Reviewed, UniProtKB/Swiss-Prot Q93R93 (ARGD_THET2)

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:	TT_C1393

Organism

Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]

Taxonomic identifier

262724 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	395 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 – 395	395	Acetylornithine/acetyl-lysine aminotransferase HAMAP MF_01107		PRO_0000112806
Regions
	Region	113 – 114	2	Pyridoxal phosphate binding By similarity
	Region	225 – 228	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	140	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	143	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	282	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	283	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	254	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q93R93-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 1D29F8E7585A5C3A	FASTA	395	43,451
	10 20 30 40 50 60 METRTLEDWR ALLEAEKTLD SGVYNKHDLL IVRGQGARVW DAEGNEYIDC VGGYGVANLG 70 80 90 100 110 120 HGNPEVVEAV KRQAETLMAM PQTLPTPMRG EFYRTLTAIL PPELNRVFPV NSGTEANEAA 130 140 150 160 170 180 LKFARAHTGR KKFVAAMRGF SGRTMGSLSV TWEPKYREPF LPLVEPVEFI PYNDVEALKR 190 200 210 220 230 240 AVDEETAAVI LEPVQGEGGV RPATPEFLRA AREITQEKGA LLILDEIQTG MGRTGKRFAF 250 260 270 280 290 300 EHFGIVPDIL TLAKALGGGV PLGVAVMREE VARSMPKGGH GTTFGGNPLA MAAGVAAIRY 310 320 330 340 350 360 LERTRLWERA AELGPWFMEK LRAIPSPKIR EVRGMGLMVG LELKEKAAPY IARLEKEHRV 370 380 390 LALQAGPTVI RFLPPLVIEK EDLERVVEAV RAVLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional and evolutionary relationship between arginine biosynthesis and prokaryotic lysine biosynthesis through alpha-aminoadipate." Miyazaki J., Kobashi N., Nishiyama M., Yamane H. J. Bacteriol. 183:5067-5073(2001) [PubMed: 11489859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of the extreme thermophile Thermus thermophilus." Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J. Nat. Biotechnol. 22:547-553(2004) [PubMed: 15064768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB055203 Genomic DNA. Translation: BAB61775.1. AE017221 Genomic DNA. Translation: AAS81735.1.
RefSeq	YP_005362.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q93R93.
Genome annotation databases
GeneID	2775684.
GenomeReviews	Gene locus TT_C1393 in contig AE017221_GR.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q93R93.
OMA	WEPKYRE.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-6741. TTHE262724:TT_C1393-MON.
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_THET2

Accession

Primary (citable) accession number: Q93R93

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 59 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)