Reviewed, UniProtKB/Swiss-Prot Q9ZJ10 (ARGD_BACAM)

Names and origin

Protein names

Recommended name:
    Acetylornithine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11

Gene names

Name:

argD

Organism

Bacillus amyloliquefaciens

Taxonomic identifier

1390 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	229 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107
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. HAMAP MF_01107
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Miscellaneous	May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the fourth step in lysine biosynthesis. HAMAP MF_01107
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›229	›229	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112718
Regions
	Region	208 – 211	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	122	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	125	1	N(2)-acetyl-L-ornithine By similarity
Experimental info
	Non-terminal residue	229	1

Sequences

	Sequence		Length	Mass (Da)
	Q9ZJ10-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 8E109AE708229176	FASTA	229	24,779
	10 20 30 40 50 60 MSSLFQTYGR WDIDIKKAKG TYVEDQNGKT YLDFIQGIAV SNLGHCHEAV TEAVKKQLDS 70 80 90 100 110 120 VWHVSNLFQN SLQEQAAQKL AAHSAGDLVF FCNSGAEANE GAIKLARKAT GKTKIITFLQ 130 140 150 160 170 180 SFHGRTYAGM AATGQDKIKT GFGPMLGGFH YLPYNDPSAF KALGEEGDIA AVMLETVQGE 190 200 210 220 GGVNPASAEF LSAVQSFCKE KQALLIIDEI QTGIGRTGTR FAYQHFGLS

References

[1]	Kim H.K., Min K.H., Yamane K. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF001833 Genomic DNA. Translation: AAD00908.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ5 based on UniProtKB P12995.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.6.1.11. 1130.
Family and domain databases
HAMAP	MF_01107. [Tree]
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
PROSITE	PS00600. AA_TRANSFER_CLASS_3. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_BACAM

Accession

Primary (citable) accession number: Q9ZJ10

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	May 1, 1999
Last modified:	September 22, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)