Reviewed, UniProtKB/Swiss-Prot Q8FTN2 (ARGD_COREF)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	CE1529

Organism

Corynebacterium efficiens [Complete proteome] [HAMAP]

Taxonomic identifier

152794 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
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 corresponding 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
Technical term	Complete proteome
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 – 402	402	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112740
Regions
	Region	231 – 234	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	143	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	146	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	288	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	289	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	260	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FTN2-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 53BDDFB1A9EA6DD3	FASTA	402	41,980
	10 20 30 40 50 60 MKNLATVEDT LTSWPQVLLN TYGTPPVELV TGKGSTVTDA DGNVYIDLLA GIAVNALGHA 70 80 90 100 110 120 HPAIIEAVTT QLSQLGHVSN LFATRPVVEV AAELVQRFAL DDATIASQTQ VFFCNSGAEA 130 140 150 160 170 180 NEAAFKLARL TGRHRILAAT NGFHGRTMGS LALTGQPDKR IPFAPLPSGV EFYPYGDLDY 190 200 210 220 230 240 LTTLVESDPT DTAAIILEPI QGETGVIPAP EGFLTGVREL CDKHGLLFIV DEVQTGIGRT 250 260 270 280 290 300 GDFFAHQHEG VTPDVVTMAK GLGGGLPIGA CLATGEAAKL FGPGKHGTTF GGNPVSAAAA 310 320 330 340 350 360 RAVLSVIDEE FCADVARKGE LFAEQLRGVA GVADVRGRGL MLGVVLDQPV AKQAVTAGFK 370 380 390 400 HGLILNAPAD NIIRLTPPLV ITDDEIRDAV RALAAVLAEL NA

References

[1]

"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens." Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T. Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000035 Genomic DNA. Translation: BAC18339.1.
RefSeq	NP_738139.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1031986.
GenomeReviews	Gene locus CE1529 in contig BA000035_GR.
KEGG	cef:CE1529.
NMPDR	fig|196164.1.peg.1529.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8FTN2.
OMA	PIQGENG.
Enzyme and pathway databases
BioCyc	CEFF196164:CE1529-MON.
BRENDA	2.6.1.11. 277326.
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]
TIGRFAMs	TIGR00707. argD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_COREF

Accession

Primary (citable) accession number: Q8FTN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 50 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)