Reviewed, UniProtKB/Swiss-Prot P63566 (ARGD_BRUME)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	BMEI1621

Organism

Brucella melitensis [Complete proteome] [HAMAP]

Taxonomic identifier

29459 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	403 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 – 403	403	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112732
Regions
	Region	219 – 222	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	134	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	137	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	276	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	277	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	248	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P63566-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: F413C19CD940A271	FASTA	403	43,453
	10 20 30 40 50 60 MTDATTVHPL YDTYNRAALR FERGEGIWLI TEDGERYIDF AAGIAVNSLG HSHPHLVETL 70 80 90 100 110 120 KTQAEKLWHL SNVYEIPAQE KLGRRLVEST FADKVFFTNS GAEALECAIK TARRYQYVSG 130 140 150 160 170 180 HPERFRIITF EGAFHGRTLA TIAAGGQAKY LEGFGPKVEG FDQVPFGDEA ALRAAITPET 190 200 210 220 230 240 AGILLEPIQG EGGLRAFPEE FLRLVRQICD ENGLLLLLDE VQTGVGRTGK LFAHEWAGIR 250 260 270 280 290 300 PDIMAIAKGI GGGFPIGACL ATAEAAKGMT AGMHGTTYGG NPLGMAVGNA VLDVVLADGF 310 320 330 340 350 360 MENVQATALV MKQGLASLVD RYPNVVSEIR GRGLLMGLKC VVPNTSLIQA LRDEHILSVG 370 380 390 400 AGDNVVRLLP PLITTPEEAR EALKHIETAV ERLSIANPIS KTV

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094 / Biotype 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008917 Genomic DNA. Translation: AAL52802.1.
PIR	AG3454.
RefSeq	NP_540538.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1197332.
GenomeReviews	Gene locus BMEI1621 in contig AE008917_GR.
KEGG	bme:BMEI1621.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P63566.
OMA	GRKLWHI.
Enzyme and pathway databases
BioCyc	BMEL224914:BMEI1621-MON.
BRENDA	2.6.1.11. 277959.
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_BRUME

Accession

Primary (citable) accession number: P63566
Secondary accession number(s): Q8YFA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	November 3, 2009
This is version 39 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)