SitesBLAST
Comparing 7026544 FitnessBrowser__ANA3:7026544 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)
3p19A Improved NADPH-dependent blue fluorescent protein (see paper)
68% identity, 98% coverage: 6:243/243 of query aligns to 2:239/239 of 3p19A
- active site: S132 (= S136), Y145 (= Y149), K149 (= K153)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G13), S11 (= S15), S12 (= S16), G13 (= G17), I14 (= I18), A33 (= A37), R34 (= R38), R35 (= R39), D53 (= D57), V54 (= V58), N80 (= N84), A81 (= A85), G82 (= G86), I130 (= I134), S132 (= S136), Y145 (= Y149), K149 (= K153), P175 (= P179), A177 (= A181), V178 (= V182), T180 (= T184), E181 (= E185), L182 (= L186)
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)
37% identity, 99% coverage: 4:243/243 of query aligns to 1023:1269/1270 of A0A1U8QWA2
- 1026:1256 (vs. 7:229, 37% identical) Aldehyde reductase domain R2
- G1036 (= G13) 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 (= Y149) 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.
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: 10:241/243 of query aligns to 9:244/245 of 2japA
- active site: S140 (= S136), Y153 (= Y149), K157 (= K153), A198 (= A194)
- binding (2r,3z,5r)-3-(2-hydroxyethylidene)-7-oxo-4-oxa-1-azabicyclo[3.2.0]heptane-2-carboxylic acid: M93 (= M88), S140 (= S136), A142 (= A138), Y153 (= Y149), T185 (≠ A181), Y203 (= Y199), R206 (≠ W202)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (= S15), S15 (= S16), G16 (= G17), I17 (= I18), A36 (= A37), R37 (= R38), R38 (= R39), L61 (≠ V56), D62 (= D57), V63 (= V58), N89 (= N84), A90 (= A85), G91 (= G86), T112 (≠ I107), M138 (≠ I134), S139 (= S135), S140 (= S136), Y153 (= Y149), K157 (= K153), P183 (= P179), T185 (≠ A181), T186 (≠ V182), T188 (= T184), E189 (= E185), L190 (= L186)
2jahC Biochemical and structural analysis of the clavulanic acid dehydeogenase (cad) from streptomyces clavuligerus (see paper)
39% identity, 95% coverage: 10:241/243 of query aligns to 10:245/246 of 2jahC
- active site: S141 (= S136), Y154 (= Y149), K158 (= K153), A199 (= A194)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G13 (= G13), S15 (= S15), S16 (= S16), G17 (= G17), I18 (= I18), A37 (= A37), R38 (= R38), R39 (= R39), D63 (= D57), V64 (= V58), N90 (= N84), A91 (= A85), G92 (= G86), T113 (≠ I107), M139 (≠ I134), S141 (= S136), Y154 (= Y149), K158 (= K153), P184 (= P179), G185 (= G180), T186 (≠ A181), T187 (≠ V182), T189 (= T184), E190 (= E185), L191 (= L186)
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)
35% identity, 96% coverage: 9:241/243 of query aligns to 16:258/267 of Q05016
- N102 (= N84) binding
- Y168 (= Y149) binding
- K172 (= K153) binding
3rkuA Substrate fingerprint and the structure of NADP+ dependent serine dehydrogenase from saccharomyces cerevisiae complexed with NADP+
35% identity, 96% coverage: 9:241/243 of query aligns to 17:259/268 of 3rkuA
- active site: A107 (≠ M88), N128 (= N108), S156 (= S136), Y169 (= Y149), K173 (= K153), N214 (≠ T191)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G21 (= G13), S23 (= S15), G25 (= G17), I26 (= I18), R49 (= R38), R50 (= R39), D76 (= D57), I77 (≠ V58), N103 (= N84), A104 (= A85), G105 (= G86), K106 (≠ V87), S156 (= S136), Y169 (= Y149), K173 (= K153), P199 (= P179), G200 (= G180), V202 (= V182), T204 (= T184), E205 (= E185), F206 (≠ L186)
2ehdB Crystal structure analysis of oxidoreductase
33% identity, 95% coverage: 9:239/243 of query aligns to 7:213/213 of 2ehdB
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)
32% identity, 99% coverage: 1:241/243 of query aligns to 1:248/259 of Q9P7B4
- S42 (≠ E41) modified: Phosphoserine
- T43 (≠ P42) modified: Phosphothreonine
Q8KES3 Sepiapterin reductase; SPR; cSR; EC 1.1.1.325 from Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum) (see 2 papers)
30% identity, 96% coverage: 6:239/243 of query aligns to 2:237/244 of Q8KES3
- 9:15 (vs. 13:19, 71% identical) binding
- SRT 40:42 (≠ ARR 37:39) binding
- DI 66:67 (≠ DV 57:58) binding
- N93 (= N84) binding
- F99 (≠ L90) binding ; mutation to A: Drastically reduces activity. Complete loss of activity; when associated with A-196.
- T116 (≠ I107) binding
- S145 (= S136) binding
- Y158 (= Y149) binding ; binding
- K162 (= K153) binding
- VYTPMW 191:196 (≠ VETELL 182:187) binding
- W196 (≠ L187) binding ; mutation to A: Drastically reduces activity. Complete loss of activity; when associated with A-99.
2bd0D Chlorobium tepidum sepiapterin reductase complexed with NADP and sepiapterin (see paper)
30% identity, 96% coverage: 6:239/243 of query aligns to 1:236/240 of 2bd0D
- active site: S144 (= S136), Y157 (= Y149), K161 (= K153)
- binding biopterin: F98 (≠ L90), S144 (= S136), Y157 (= Y149), M194 (≠ L186), W195 (≠ L187)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G13), K11 (≠ S16), I13 (= I18), S39 (≠ A37), R40 (= R38), T41 (≠ R39), D65 (= D57), I66 (≠ V58), N92 (= N84), G94 (= G86), V95 (= V87), T115 (≠ I107), S144 (= S136), Y157 (= Y149), K161 (= K153), P187 (= P179), A189 (= A181), V190 (= V182), T192 (= T184), P193 (≠ E185), M194 (≠ L186), W195 (≠ L187)
2bd0A Chlorobium tepidum sepiapterin reductase complexed with NADP and sepiapterin (see paper)
30% identity, 96% coverage: 6:239/243 of query aligns to 1:236/240 of 2bd0A
- active site: S144 (= S136), Y157 (= Y149), K161 (= K153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G13), K11 (≠ S16), G12 (= G17), I13 (= I18), R40 (= R38), T41 (≠ R39), D65 (= D57), I66 (≠ V58), N92 (= N84), A93 (= A85), G94 (= G86), V95 (= V87), T115 (≠ I107), I142 (= I134), S144 (= S136), K161 (= K153), P187 (= P179), A189 (= A181), V190 (= V182), T192 (= T184), P193 (≠ E185), M194 (≠ L186), W195 (≠ L187)
3rkrA Crystal structure of a metagenomic short-chain oxidoreductase (sdr) in complex with NADP (see paper)
37% identity, 73% coverage: 8:185/243 of query aligns to 7:191/221 of 3rkrA
- active site: G16 (= G17), S142 (= S136), Y155 (= Y149), K159 (= K153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), R15 (≠ S16), A36 (= A37), R37 (= R38), D38 (≠ R39), C61 (≠ V56), D62 (= D57), L63 (≠ V58), A90 (= A85), G91 (= G86), V92 (= V87), G93 (≠ M88)
6wprA Crystal structure of a putative 3-oxoacyl-acp reductase (fabg) with NADP(h) from acinetobacter baumannii (see paper)
30% identity, 89% coverage: 6:221/243 of query aligns to 5:221/244 of 6wprA
- active site: G16 (= G17), S138 (= S136), Y151 (= Y149)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (= S15), R15 (≠ S16), T37 (≠ V40), L58 (≠ V56), D59 (= D57), V60 (= V58), N86 (= N84), A87 (= A85), G88 (= G86), I89 (≠ V87), I136 (= I134), Y151 (= Y149), K155 (= K153), P181 (= P179)
6t62A Crystal structure of acinetobacter baumannii fabg in complex with NADPH at 1.8 a resolution (see paper)
30% identity, 89% coverage: 6:221/243 of query aligns to 5:221/244 of 6t62A
- active site: G16 (= G17), S138 (= S136), Y151 (= Y149)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (= S15), R15 (≠ S16), A36 (≠ R39), T37 (≠ V40), L58 (≠ V56), D59 (= D57), V60 (= V58), N86 (= N84), A87 (= A85), G88 (= G86), I89 (≠ V87), I136 (= I134), S137 (= S135), S138 (= S136), Y151 (= Y149), K155 (= K153), P181 (= P179), G182 (= G180), I184 (≠ V182), M188 (≠ L186)
4ituA Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) bound to s-hpc and nadh (see paper)
35% identity, 77% coverage: 36:221/243 of query aligns to 41:230/253 of 4ituA
- active site: N113 (= N108), S141 (= S136), Y154 (= Y149), K158 (= K153)
- binding 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonic acid: S141 (= S136), Y154 (= Y149), T186 (≠ A181), R209 (≠ Q200), Y213 (≠ V204)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D62 (= D57), V63 (= V58), N89 (= N84), V112 (≠ I107), F139 (≠ I134), S141 (= S136), Y154 (= Y149), K158 (= K153), P184 (= P179), T186 (≠ A181), V187 (= V182), T190 (vs. gap), M192 (vs. gap)
Sites not aligning to the query:
A7IQH5 2-(S)-hydroxypropyl-CoM dehydrogenase 3; S-HPCDH 3; 2-[(S)-2-hydroxypropylthio]ethanesulfonate dehydrogenase 3; Aliphatic epoxide carboxylation component IV; Epoxide carboxylase component IV; SHPCDH3; EC 1.1.1.269 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 2 papers)
35% identity, 77% coverage: 36:221/243 of query aligns to 43:232/255 of A7IQH5
- DV 64:65 (= DV 57:58) binding
- N91 (= N84) binding
- S143 (= S136) binding ; mutation to A: Retains very weak activity.
- Y156 (= Y149) binding ; mutation to A: Retains some activity but with more than 2200-fold decrease in catalytic efficiency.; mutation to F: Loss of activity.
- K160 (= K153) binding ; mutation to A: Loss of activity.
- T188 (≠ A181) binding
- VTSTG 189:193 (≠ VET-- 182:184) binding
- R211 (≠ Q200) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
- K214 (= K203) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
- Y215 (≠ V204) binding
Sites not aligning to the query:
5u9pB Crystal structure of a gluconate 5-dehydrogenase from burkholderia cenocepacia j2315 in complex with NADP and tartrate
33% identity, 79% coverage: 10:202/243 of query aligns to 20:215/261 of 5u9pB
- active site: G27 (= G17), S152 (= S136), Y165 (= Y149), K169 (= K153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G23 (= G13), R26 (≠ S16), G27 (= G17), I28 (= I18), R48 (vs. gap), D73 (= D57), V74 (= V58), N100 (= N84), A101 (= A85), I150 (= I134), Y165 (= Y149), K169 (= K153), P195 (= P179), F198 (≠ V182), T200 (= T184), L202 (= L186), N203 (≠ L187)
6ixjA The crystal structure of sulfoacetaldehyde reductase from klebsiella oxytoca (see paper)
33% identity, 96% coverage: 8:241/243 of query aligns to 3:241/251 of 6ixjA
- binding 2-hydroxyethylsulfonic acid: S138 (= S136), Y145 (≠ F143), Y151 (= Y149)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G13), T10 (≠ S15), S11 (= S16), G12 (= G17), F13 (≠ I18), R33 (= R38), R34 (= R39), D57 (= D57), V58 (= V58), N84 (= N84), A85 (= A85), G86 (= G86), T108 (≠ I107), I136 (= I134), S138 (= S136), Y151 (= Y149), K155 (= K153), P181 (= P179), G182 (= G180), A184 (≠ V182), T186 (= T184), E187 (= E185), F188 (≠ L186)
4gh5A Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) (see paper)
34% identity, 77% coverage: 36:221/243 of query aligns to 41:225/248 of 4gh5A
- active site: N113 (= N108), S141 (= S136), Y154 (= Y149), K158 (= K153)
- binding nicotinamide-adenine-dinucleotide: A61 (≠ V56), D62 (= D57), V63 (= V58), N89 (= N84), A90 (= A85), V112 (≠ I107), F139 (≠ I134), S141 (= S136), Y154 (= Y149), K158 (= K153), P184 (= P179), V187 (= V182), T190 (≠ E185), G191 (≠ L186), M192 (≠ L187)
Sites not aligning to the query:
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
33% identity, 79% coverage: 1:193/243 of query aligns to 3:198/246 of 3osuA
Query Sequence
>7026544 FitnessBrowser__ANA3:7026544
MTKPTQPLVVITGASSGIGAAIAKQFSAAGHPLLLLARRVEPMQALELPNSLAIGVDVTD
TDAIKAAINQAEAQFGPVGCLINNAGVMLLGQIDTQDPNEWSRMLNINVMGVLNGIHAVL
AGMKARKTGTIINISSVAGRKTFPNHAAYCATKFAVHALTENIREEVAMDDVRLITIAPG
AVETELLSHTTDDAIKAGYQDWKVQMGGVIAPENVAAAALFAWQQPQNVCVREIVLAPTR
QQP
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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