SitesBLAST
Comparing GFF42 FitnessBrowser__Marino:GFF42 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)
5jy1A Crystal structure of putative short-chain dehydrogenase/reductase from burkholderia xenovorans lb400 bound to NAD
72% identity, 100% coverage: 1:266/266 of query aligns to 1:266/266 of 5jy1A
- active site: G17 (= G17), S143 (= S143), H153 (= H153), Y156 (= Y156), K160 (= K160), P201 (= P201)
- binding nicotinamide-adenine-dinucleotide: G13 (= G13), G17 (= G17), I18 (= I18), E37 (= E37), I38 (≠ L38), T62 (= T62), D63 (= D63), V64 (= V64), N90 (= N90), A91 (= A91), F92 (= F92), V93 (≠ A93), S143 (= S143), Y156 (= Y156), K160 (= K160), P186 (= P186), T187 (= T187), A188 (= A188), A191 (= A191)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
38% identity, 94% coverage: 1:251/266 of query aligns to 2:244/244 of 4nbuB
- active site: G18 (= G17), N111 (≠ T115), S139 (= S143), Q149 (≠ H153), Y152 (= Y156), K156 (= K160)
- binding acetoacetyl-coenzyme a: D93 (≠ N97), K98 (≠ E102), S139 (= S143), N146 (≠ A150), V147 (≠ W151), Q149 (≠ H153), Y152 (= Y156), F184 (≠ A191), M189 (≠ L196), K200 (≠ R206)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), N17 (≠ G16), G18 (= G17), I19 (= I18), D38 (≠ E37), F39 (≠ L38), V59 (≠ T62), D60 (= D63), V61 (= V64), N87 (= N90), A88 (= A91), G89 (≠ A93), I90 (≠ P94), T137 (≠ F141), S139 (= S143), Y152 (= Y156), K156 (= K160), P182 (= P186), F184 (≠ A191), T185 (= T192), T187 (≠ H194), M189 (≠ L196)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
36% identity, 92% coverage: 3:248/266 of query aligns to 2:244/248 of 6ixmC
- active site: G16 (= G17), S142 (= S143), Y155 (= Y156), K159 (= K160)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S15 (≠ G16), G16 (= G17), I17 (= I18), D36 (≠ E37), I37 (≠ L38), A61 (≠ T62), D62 (= D63), T63 (≠ V64), N89 (= N90), A90 (= A91), M140 (≠ F141), S142 (= S143), Y155 (= Y156), K159 (= K160), P185 (= P186), A186 (≠ T187), Y187 (≠ A188), I188 (≠ M189), L192 (≠ G202)
7wbcA Hydroxysteroid dehydrogenase wild-type complexed with NAD+ and (4s)-2- 2-methyl-2,4-pentanediol
38% identity, 92% coverage: 4:248/266 of query aligns to 3:245/250 of 7wbcA
- binding calcium ion: Y115 (≠ W117), P116 (≠ A118), H119 (≠ W121)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), G16 (= G17), I17 (= I18), D36 (≠ E37), V37 (≠ L38), A61 (≠ T62), D62 (= D63), I63 (≠ V64), N89 (= N90), F138 (= F141), S140 (= S143), Y153 (= Y156), K157 (= K160), P183 (= P186), F184 (≠ T187), A185 (= A188), T187 (≠ G190), G189 (≠ T192), V190 (≠ F193)
7do7A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NAD and l-rhamnose bound-form) (see paper)
38% identity, 94% coverage: 2:251/266 of query aligns to 1:253/256 of 7do7A
- active site: G16 (= G17), S146 (= S143), Y159 (= Y156)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), R15 (≠ G16), G16 (= G17), I17 (= I18), S37 (≠ L38), D66 (= D63), A67 (≠ V64), N93 (= N90), A94 (= A91), G95 (≠ A93), I96 (≠ P94), V144 (≠ F141), S145 (≠ Y142), S146 (= S143), Y159 (= Y156), K163 (= K160), P189 (= P186), G190 (≠ T187), I192 (≠ M189), T194 (≠ A191), I196 (≠ F193)
- binding beta-L-rhamnopyranose: F99 (≠ N97), S146 (= S143), S148 (≠ D145), Q156 (≠ H153), Y159 (= Y156), N197 (≠ H194), D235 (≠ E233), M236 (= M234), R238 (= R236)
7b81A Crystal structure of azotobacter vinelandii l-rhamnose 1-dehydrogenase (NAD bound-form) (see paper)
38% identity, 94% coverage: 2:251/266 of query aligns to 1:253/256 of 7b81A
- active site: G16 (= G17), S146 (= S143), Y159 (= Y156)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S14 (≠ G15), R15 (≠ G16), I17 (= I18), D66 (= D63), A67 (≠ V64), N93 (= N90), A94 (= A91), G95 (≠ A93), I96 (≠ P94), T116 (= T114), V144 (≠ F141), S146 (= S143), Y159 (= Y156), K163 (= K160), P189 (= P186), G190 (≠ T187), I192 (≠ M189), T194 (≠ A191), I196 (≠ F193)
7do6A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NADP bound-form) (see paper)
38% identity, 94% coverage: 2:251/266 of query aligns to 1:244/247 of 7do6A
- active site: G16 (= G17), S146 (= S143), Y159 (= Y156)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (≠ G15), R15 (≠ G16), G16 (= G17), I17 (= I18), H36 (≠ E37), S37 (≠ L38), G42 (= G43), D66 (= D63), A67 (≠ V64), N93 (= N90), A94 (= A91), G95 (≠ A93), I96 (≠ P94), T116 (= T114), S146 (= S143), Y159 (= Y156), K163 (= K160), I192 (≠ M189)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
36% identity, 92% coverage: 4:249/266 of query aligns to 5:251/254 of 4fn4A
- active site: G18 (= G17), S144 (= S143), Y157 (= Y156), K161 (= K160), S202 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: G14 (= G13), S17 (≠ G16), G18 (= G17), I19 (= I18), E38 (= E37), L39 (= L38), R43 (≠ L42), A63 (≠ T62), D64 (= D63), V65 (= V64), N91 (= N90), G93 (≠ F92), I94 (≠ A93), T142 (≠ F141), S144 (= S143), Y157 (= Y156), K161 (= K160), P187 (= P186), V190 (≠ M189), T192 (= T192), N193 (≠ F193), I194 (≠ H194)
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 92% coverage: 3:248/266 of query aligns to 2:244/248 of 4urfB
- active site: G16 (= G17), S142 (= S143), I152 (≠ H153), Y155 (= Y156), K159 (= K160)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (= L213), R211 (≠ G214), R212 (= R215)
- binding bicarbonate ion: I92 (vs. gap), G94 (vs. gap), R109 (≠ Q110), R179 (= R180), S228 (= S232)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), G14 (= G15), N15 (≠ G16), G16 (= G17), I17 (= I18), D36 (≠ E37), I37 (≠ L38), D62 (= D63), T63 (≠ V64), N89 (= N90), A90 (= A91), G91 (vs. gap), I140 (≠ F141), Y155 (= Y156), K159 (= K160), P185 (= P186), A186 (≠ T187), I188 (≠ M189), T190 (≠ A191)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 92% coverage: 3:248/266 of query aligns to 2:244/248 of 4urfA
- active site: G16 (= G17), S142 (= S143), I152 (≠ H153), Y155 (= Y156), K159 (= K160)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (vs. gap), S93 (vs. gap), G94 (vs. gap), E95 (vs. gap), T97 (≠ A93), E101 (= E102), T103 (= T104), Q106 (≠ M107), R109 (≠ Q110), S175 (≠ R176), G177 (≠ N178)
- binding magnesium ion: S237 (≠ E241), Y238 (≠ S242)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), G14 (= G15), N15 (≠ G16), G16 (= G17), I17 (= I18), D36 (≠ E37), I37 (≠ L38), W41 (≠ L42), D62 (= D63), T63 (≠ V64), N89 (= N90), A90 (= A91), G91 (vs. gap), I140 (≠ F141), Y155 (= Y156), K159 (= K160), P185 (= P186), I188 (≠ M189), T190 (≠ A191)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 92% coverage: 3:248/266 of query aligns to 2:244/248 of 4ureB
- active site: G16 (= G17), S142 (= S143), I152 (≠ H153), Y155 (= Y156), K159 (= K160)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ G16), G16 (= G17), I17 (= I18), N89 (= N90), G91 (vs. gap), Y155 (= Y156), P185 (= P186), A186 (≠ T187)
G9FRD7 7alpha-hydroxysteroid dehydrogenase; 7alpha-HSDH; NADP-dependent 7alpha-hydroxysteroid dehydrogenase; EC 1.1.1.- from Clostridium sardiniense (Clostridium absonum) (see 2 papers)
38% identity, 96% coverage: 1:255/266 of query aligns to 1:257/262 of G9FRD7
- SSTRGI 13:18 (≠ GAGGGI 13:18) binding
- R38 (≠ L38) binding ; mutation to D: Loss of catalytic activity.
- NA 63:64 (≠ DV 63:64) binding
- N90 (= N90) binding
- T145 (≠ S143) binding
- Y158 (= Y156) binding ; binding
- K162 (= K160) binding
- IGT---RA 191:195 (≠ MGATFHKL 189:196) binding
Sites not aligning to the query:
- 261:262 mutation Missing: 5-fold reduction in catalytic efficiency.
Q9C826 Xanthoxin dehydrogenase; Protein ABSCISIC ACID DEFICIENT 2; Protein GLUCOSE INSENSITIVE 1; Protein IMPAIRED SUCROSE INDUCTION 4; Protein SALOBRENO 3; Protein SALT RESISTANT 1; Protein SUGAR INSENSITIVE 4; Short-chain alcohol dehydrogenase ABA2; Short-chain dehydrogenase reductase 1; AtSDR1; Xanthoxin oxidase; EC 1.1.1.288 from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
38% identity, 92% coverage: 4:249/266 of query aligns to 18:274/285 of Q9C826
- G28 (≠ A14) mutation to R: In aba2-12/sre1-2; reduced absicic acid synthesis.
- A45 (= A31) mutation to V: In aba2-4/sis4-2; reduced absicic acid synthesis.
- R145 (≠ P128) mutation to C: In gin1-2; reduced absicic acid synthesis.
- G162 (≠ D145) mutation to R: In aba2-3/sis4-1; reduced absicic acid synthesis.
- S176 (≠ A159) mutation to F: In aba2-13/san3-1; reduced absicic acid synthesis.
- A236 (≠ R211) mutation to V: In isi4; reduced absicic acid synthesis.
- S264 (≠ T239) mutation to N: In aba2-1; reduced absicic acid synthesis.
5epoA The three-dimensional structure of clostridium absonum 7alpha- hydroxysteroid dehydrogenase (see paper)
38% identity, 95% coverage: 4:255/266 of query aligns to 3:256/261 of 5epoA
- active site: G16 (= G17), T144 (≠ S143), I152 (≠ W151), Y157 (= Y156), K161 (= K160), R193 (≠ K195)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S12 (≠ G13), T14 (≠ G15), R15 (≠ G16), G16 (= G17), I17 (= I18), R37 (≠ L38), F61 (≠ T62), N62 (≠ D63), N89 (= N90), Y90 (≠ F92), G91 (≠ A93), Y157 (= Y156), K161 (= K160), P187 (= P186), G188 (≠ T187), I190 (≠ M189), T192 (≠ A191), R193 (≠ K195), A194 (≠ L196), A195 (= A197)
- binding taurochenodeoxycholic acid: T93 (= T95), T144 (≠ S143), G146 (≠ D145), R154 (≠ H153), Y157 (= Y156), G188 (≠ T187), N198 (= N200), M199 (≠ P201), F203 (≠ E205)
3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
36% identity, 92% coverage: 4:248/266 of query aligns to 6:249/254 of 3o4rA
- active site: G19 (= G17), S145 (= S143), F155 (≠ H153), Y158 (= Y156), K162 (= K160), K203 (≠ P201)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G13), T17 (≠ G15), D18 (≠ G16), G19 (= G17), I20 (= I18), S39 (≠ E37), R40 (≠ L38), K41 (≠ S39), N44 (≠ L42), H65 (= H61), V66 (= V64), N92 (= N90), A94 (≠ F92), S145 (= S143), Y158 (= Y156), K162 (= K160), P188 (= P186), G189 (≠ T187), L190 (≠ A188), I191 (≠ M189), T193 (≠ A191), F195 (= F193), S196 (≠ H194)
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)
36% identity, 92% coverage: 4:248/266 of query aligns to 30:273/278 of Q9BTZ2
- S176 (≠ A150) 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 (≠ H153) 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 (≠ S169) 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.
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
35% identity, 93% coverage: 4:251/266 of query aligns to 2:244/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G13), M16 (≠ I18), D35 (≠ E37), I36 (≠ L38), I62 (≠ V64), N88 (= N90), G90 (≠ F92), I138 (≠ F141), S140 (= S143), Y152 (= Y156), K156 (= K160), I185 (≠ T192)
Q9KJF1 (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase subunit BbsD; (S,R)-2-(alpha-hydroxybenzyl)succinyl-CoA dehydrogenase subunit BbsD; EC 1.1.1.429 from Thauera aromatica (see 2 papers)
35% identity, 93% coverage: 4:251/266 of query aligns to 3:245/248 of Q9KJF1
- S15 (≠ G16) binding
- D36 (≠ E37) binding
- D62 (= D63) binding
- I63 (≠ V64) binding
- N89 (= N90) binding
- Y153 (= Y156) binding
- K157 (= K160) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
37% identity, 94% coverage: 1:250/266 of query aligns to 6:253/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G13), S20 (≠ G15), K21 (≠ G16), G22 (= G17), I23 (= I18), A43 (≠ L38), S44 (= S39), S45 (≠ E40), G68 (≠ T62), D69 (= D63), V70 (= V64), N96 (= N90), S97 (≠ A91), G98 (vs. gap), Y100 (vs. gap), I144 (≠ F141), S146 (= S143), Y159 (= Y156), K163 (= K160), P189 (= P186), G190 (≠ A188), M191 (= M189), I192 (≠ G190), T194 (= T192), G196 (vs. gap), T197 (≠ F193)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S143), Y159 (= Y156), M191 (= M189), I202 (≠ A198)
Q48436 Diacetyl reductase [(S)-acetoin forming]; Acetoin(diacetyl) reductase; AR; Meso-2,3-butanediol dehydrogenase; EC 1.1.1.304 from Klebsiella pneumoniae (see paper)
36% identity, 92% coverage: 6:249/266 of query aligns to 2:253/256 of Q48436
- 6:33 (vs. 10:37, 57% identical) binding
- D59 (= D63) binding
- K156 (= K160) binding
Query Sequence
>GFF42 FitnessBrowser__Marino:GFF42
MNLLENKVALITGAGGGIGEGVARYFVKQGAAVIIAELSEQLGEAVAADLRAQGGKALFC
HTDVSNKSSIENAVATAVDHFGSIDVLVNNAFAPTPNVKLEEKTDEMLTQTLNTTVWAAW
WAMKAAFPHMCERGGGSIVNFYSIDTEIGAWLHGDYNTAKSAILGLTRSAAAEWGRFNIR
ANAIAPTAMGATFHKLAAENPGFEERSAAMRPLGRCGEPEADIGPVVAFLASEMSRFVTG
ESIHVDGGLHLPGYNSRPAEVPVREY
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