Reviewed, UniProtKB/Swiss-Prot P59315 (ARGD_BIFLO)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	BL1061

Organism

Bifidobacterium longum [Complete proteome] [HAMAP]

Taxonomic identifier

216816 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length	431 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 – 431	431	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112722
Regions
	Region	251 – 254	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	157	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	160	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	313	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	314	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	284	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59315-1 [UniParc]. Last modified February 12, 2003. Version 1. Checksum: 1A9245B103521BCE	FASTA	431	45,615
	10 20 30 40 50 60 MATEHEEKLG TEDSKWLGEY SQVHMNVFGT PLRVMDHGQG AHIWDVDGNE YLDFLAGIAV 70 80 90 100 110 120 NSLGYAHPKW VKAVADQAAK VAHISNYFAS EPQIELASKL VKLAGAPEGS KVYFGNSGAE 130 140 150 160 170 180 GNEAALKLAK LYGRTLPGAL PSIGGKPARI LAMTHGFHGR TMGALSATWK PGIRKPYDPL 190 200 210 220 230 240 VPNIEFVRAG DKVALHDAFA QTGLGRYGKG PVAAVILELI QGEAGVQPLG ADYVKFVREL 250 260 270 280 290 300 CDINHALLII DEVQTGIGRT GKWFAFQRDD LSGGVTPDMV TFAKGVAGGF PMGGMIAFGE 310 320 330 340 350 360 KLAALFTPGS HGSTFAGNPL GAAAGLATLD VIEDENLVAN AEARGEQLRD GIMATGNPLF 370 380 390 400 410 420 VSVRGRGLLD AVELKHPCSH AVMNYCLEHG LIVNAVAPNA LRFAPPLIVT AQDVDQALAI 430 LKDVPTDLPD D

References

[1]

"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract." Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F. Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 2705.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014295 Genomic DNA. Translation: AAN24869.1.
RefSeq	NP_696233.1.
3D structure databases
HSSP	HSSP built from PDB template 2OAT based on UniProtKB P04181.
ModBase	Search...
Genome annotation databases
GeneID	1022592.
GenomeReviews	Gene locus BL1061 in contig AE014295_GR.
KEGG	blo:BL1061.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P59315.
OMA	P59315. ERTRVIT.
Enzyme and pathway databases
BioCyc	BLON206672:BL1061-MON.
BRENDA	2.6.1.11. 39917.
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_BIFLO

Accession

Primary (citable) accession number: P59315

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	February 12, 2003
Last modified:	June 16, 2009
This is version 50 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)