Reviewed, UniProtKB/Swiss-Prot Q9YBY6 (ARGD_AERPE)

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:	APE_1464

Organism

Aeropyrum pernix [Complete proteome] [HAMAP]

Taxonomic identifier

56636 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	388 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 – 388	388	Acetylornithine/acetyl-lysine aminotransferase HAMAP MF_01107		PRO_0000112818
Regions
	Region	100 – 101	2	Pyridoxal phosphate binding By similarity
	Region	211 – 214	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	127	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	130	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	268	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	269	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	240	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9YBY6-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 42FC55B19CACD15A	FASTA	388	41,523
	10 20 30 40 50 60 MNVVLKFVRF YGYRGLRIVK GSMQYVWDDS GRKYLDCHAG HGAAFLGHSN PAIVEAVVRQ 70 80 90 100 110 120 ARELVAASSS FSTPSLEEAL TEFSRIAPPW AEEIVFLNTG TEAVEAALKA AWLATGKRGI 130 140 150 160 170 180 VALKNSFHGR TLASLSVTWN PRYRRGVPVL DTRFLSPSTD PGEVEKLVPE DTAAIIVEPI 190 200 210 220 230 240 QGEGGLTKIY AELAKALREA ADRVGALLIF DEIQTGFGRT GRVWAHESLG VEPDIMTAGK 250 260 270 280 290 300 SIAGGLPASA VLSREGVLAT LASGRHGSTH AANPLSMAAV AAASRFLREE GVPDKARAAG 310 320 330 340 350 360 ALLEGLLRDR IEGLRLVRGV RGEGLMLGVE LRLDPGPVLR CLQESERVLA LRSGATVVRL 370 380 LPPYSISRED AEMVVYGLER CICGGSGC

References

[1]

"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000002 Genomic DNA. Translation: BAA80462.1.
PIR	H72625.
RefSeq	NP_147962.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1446033.
GenomeReviews	Gene locus APE_1464 in contig BA000002_GR.
KEGG	ape:APE_1464.
NMPDR	fig|272557.1.peg.1070.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9YBY6.
OMA	SLSITWN.
Enzyme and pathway databases
BRENDA	2.6.1.11. 256344.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_AERPE

Accession

Primary (citable) accession number: Q9YBY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	November 1, 1999
Last modified:	November 3, 2009
This is version 63 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)