Q9Y7D1 · LOVD_ASPTE
- ProteinMonacolin J acid methylbutanoyltransferase
- GenelovD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids413 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Monacolin J acid methylbutanoyltransferase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) (PubMed:10334994, PubMed:12929390, PubMed:21495633).
The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units (PubMed:10334994, PubMed:10381407, PubMed:19900898, PubMed:22733743).
Dihydromonacolin L acid is released from lovB by the thioesterase lovG (PubMed:23653178).
Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid (PubMed:12929390, PubMed:21495633).
The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit (PubMed:19530726, PubMed:21069965).
Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin (PubMed:10334994, PubMed:17113998, PubMed:18988191, PubMed:19875080, PubMed:24727900).
LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro (PubMed:19875080).
LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates (PubMed:21069965).
The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units (PubMed:10334994, PubMed:10381407, PubMed:19900898, PubMed:22733743).
Dihydromonacolin L acid is released from lovB by the thioesterase lovG (PubMed:23653178).
Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid (PubMed:12929390, PubMed:21495633).
The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit (PubMed:19530726, PubMed:21069965).
Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin (PubMed:10334994, PubMed:17113998, PubMed:18988191, PubMed:19875080, PubMed:24727900).
LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro (PubMed:19875080).
LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates (PubMed:21069965).
Miscellaneous
Directed evolution toward higher catalytic activity with free diketides led to an enzyme with 1000-fold higher activity in simvastatin synthesis, due to numerous mutations that affect protein folding and promote optimal alignment of the residues that are important for substrate binding and catalysis.
Catalytic activity
- (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + monacolin J carboxylate = holo-[2-methylbutanoate polyketide synthase] + lovastatin carboxylate
Biotechnology
Lovastatin acts as a hypolipidemic agent that works as inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) which reduces HMG-CoA to mevalonate and is the key step in cholesterol biosynthesis (PubMed:6933445).
Lovastatin, simvastatin and related compounds are widely used to treat hypercholesteremia and reduce the risk of cardiovascular disease (PubMed:6933445).
Furthermore, statins such as lovastatin were found to be anticancer agents (PubMed:29236027, PubMed:29932104).
Lovastatin, simvastatin and related compounds are widely used to treat hypercholesteremia and reduce the risk of cardiovascular disease (PubMed:6933445).
Furthermore, statins such as lovastatin were found to be anticancer agents (PubMed:29236027, PubMed:29932104).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.78 mM | monacolin J | |||||
0.67 mM | alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate |
kcat is 0.62 min-1 for simvastatin synthesis.
Pathway
Polyketide biosynthesis; lovastatin biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 73 | monacolin J (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 76 | Acyl-ester intermediate | ||||
Sequence: S | ||||||
Binding site | 173 | monacolin J (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 188 | monacolin J (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 258 | monacolin J (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 366 | 2-methylbutanoate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 388 | monacolin J (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 390 | monacolin J (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | acyltransferase activity | |
Molecular Function | hydrolase activity | |
Molecular Function | polyketide synthase activity | |
Biological Process | antibiotic biosynthetic process | |
Biological Process | defense response to fungus | |
Biological Process | lovastatin biosynthetic process | |
Biological Process | polyketide biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMonacolin J acid methylbutanoyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionQ9Y7D1
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Loss of lovastatin biosynthesis.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 4 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: I → N | ||||||
Mutagenesis | 9 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: A → V | ||||||
Mutagenesis | 12 | Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with E-26; A-40; N-60; V-86; Y-161; T-190; S-275 and F-334. | ||||
Sequence: D → G | ||||||
Mutagenesis | 26 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: K → E | ||||||
Mutagenesis | 26 | Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; A-40; N-60; V-86; Y-161; T-190; S-275 and F-334. | ||||
Sequence: K → E | ||||||
Mutagenesis | 28 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: R → S | ||||||
Mutagenesis | 35 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: I → L | ||||||
Mutagenesis | 40 | Improves protein solubility upon overexpression in E.coli. Strongly improves protein solubility; when associated with N-60. Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; N-60; V-86; Y-161; T-190; S-275 and F-334. | ||||
Sequence: C → A | ||||||
Mutagenesis | 43 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: N → R | ||||||
Mutagenesis | 60 | Minor effect on protein solubility upon overexpression in E.coli. Strongly improves protein solubility; when associated with A-40. Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; V-86; Y-161; T-190; S-275 and F-334. | ||||
Sequence: C → A or N | ||||||
Mutagenesis | 76 | Abolishes enzyme activity. | ||||
Sequence: S → A or N | ||||||
Mutagenesis | 86 | Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; N-60; Y-161; T-190; S-275 and F-334. | ||||
Sequence: A → V | ||||||
Mutagenesis | 96 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: D → R | ||||||
Mutagenesis | 109 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96;. | ||||
Sequence: S → C | ||||||
Mutagenesis | 123 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: A → P | ||||||
Mutagenesis | 157 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: M → V | ||||||
Mutagenesis | 161 | Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; N-60; V-86; T-190; S-275 and F-334. | ||||
Sequence: H → Y | ||||||
Mutagenesis | 164 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: S → G | ||||||
Mutagenesis | 172 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; V-383; M-355; L-361; I-370; S-391 and K-404. | ||||
Sequence: S → N | ||||||
Mutagenesis | 174 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: L → F | ||||||
Mutagenesis | 178 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: A → L | ||||||
Mutagenesis | 190 | Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; N-60; V-86; Y-161; S-275 and F-334. | ||||
Sequence: A → T | ||||||
Mutagenesis | 191 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: N → G | ||||||
Mutagenesis | 192 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; M-241; S-247; K-250; T-256; H-261; S-275; G-297; V-383; M-355; L-361; I-370; S-391 and K-404. | ||||
Sequence: L → I | ||||||
Mutagenesis | 241 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: Q → M | ||||||
Mutagenesis | 247 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: A → S | ||||||
Mutagenesis | 250 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: R → K | ||||||
Mutagenesis | 256 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: S → T | ||||||
Mutagenesis | 261 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; S-275; G-297; V-383; M-355; L-361; I-370; S-391 and K-404. | ||||
Sequence: A → H | ||||||
Mutagenesis | 275 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: G → S | ||||||
Mutagenesis | 275 | Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; N-60; V-86; Y-161; T-190 and F-334. | ||||
Sequence: G → S | ||||||
Mutagenesis | 297 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; M-355; L-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: Q → G | ||||||
Mutagenesis | 334 | Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; N-60; V-86; Y-161; T-190 and S-275. | ||||
Sequence: V → F | ||||||
Mutagenesis | 355 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-361; I-370; V-383; S-391 and K-404. | ||||
Sequence: W → M | ||||||
Mutagenesis | 361 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; V-383; G-297; M-355; I-370; S-391 and K-404. | ||||
Sequence: L → M | ||||||
Mutagenesis | 370 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; M-361; V-383; S-391 and K-404. | ||||
Sequence: V → I | ||||||
Mutagenesis | 383 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; S-391 and K-404. | ||||
Sequence: A → V | ||||||
Mutagenesis | 391 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; M-361; I-370; V-383 and K-404. | ||||
Sequence: N → S | ||||||
Mutagenesis | 404 | Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; V-383; G-297; M-355; M-361; I-370; V-383 and S-391. | ||||
Sequence: H → K |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000430100 | 1-413 | Monacolin J acid methylbutanoyltransferase | |||
Sequence: MGSIIDAAAAADPVVLMETAFRKAVKSRQIPGAVIMARDCSGNLNYTRCFGARTVRRDECNQLPPLQVDTPCRLASATKLLTTIMALQCMERGLVDLDETVDRLLPDLSAMPVLEGFDDAGNARLRERRGKITLRHLLTHTSGLSYVFLHPLLREYMAQGHLQSAEKFGIQSRLAPPAVNDPGAEWIYGANLDWAGKLVERATGLDLEQYLQENICAPLGITDMTFKLQQRPDMLARRADQTHRNSADGRLRYDDSVYFRADGEECFGGQGVFSGPGSYMKVLHSLLKRDGLLLQPQTVDLMFQPALEPRLEEQMNQHMDASPHINYGGPMPMVLRRSFGLGGIIALEDLDGENWRRKGSLTFGGGPNIVWQIDPKAGLCTLAFFQLEPWNDPVCRDLTRTFEHAIYAQYQQG |
Interaction
Subunit
Interacts with LovF.
Structure
Sequence
- Sequence statusComplete
- Length413
- Mass (Da)46,037
- Last updated1999-11-01 v1
- Checksum731A140B6E609A24
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AH007774 EMBL· GenBank· DDBJ | AAD34555.1 EMBL· GenBank· DDBJ | Genomic DNA |