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HAMAP annotation rule: MF_01107

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General rule information

Accession MF_01107
Dates 11-FEB-2003 (Created)
4-MAY-2009 (Last updated, Version 35)
Data class Protein
Predictors HAMAP; MF_01107; [distribution of match scores in UniProtKB];[seed alignment for MF_01107]


Propagated annotation

Identifier, protein and gene names
Identifier ARGD

case <OC:Enterobacteriaceae>
Protein name
RecName: Full=Acetylornithine/succinyldiaminopimelate aminotransferase;
Short=ACOAT;
Short=Succinyldiaminopimelate transferase;
Short=DapATase;
EC=2.6.1.11;
EC=2.6.1.17;
Gene name argD, dapC
end case


case <OC:Deinococci> or <OC:Pyrococcus> or <OC:Crenarchaeota>
Protein name
RecName: Full=Acetylornithine/acetyl-lysine aminotransferase;
Short=ACOAT;
EC=2.6.1.11;
EC=2.6.1.-;
Gene name argD, lysJ
end case


case not <OC:Enterobacteriaceae> and not <OC:Deinococci> and not <OC:Pyrococcus> and not <OC:Crenarchaeota>
Protein name
RecName: Full=Acetylornithine aminotransferase;
Short=ACOAT;
EC=2.6.1.11;
Gene name argD
end case

Comments

case <OC:Enterobacteriaceae> or <OC:Deinococci> or <OC:Pyrococcus> or <OC:Crenarchaeota>
FUNCTION: Involved in both the arginine and lysine biosynthetic pathways (By similarity).
end case


case <OC:Enterobacteriaceae>
CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
CATALYTIC ACTIVITY: N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate.
end case


case <OC:Deinococci> or <OC:Pyrococcus> or <OC:Crenarchaeota>
CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
CATALYTIC ACTIVITY: N(2)-acetyl-L-lysine + 2-oxoglutarate = N-acetyl-L-aminoadipate semialdehyde + L-glutamate.
end case


case not <OC:Enterobacteriaceae> and not <OC:Deinococci> and not <OC:Pyrococcus> and not <OC:Crenarchaeota>
CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
end case

COFACTOR: Binds 1 pyridoxal phosphate per subunit (By similarity).
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.

case <OC:Enterobacteriaceae>
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-diaminopimelate from tetrahydrodipicolinate (succinylase route): step 2/3.
end case


case <OC:Deinococci> or <OC:Pyrococcus> or <OC:Crenarchaeota>
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5.
end case

SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).

case not <OC:Enterobacteriaceae> and not <OC:Deinococci> and not <OC:Pyrococcus> and not <OC:Crenarchaeota>
MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.
end case

SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
Cross-references
Pfam PF00202; aminotran_3; 1;
TIGRFAMs TIGR00707; argD; 1;
PROSITE PS00600; AA_TRANSFER_CLASS_3; 1;
Keywords
Cytoplasm, Amino-acid biosynthesis, Arginine biosynthesis.

case <OC:Enterobacteriaceae> or <OC:Deinococci> or <OC:Pyrococcus> or <OC:Crenarchaeota>
Lysine biosynthesis.
end case

Transferase, Aminotransferase, Pyridoxal phosphate.
Gene Ontology
GO:0003992; Molecular function: acetylornithine transaminase activity.

case <OC:Enterobacteriaceae>
GO:0009016; Molecular function: succinyldiaminopimelate transaminase activity.
end case

GO:0006526; Biological process: arginine biosynthetic process.

case <OC:Enterobacteriaceae> or <OC:Deinococci> or <OC:Pyrococcus> or <OC:Crenarchaeota>
GO:0009085; Biological process: lysine biosynthetic process.
end case

GO:0005737; Cellular component: cytoplasm.
Features
From: ARGD_THET8 (Q5SHH5)
Key     From     To       Description   Condition   FTGroup
REGION (Optional)     113     114       Pyridoxal phosphate binding (By similarity)   G-T  
REGION     225     228       Pyridoxal phosphate binding (By similarity)   D-E-[IV]-Q  
BINDING     140     140       Pyridoxal phosphate; via carbonyl oxygen (By similarity)   F  
BINDING     143     143       N(2)-acetyl-L-ornithine (By similarity)   R  
BINDING     282     282       N(2)-acetyl-L-ornithine (By similarity)   [ST]  
BINDING     283     283       Pyridoxal phosphate (By similarity)   T  
MOD_RES     254     254       N6-(pyridoxal phosphate)lysine (By similarity)   K  


Additional information

Size range: 362-431 amino acids
Related UniRules: MF_01689 (OAT (supersedes the current rule)); MF_01173 (ASTC (supersedes the current rule))
Template: P18335 (ARGD_ECOLI); Q93R93 (ARGD_THET2); Q7SI94 (ARGD_SULSO): [Recover all]
Scope: Bacteria
Archaea
Fusion: Nter: None; Cter: None
Duplicate: in BORBR, BORPA, BORPE, BRAJA, PSESM
Plasmid encoded: None

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UniProtKB rule member sequences



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