Q8ZV07 (ARGD_PYRAE) 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:	PAE2515

Organism

Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)

Taxonomic identifier

178306 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum

Protein attributes

Sequence length	383 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 – 383	383	Acetylornithine/acetyl-lysine aminotransferase HAMAP MF_01107		PRO_0000112826
Regions
	Region	97 – 98	2	Pyridoxal phosphate binding By similarity
	Region	209 – 212	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	124	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	127	1	N2-acetyl-L-ornithine By similarity
	Binding site	266	1	N2-acetyl-L-ornithine By similarity
	Binding site	267	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	238	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8ZV07 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: A69E88520F3F74A6	FASTA	383	42,146
	10 20 30 40 50 60 MGRIAKYYRE YGIRIVKGFM QYVWDDKGQR YIDCNTNHGV VFLGHANPKI VEAVKKQVEE 70 80 90 100 110 120 IWAVPLNFAT PARERFIEEF SKLLPPKFGV VFLQNTGTEA VEVAIKIAKK VTRKPTIVAF 130 140 150 160 170 180 TNSFHGRTMG SLSITWNEKY KKAFEPLYPH VRFGKFNVPH EVDKLIGEDT CCVVVEPIQG 190 200 210 220 230 240 EGGVNPATPE FLKALREEAQ RKGALLIFDE VQTGFGRTGA VWAFQKYGVE PDIFTAGKPV 250 260 270 280 290 300 AGGLPIGLAV AREDFGDVFE PGEHGSTFAG NAVVMAAAAA ASRLLREEDV PGRAERIGAE 310 320 330 340 350 360 LAKALGDTGS RLAVRVKGMG LMLGLELRVK ADQFIQPLLE RGVMALTAGV NTLRFLPPYM 370 380 ISKEDVEVVH AAVTEVLKKA EQQ

References

[1]	"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum." Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H. Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed: 11792869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009441 Genomic DNA. Translation: AAL64249.1.
RefSeq	NP_560067.1. NC_003364.1.
3D structure databases
ProteinModelPortal	Q8ZV07.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1464590.
GenomeReviews	Gene locus PAE2515 in contig AE009441_GR.
KEGG	pai:PAE2515.
NMPDR	fig|178306.1.peg.1757.
Phylogenomic databases
HOGENOM	HBG725944.
OMA	WLCNSGT.
ProtClustDB	CLSK899771.
Enzyme and pathway databases
BioCyc	PAER178306:PAE2515-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.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_PYRAE

Accession

Primary (citable) accession number: Q8ZV07

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	March 1, 2002
Last modified:	November 16, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program