Reviewed, UniProtKB/Swiss-Prot Q9RW75 (ARGD_DEIRA)

Names and origin

Protein names

Recommended name:
    Acetylornithine/acetyl-lysine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11
    EC=2.6.1.-

Gene names

Name:	argD
Synonyms:	lysJ
Ordered Locus Names:	DR_0794

Organism

Deinococcus radiodurans [Complete proteome] [HAMAP]

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Involved in both the arginine and lysine biosynthetic pathways By similarity. HAMAP MF_01107
Catalytic activity	N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107 N(2)-acetyl-L-lysine + 2-oxoglutarate = N-acetyl-L-aminoadipate semialdehyde + L-glutamate. HAMAP MF_01107
Cofactor	Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_01107
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107 Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5. HAMAP MF_01107
Subunit structure	Homodimer By similarity. HAMAP MF_01107
Subcellular location	Cytoplasm Probable 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 Lysine 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 lysine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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 – 429	429	Acetylornithine/acetyl-lysine aminotransferase HAMAP MF_01107		PRO_0000112742
Regions
	Region	112 – 113	2	Pyridoxal phosphate binding By similarity
	Region	226 – 229	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	139	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	142	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	283	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	284	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	255	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RW75-1 [UniParc]. Last modified February 12, 2003. Version 2. Checksum: BA614DEDBA7B1025	FASTA	429	46,613
	10 20 30 40 50 60 MTGNEQNPSK WLAAEKKYDS GVYNKHDVVM VRGQGATVWD ENGRSYIDCV VGYGVATLGH 70 80 90 100 110 120 SHPDVVKAVQ EQAGKLMVMP QTVPNDKRAE FLQELVGVLP QGLDRVFLCN SGTEAMEAAK 130 140 150 160 170 180 KFAITATGRS RFVSMKRGFS GRSLGALSFT WEPKYREPFG DAVDNKSVDF VTYGNLDELR 190 200 210 220 230 240 AAVTEQTAAV IMEPVQGEGG VRPASAEFIQ EARRITREKG ALLILDEIQT GFCRTGKMFA 250 260 270 280 290 300 CEHFGVIPDG MTLAKAIAGG TPTAAFAMMS EVADRMPAGG HGTTFGGNPL SMAAGVASLR 310 320 330 340 350 360 AMKREGLAEQ AREKGAYMMD KLRAIQSPKI REVRGLGLMI GVELKEKSAP YIHAMEHDEG 370 380 390 400 410 420 VLCLAATPLV VRFLPPAVIS KEQIDQVVAA FERVLNNVNP REERQAELRA QQSEMGQQQV SQGESVQTE

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000513 Genomic DNA. Translation: AAF10373.1. Different initiation.
PIR	E75474.
RefSeq	NP_294518.1.
3D structure databases
SMR	Q9RW75. Positions 12-395.
ModBase	Search...
Genome annotation databases
GeneID	1798912.
GenomeReviews	Gene locus DR_0794 in contig AE000513_GR.
KEGG	dra:DR_0794.
NMPDR	fig|243230.1.peg.977.
TIGR	DR_0794.
Phylogenomic databases
HOGENOM	HBG725944.
OMA	GVYNKHD.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_0794-MONOMER.
BRENDA	2.6.1.11. 96172.
Family and domain databases
HAMAP	MF_01107. ArgD_aminotrans_3. [Tree]
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase_major_dom. 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_DEIRA

Accession

Primary (citable) accession number: Q9RW75

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	February 12, 2003
Last modified:	February 9, 2010
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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