Reviewed, UniProtKB/Swiss-Prot P63569 (ARGD_MYCBO)

Names and origin

Protein names

Recommended name:
    Acetylornithine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11

Gene names

Name:	argD
Ordered Locus Names:	Mb1683

Organism

Mycobacterium bovis [Complete proteome] [HAMAP]

Taxonomic identifier

1765 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-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
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Miscellaneous	May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis. 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
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
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 – 400	400	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112757
Regions
	Region	224 – 227	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	139	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	142	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	281	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	282	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	253	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P63569-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 833846D529795019	FASTA	400	40,910
	10 20 30 40 50 60 MTGASTTTAT MRQRWQAVMM NNYGTPPIAL ASGDGAVVTD VDGRTYIDLL GGIAVNVLGH 70 80 90 100 110 120 RHPAVIEAVT RQMSTLGHTS NLYATEPGIA LAEELVALLG ADQRTRVFFC NSGAEANEAA 130 140 150 160 170 180 FKLSRLTGRT KLVAAHDAFH GRTMGSLALT GQPAKQTPFA PLPGDVTHVG YGDVDALAAA 190 200 210 220 230 240 VDDHTAAVFL EPIMGESGVV VPPAGYLAAA RDITARRGAL LVLDEVQTGM GRTGAFFAHQ 250 260 270 280 290 300 HDGITPDVVT LAKGLGGGLP IGACLAVGPA AELLTPGLHG STFGGNPVCA AAALAVLRVL 310 320 330 340 350 360 ASDGLVRRAE VLGKSLRHGI EALGHPLIDH VRGRGLLLGI ALTAPHAKDA EATARDAGYL 370 380 390 400 VNAAAPDVIR LAPPLIIAEA QLDGFVAALP AILDRAVGAP

References

[1]

"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX248339 Genomic DNA. Translation: CAD96350.1.
RefSeq	NP_855335.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1092626.
GenomeReviews	Gene locus Mb1683 in contig BX248333_GR.
KEGG	mbo:Mb1683.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P63569.
OMA	P63569. PIQGENG.
Enzyme and pathway databases
BRENDA	2.6.1.11. 3091.
Family and domain databases
HAMAP	MF_01107. [Tree]
InterPro	IPR005814. Aminotrans_3. IPR004636. ArgD_aminotrans. 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_MYCBO

Accession

Primary (citable) accession number: P63569
Secondary accession number(s): P94990

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 34 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)