Reviewed, UniProtKB/Swiss-Prot Q5JFW3 (ARGD_PYRKO)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	TK0275

Organism

Pyrococcus kodakaraensis (Thermococcus kodakaraensis) [Complete proteome] [HAMAP]

Taxonomic identifier

311400 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

Protein attributes

Sequence length	362 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 – 362	362	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112829
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)
	Q5JFW3-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 0165413621B3AC06	FASTA	362	40,170
	10 20 30 40 50 60 MPLYRKRLRL VRGEGVYVWD EKGRRYLDLI AGIGVNVLGH AHPEWVLDMS RQLEKIVVAG 70 80 90 100 110 120 PMFEHDEREE MLEELSHWVD YEYVYMGNSG TEAVEAAIKF ARLATGRSEI VAMTNAFHGR 130 140 150 160 170 180 TLGSLSATWK KKYREGFGPL VPGFKHIPFN NVEAAKEAIT KETAAVIFEP IQGEGGIVPA 190 200 210 220 230 240 DEEFVKTLRD LTEDVGALLI ADEVQSGLRT GKFLAIEHYG VRPDIVTMGK GIGNGFPVSL 250 260 270 280 290 300 TLTDLEIPRG KHGSTFGGNP LACRAVATTL RILRRDRLVE KAGEKFMEFS GERVVKTRGR 310 320 330 340 350 360 GLMIGIVLRR PAGNYVKALQ ERGILVNTAG NRVIRLLPPL IIEGDTLEEA RKEIEGVLND IL

References

[1]

"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes." Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T. Genome Res. 15:352-363(2005) [PubMed: 15710748] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KOD1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP006878 Genomic DNA. Translation: BAD84464.1.
RefSeq	YP_182688.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5JFW3.
Genome annotation databases
GeneID	3235753.
GenomeReviews	Gene locus TK0275 in contig AP006878_GR.
KEGG	tko:TK0275.
NMPDR	fig|69014.3.peg.22.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5JFW3.
OMA	SLSITWN.
Enzyme and pathway databases
BioCyc	TKOD69014:TK0275-MON.
BRENDA	2.6.1.11. 192130.
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_PYRKO

Accession

Primary (citable) accession number: Q5JFW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	February 15, 2005
Last modified:	November 3, 2009
This is version 37 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)