠ G157), D60 (= D158), V61 (≠ I159), N87 (= N185), S140 (≠ A235), Y153 (= Y249), K157 (= K253), P183 (= P279), V186 (≠ F282), T188 (= T284), M190 (vs. gap), W191 (vs. gap)
Query Sequence
>WP_086508208.1 NCBI__GCF_002151265.1:WP_086508208.1
MSSDHPHDPTRRKFVGGLATGMAAAVAGPAFAQQNGGNQASAQGSPEESPLTQMQDPREQ
FPRPPFPEQPQEWPGLAGEMEPRPDHGEESYHGSGRLVGRKALITGGDSGIGRAAAIAYA
REGADVAINYLEVEEPDAREVIELIEAEGRTAVAIPGDIRDEAFCHELVETAVERLGGLD
ILVNNAARQQWAESIMDVSTEIFDDTMKTNLYAMFWITKAALPHMEEGASIINVASMVAE
DPPAILLEYNMTKAAIVNFTKTLSKQVADQGIRVNTISPGPFWTPLQPSGGQPQEVVATF
GEDSLMGRPGQPVEIAGVFVLLASQESSFATGQNYSATGGA
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