Reviewed, UniProtKB/Swiss-Prot Q9V1I4 (ARGD_PYRAB)

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:	PYRAB04430
ORF Names:	PAB2440

Organism

Pyrococcus abyssi [Complete proteome] [HAMAP]

Taxonomic identifier

29292 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Involved in both the arginine and lysine biosynthetic pathways By similarity.
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.
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.
Subcellular location	Cytoplasm Probable.
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 – 364	364	Acetylornithine/acetyl-lysine aminotransferase HAMAP MF_01107		PRO_0000112825
Regions
	Region	90 – 91	2	Pyridoxal phosphate binding By similarity
	Region	202 – 205	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	117	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	120	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	254	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	255	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	230	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9V1I4-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 32CC172CC999E60F	FASTA	364	40,392
	10 20 30 40 50 60 MSLYRKRLKI VRGEGIYVWD SEGKRYLDLI AGIGVAILGH NHPKWVEEVG NQLNKLVVAG 70 80 90 100 110 120 PMFEHEEKEE MLEELSRWVN FEYVYMGNSG TEAVEAALKF ARLYTGRKEI IAMTNAFHGR 130 140 150 160 170 180 TMGALSATWK SKYKKDFEPL VPGFKHIPFN DVEAAKEAIT RTTAAVIFEP IQGESGIIPA 190 200 210 220 230 240 KEEFVKTLRD LTEDVGALLI ADEVQSGLRT GKFLAVEHYK VEPDIVTLGK GIGNGVPVSL 250 260 270 280 290 300 TLTNFDVERG KHGSTFGGNP LACKAVAVTL RILRKERLVE KASEKFIKVK GKDVVTTRGR 310 320 330 340 350 360 GLMIGIVLKK PVGRYVEELQ NEGYLVHTSG QRVIRLLPPL IISKEKMMEV KSAIEGVING DTEG

References

[1]

"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi." Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P. Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GE5 / Orsay.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ248284 Genomic DNA. Translation: CAB49365.1.
PIR	F75160.
RefSeq	NP_126134.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1495338.
GenomeReviews	Gene locus PYRAB04430 in contig AL096836_GR.
KEGG	pab:PAB2440.
NMPDR	fig|272844.1.peg.462.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9V1I4.
OMA	SLSITWN.
Enzyme and pathway databases
BioCyc	PABY272844:PAB2440-MON.
BRENDA	2.6.1.11. 262861.
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_PYRAB

Accession

Primary (citable) accession number: Q9V1I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 62 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)