O59401 (ARGD_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	argD
Synonyms:	lysJ
Ordered Locus Names:	PH1716

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	366 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: UniProtKB-KW 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: EC 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 – 366	366	Acetylornithine/acetyl-lysine aminotransferase HAMAP MF_01107		PRO_0000112828
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	N2-acetyl-L-ornithine By similarity
	Binding site	254	1	N2-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)
	O59401 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 58DD45CC427CB200	FASTA	366	40,745
	10 20 30 40 50 60 MSLYRKRLKI IKGEGIYVWD DQGRRYVDLI AGIGVAILGH NHPEWVEGIR EQLNKLVIAG 70 80 90 100 110 120 PMFNHEEKEE MLEELSKFVN FEYLYMGNSG TEAVEAALKF ARLYTGRKEI IAMVNAFHGR 130 140 150 160 170 180 TMGALSATWK PKYKKDFEPL VPGFKHIPFN DVEAAKEAIS KETAAVIVEP IQGESGVIPA 190 200 210 220 230 240 KKEFMKALRD LTEDVGALLI VDEVQTGLRT GKFLAVEHYK IEPDIVTMGK GIGNGIPVGL 250 260 270 280 290 300 TLTNFDVERG KHGSTFGGNP LACKAVAITL RILRKERLIE KAKNKFIQID ADEVVTTRGK 310 320 330 340 350 360 GLMIGIVFKT TIGKYVEELQ NRGYLVHTAG QRVMRLLPPL IISKETMQDV KLAIEGVIND LRGGEN

References

[1]

"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000001 Genomic DNA. Translation: BAA30830.1.
PIR	G71179.
RefSeq	NP_143559.1. NC_000961.1.
3D structure databases
ProteinModelPortal	O59401.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000001076; EBPYRP00000001076; EBPYRG00000001076.
GeneID	1442563.
GenomeReviews	Gene locus PH1716 in contig BA000001_GR.
KEGG	pho:PH1716.
NMPDR	fig|70601.1.peg.1677.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000022264.
HOGENOM	HBG725944.
OMA	WLCNSGT.
PhylomeDB	O59401.
ProtClustDB	PRK04013.
Enzyme and pathway databases
BioCyc	PHOR70601:PH1716-MONOMER.
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. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K05830.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00707. ArgD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_PYRHO

Accession

Primary (citable) accession number: O59401

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program