Probable arginine biosynthesis bifunctional protein ArgJ; Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Belongs to the ArgJ family.

N-acetyl-gamma-glutamyl-phosphate reductase; Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Belongs to the NAGSA dehydrogenase family. Type 2 subfamily.

Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear.

ArgG protein; Argininosuccinate synthase, argG. Similar to SWISSPROT:ASSY_NITEU (81%). Argininosuccinate synthase is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate. InterPro (PF00764): Argininosuccinate synthase InterPro (TIGR00032): Argininosuccinate synthase; High confidence in function and specificity.

ArgB protein; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily.

ArgH protein; Argininosuccinate lyase (EC 4.3.2.1) (Arginosuccinase) (ASAL); High confidence in function and specificity.

Putative calcium binding protein,40% similarity to TrEMBL;O22845. Has 3 EFh|EF-hand, calcium binding motif;(SMART|SM00054):Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X [...]

Probable bifunctional PutA protein; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. Homology to dapD of E. coli of 74% (sprot|DAPD_ECOLI). Involved in biosynthesis of diaminopimelate and lysine from aspartate semialdehyde. Catalytic activity: succinyl-coa + (r)-2,3,4,5-tetrahydropyridine- 2,6-dicarboxylate + h(2)o = coa + (r)-2-(succinylamino)-6- oxoheptanedioate. InterPro: Bacterial transferase hexapeptide repeat (IPR001451) no signal peptide no TMH; High confidence in function and specificity.