SitesBLAST
Comparing 349937 FitnessBrowser__Btheta:349937 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)
Q9P7B4 NADP-dependent 3-hydroxy acid dehydrogenase; L-allo-threonine dehydrogenase; EC 1.1.1.381 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
46% identity, 100% coverage: 1:255/256 of query aligns to 4:259/259 of Q9P7B4
- S42 (= S38) modified: Phosphoserine
- T43 (≠ K39) modified: Phosphothreonine
3asvA The closed form of serine dehydrogenase complexed with NADP+ (see paper)
44% identity, 98% coverage: 5:254/256 of query aligns to 2:248/248 of 3asvA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G7 (= G10), T9 (≠ S12), G11 (= G14), F12 (≠ I15), R32 (= R35), R33 (≠ T36), D54 (= D61), V55 (= V62), N81 (= N88), G83 (= G90), I132 (= I139), S134 (= S141), Y147 (= Y154), K151 (= K158), G178 (= G185), V180 (= V187), T183 (= T189), E184 (≠ N190), F185 (= F191)
- binding phosphate ion: S134 (= S141), Y147 (= Y154), G178 (= G185), F185 (= F191)
6ixjA The crystal structure of sulfoacetaldehyde reductase from klebsiella oxytoca (see paper)
47% identity, 95% coverage: 3:245/256 of query aligns to 1:242/251 of 6ixjA
- binding 2-hydroxyethylsulfonic acid: S138 (= S141), Y145 (= Y148), Y151 (= Y154)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), T10 (≠ S12), S11 (= S13), G12 (= G14), F13 (≠ I15), R33 (= R35), R34 (≠ T36), D57 (= D61), V58 (= V62), N84 (= N88), A85 (= A89), G86 (= G90), T108 (= T112), I136 (= I139), S138 (= S141), Y151 (= Y154), K155 (= K158), P181 (= P184), G182 (= G185), A184 (≠ V187), T186 (= T189), E187 (≠ N190), F188 (= F191)
Q05016 NADP-dependent 3-hydroxy acid dehydrogenase; L-allo-threonine dehydrogenase; EC 1.1.1.-; EC 1.1.1.381 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
43% identity, 95% coverage: 4:246/256 of query aligns to 14:260/267 of Q05016
- N102 (= N88) binding
- Y168 (= Y154) binding
- K172 (= K158) binding
3rkuA Substrate fingerprint and the structure of NADP+ dependent serine dehydrogenase from saccharomyces cerevisiae complexed with NADP+
43% identity, 95% coverage: 4:246/256 of query aligns to 15:261/268 of 3rkuA
- active site: A107 (≠ V92), N128 (= N113), S156 (= S141), Y169 (= Y154), K173 (= K158), N214 (≠ D199)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G21 (= G10), S23 (= S12), G25 (= G14), I26 (= I15), R49 (= R35), R50 (≠ T36), D76 (= D61), I77 (≠ V62), N103 (= N88), A104 (= A89), G105 (= G90), K106 (≠ L91), S156 (= S141), Y169 (= Y154), K173 (= K158), P199 (= P184), G200 (= G185), V202 (= V187), T204 (= T189), E205 (≠ N190), F206 (= F191)
1xg5C Structure of human putative dehydrogenase mgc4172 in complex with nadp
37% identity, 94% coverage: 2:242/256 of query aligns to 9:255/257 of 1xg5C
- active site: S150 (= S141), Y165 (= Y154), K169 (= K158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G17 (= G10), S19 (= S12), G21 (= G14), I22 (= I15), A41 (= A34), R42 (= R35), T43 (= T36), D69 (= D61), L70 (≠ V62), N96 (= N88), G98 (= G90), I148 (= I139), S150 (= S141), Y165 (= Y154), K169 (= K158), G198 (= G185), V200 (= V187), T202 (= T189), F204 (= F191), K207 (≠ V194)
A0A1U8QWA2 Glycine betaine reductase ATRR; Nonribosomal peptide synthetase-like protein ATRR; EC 1.2.1.-; EC 1.1.1.- from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see paper)
35% identity, 94% coverage: 1:241/256 of query aligns to 1027:1265/1270 of A0A1U8QWA2
- G1036 (= G10) mutation to A: Compromises binding of the cosubstrate NADPH to aldehyde reductase domain R2. Decreases the aldehyde reductase activity by 4,000-fold; when associated with F-1178.
- Y1178 (= Y154) mutation to F: Does not substantially affect carboxylic acid reductase activity but results to a 150-fold loss of aldehyde reductase activity and the accumulation of glycine betaine aldehyde intermediate. Further decreases the aldehyde reductase activity by 4,000-fold; when associated with F-1178.
Sites not aligning to the query:
- 14:418 Adenylation (A) domain
- 643:937 Carboxylic acid reductase domain R1
- 812 Y→F: Abolishes overall carboxylic acid reductase activity but does nor affect aldehyde reductase activity.
- 1026:1256 Aldehyde reductase domain R2
3p19A Improved NADPH-dependent blue fluorescent protein (see paper)
36% identity, 94% coverage: 4:244/256 of query aligns to 3:237/239 of 3p19A
- active site: S132 (= S141), Y145 (= Y154), K149 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G10), S11 (= S12), S12 (= S13), G13 (= G14), I14 (= I15), A33 (= A34), R34 (= R35), R35 (≠ T36), D53 (= D61), V54 (= V62), N80 (= N88), A81 (= A89), G82 (= G90), I130 (= I139), S132 (= S141), Y145 (= Y154), K149 (= K158), P175 (= P184), A177 (≠ M186), V178 (= V187), T180 (= T189), E181 (≠ N190), L182 (≠ F191)
2japA Clavulanic acid dehydrogenase: structural and biochemical analysis of the final step in the biosynthesis of the beta- lactamase inhibitor clavulanic acid (see paper)
39% identity, 95% coverage: 1:244/256 of query aligns to 3:244/245 of 2japA
- active site: S140 (= S141), Y153 (= Y154), K157 (= K158), A198 (≠ G198)
- binding (2r,3z,5r)-3-(2-hydroxyethylidene)-7-oxo-4-oxa-1-azabicyclo[3.2.0]heptane-2-carboxylic acid: M93 (≠ V92), S140 (= S141), A142 (= A143), Y153 (= Y154), T185 (≠ M186), Y203 (≠ A203), R206 (≠ F206)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G10), S14 (= S12), S15 (= S13), G16 (= G14), I17 (= I15), A36 (= A34), R37 (= R35), R38 (≠ T36), L61 (≠ F60), D62 (= D61), V63 (= V62), N89 (= N88), A90 (= A89), G91 (= G90), T112 (= T112), M138 (≠ I139), S139 (≠ G140), S140 (= S141), Y153 (= Y154), K157 (= K158), P183 (= P184), T185 (≠ M186), T186 (≠ V187), T188 (= T189), E189 (≠ N190), L190 (≠ F191)
2jahC Biochemical and structural analysis of the clavulanic acid dehydeogenase (cad) from streptomyces clavuligerus (see paper)
39% identity, 95% coverage: 1:244/256 of query aligns to 4:245/246 of 2jahC
- active site: S141 (= S141), Y154 (= Y154), K158 (= K158), A199 (≠ G198)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G13 (= G10), S15 (= S12), S16 (= S13), G17 (= G14), I18 (= I15), A37 (= A34), R38 (= R35), R39 (≠ T36), D63 (= D61), V64 (= V62), N90 (= N88), A91 (= A89), G92 (= G90), T113 (= T112), M139 (≠ I139), S141 (= S141), Y154 (= Y154), K158 (= K158), P184 (= P184), G185 (= G185), T186 (≠ M186), T187 (≠ V187), T189 (= T189), E190 (≠ N190), L191 (≠ F191)
2ehdB Crystal structure analysis of oxidoreductase
35% identity, 93% coverage: 6:242/256 of query aligns to 7:213/213 of 2ehdB
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
32% identity, 77% coverage: 3:200/256 of query aligns to 2:199/250 of 2cfcA
- active site: G13 (= G14), S142 (= S141), Y155 (= Y154), K159 (= K158)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ Y148), R152 (≠ G151), Y155 (= Y154), W195 (≠ Y196), R196 (= R197)
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), S12 (= S13), G13 (= G14), N14 (≠ I15), D33 (≠ A34), L34 (≠ R35), A59 (≠ F60), D60 (= D61), V61 (= V62), N87 (= N88), A88 (= A89), G89 (= G90), I140 (= I139), P185 (= P184), G186 (= G185), M187 (= M186), I188 (≠ V187), T190 (= T189), P191 (≠ N190), M192 (≠ F191), T193 (= T192)
Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase; R-HPCDH; 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase; Aliphatic epoxide carboxylation component III; Epoxide carboxylase component III; RHPCDH1; EC 1.1.1.268 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 4 papers)
32% identity, 77% coverage: 3:200/256 of query aligns to 2:199/250 of Q56840
- SGN 12:14 (≠ SGI 13:15) binding
- D33 (≠ A34) binding
- DV 60:61 (= DV 61:62) binding
- N87 (= N88) binding
- S142 (= S141) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ G151) binding ; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- Y155 (= Y154) mutation Y->E,F: Loss of activity.
- K159 (= K158) mutation to A: Loss of activity.
- R179 (= R178) mutation to A: Loss of activity.
- IETPM 188:192 (≠ VETNF 187:191) binding
- WR 195:196 (≠ YR 196:197) binding
- R196 (= R197) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 203 R→A: Slight decrease in catalytic efficiency.
- 209 R→A: Does not affect catalytic efficiency.
4qecA Elxo with NADP bound (see paper)
27% identity, 92% coverage: 4:238/256 of query aligns to 3:239/248 of 4qecA
- active site: G13 (= G14), N111 (= N113), S139 (= S141), Y152 (= Y154), K156 (= K158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K12 (≠ S13), G13 (= G14), I14 (= I15), S33 (≠ A34), R34 (= R35), K38 (= K39), D59 (= D61), V60 (= V62), N86 (= N88), A87 (= A89), G88 (= G90), I137 (= I139), Y152 (= Y154), K156 (= K158), P182 (= P184), I185 (≠ V187)
4bmvC Short-chain dehydrogenase from sphingobium yanoikuyae in complex with NADPH
39% identity, 73% coverage: 6:191/256 of query aligns to 6:189/258 of 4bmvC
- active site: N111 (= N113), S139 (= S141), Y152 (= Y154), K156 (= K158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G10 (= G10), S12 (= S12), S13 (= S13), G14 (= G14), I15 (= I15), R35 (= R35), D36 (≠ T36), A60 (≠ F60), D61 (= D61), N87 (= N88), G89 (= G90), L110 (≠ T112), I137 (= I139), S139 (= S141), Y152 (= Y154), K156 (= K158), P182 (= P184), T185 (≠ V187), T187 (= T189), E188 (≠ N190), I189 (≠ F191)
Sites not aligning to the query:
3ai2A The crystal structure of l-sorbose reductase from gluconobacter frateurii complexed with NADPH (see paper)
33% identity, 74% coverage: 1:189/256 of query aligns to 5:192/263 of 3ai2A
- active site: G18 (= G14), S144 (= S141), Y157 (= Y154), K161 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G14 (= G10), S16 (= S12), S17 (= S13), G18 (= G14), I19 (= I15), A38 (= A34), R39 (= R35), Q40 (≠ T36), V64 (≠ F60), D65 (= D61), V66 (= V62), N92 (= N88), G94 (= G90), N142 (≠ I139), Y157 (= Y154), K161 (= K158), P187 (= P184), I190 (≠ V187), T192 (= T189)
Sites not aligning to the query:
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
31% identity, 74% coverage: 4:192/256 of query aligns to 2:189/239 of 3sj7A
- active site: G12 (= G14), S138 (= S141), Q148 (≠ G151), Y151 (= Y154), K155 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), S10 (= S12), R11 (≠ S13), I13 (= I15), N31 (= N33), Y32 (≠ A34), A33 (≠ R35), G34 (≠ T36), S35 (≠ V37), A58 (≠ F60), N59 (≠ D61), V60 (= V62), N86 (= N88), A87 (= A89), T109 (= T112), S138 (= S141), Y151 (= Y154), K155 (= K158), P181 (= P184), G182 (= G185)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
32% identity, 74% coverage: 4:192/256 of query aligns to 5:192/246 of 3osuA
3ai3C The crystal structure of l-sorbose reductase from gluconobacter frateurii complexed with NADPH and l-sorbose (see paper)
33% identity, 74% coverage: 1:189/256 of query aligns to 5:192/263 of 3ai3C
- active site: G18 (= G14), S144 (= S141), Y157 (= Y154), K161 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G14 (= G10), S16 (= S12), S17 (= S13), G18 (= G14), I19 (= I15), A38 (= A34), R39 (= R35), Q40 (≠ T36), R43 (≠ K39), D65 (= D61), V66 (= V62), N92 (= N88), G94 (= G90), N142 (≠ I139), Y157 (= Y154), K161 (= K158), P187 (= P184), G188 (= G185), I190 (≠ V187), T192 (= T189)
- binding L-sorbose: G96 (= G94), E154 (≠ G151), Y157 (= Y154)
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)
33% identity, 74% coverage: 1:189/256 of query aligns to 5:192/263 of 3ai3A
- active site: G18 (= G14), S144 (= S141), Y157 (= Y154), K161 (= K158)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G14 (= G10), S16 (= S12), S17 (= S13), G18 (= G14), I19 (= I15), A38 (= A34), R39 (= R35), Q40 (≠ T36), R43 (≠ K39), V64 (≠ F60), D65 (= D61), V66 (= V62), N92 (= N88), G94 (= G90), N142 (≠ I139), S144 (= S141), Y157 (= Y154), K161 (= K158), P187 (= P184), G188 (= G185), I190 (≠ V187), T192 (= T189)
- binding L-sorbose: G96 (= G94), S144 (= S141), L151 (≠ Y148), E154 (≠ G151), Y157 (= Y154), G188 (= G185)
Sites not aligning to the query:
Query Sequence
>349937 FitnessBrowser__Btheta:349937
MKAKIVFITGASSGIGEGCARKFAKEGWNLILNARTVSKLEELKAELEKEYGIQVYVLPF
DVRDRKQAAAALEALPEEWKSIDVLINNAGLVIGVDKEFEGSLDEWDIMIDTNIRGLLAM
TRLVVPGMVERGCGHIINIGSIAGDAAYPGGSVYCATKAAVKALSDGLRIDLVDTPLRVT
NIKPGMVETNFTVVRYRGDKQAADNFYKGIRPLTGDDIAETVYYAASAPAHIQIAEVLLM
PTYQATGTISYKKKAE
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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