Q8U0B4 (ARGD_PYRFU) 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:	PF1685

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Taxonomic identifier

186497 [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 Reference 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_0000112827
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)
	Q8U0B4 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 3E8AAF15CDF30B92	FASTA	366	40,704
	10 20 30 40 50 60 MSLYRKRLRL VKGEGIYVWD SQGKKYIDLI AGIGVNVLGH NHPEWVSELQ EQLEKLVVAG 70 80 90 100 110 120 PMFDHEEKYE MLEELEKFVT YEYVYIGNSG TEAVEAALKF ARLYTGRKEI IAMTNAFHGR 130 140 150 160 170 180 TMGALSATWK PKYREDFKPL VPGFKHIPFN DVEAAKEAIT TETAAVIFEP IQGEGGVVPA 190 200 210 220 230 240 NEEFVKTLRD LTEDKGALLI ADEVQSGLRT GKFLAIEHYK VEPDIVTMGK GIGNGVPVSL 250 260 270 280 290 300 TLTNFDVERG KHGSTFGGNP LACKAVAVTL RILRREKLIE KAAEKFIEIK GENVVLTRGK 310 320 330 340 350 360 GLMIGIVMKK PVAKVVEELQ NRGYLVHTAG QRVIRLLPPL IISKDEINQA KSAIEGVIND IYGRKN

References

[1]	"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009950 Genomic DNA. Translation: AAL81809.1.
RefSeq	NP_579414.1. NC_003413.1.
3D structure databases
ProteinModelPortal	Q8U0B4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8U0B4. 1 interaction.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000005525; EBPYRP00000005386; EBPYRG00000005524.
GeneID	1469562.
GenomeReviews	Gene locus PF1685 in contig AE009950_GR.
KEGG	pfu:PF1685.
NMPDR	fig|186497.1.peg.1733.
Phylogenomic databases
GeneTree	EBGT00050000022264.
HOGENOM	HBG725944.
OMA	WLCNSGT.
PhylomeDB	Q8U0B4.
ProtClustDB	PRK04013.
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_PYRFU

Accession

Primary (citable) accession number: Q8U0B4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	June 1, 2002
Last modified:	December 14, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program