Reviewed, UniProtKB/Swiss-Prot Q89LG2 (ARGD2_BRAJA)

Names and origin

Protein names

Recommended name:
    Acetylornithine aminotransferase 2
      Short name=ACOAT 2
    EC=2.6.1.11

Gene names

Name:	argD2
Ordered Locus Names:	blr4582

Organism

Bradyrhizobium japonicum [Complete proteome] [HAMAP]

Taxonomic identifier

375 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
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. HAMAP MF_01107
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. HAMAP MF_01107
Subcellular location	Cytoplasm Probable HAMAP MF_01107.
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 – 398	398	Acetylornithine aminotransferase 2 HAMAP MF_01107		PRO_0000112730
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	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	248	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89LG2-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 874323922CF5CEBB	FASTA	398	42,207
	10 20 30 40 50 60 MTTATHPYDA LMDITARPKA VFVRGAGSYL WDDSRKRYLD FVQGWAVNCL GHSPSAIADA 70 80 90 100 110 120 LAAQAKRLLT PSPAFYNEPS LKLAQALVAN SAFDQVFFAN SGAEANEGAI KLARKYGSLH 130 140 150 160 170 180 KGGAFEIISF EGGFHGRTLA TMSASGKKAF EPLFEPKVAG FKKAKLNDIA SVEKLINDNT 190 200 210 220 230 240 VAVMLEPIQG ESGVWPATDQ FLQELRALTK AHGLLLILDE IQTGMGRTGK LFHYEHTGIA 250 260 270 280 290 300 PDIMTLGKGI GGGVPLAALL ATERAACFEH GDQGGTFNGN PIMCAAGLAV LDEVGKPDFL 310 320 330 340 350 360 KSVTETGLLL ESELQKVSAR HGLGGVRGRG LLLALDLKLP IAPGIVAQAF EAGVLLNAPQ 370 380 390 VDTLRFMPAL NVTRAEIAEM IDCLDAILTK AGAARRVA

References

[1]

"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110." Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S. DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: USDA 110.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000040 Genomic DNA. Translation: BAC49847.1.
RefSeq	NP_771222.1.
3D structure databases
SMR	Q89LG2. Positions 12-388.
ModBase	Search...
Genome annotation databases
GeneID	1052493.
GenomeReviews	Gene locus blr4582 in contig BA000040_GR.
KEGG	bja:blr4582.
NMPDR	fig|224911.1.peg.4582.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG725944.
OMA	HIITASQ.
Enzyme and pathway databases
BioCyc	BJAP224911:BLR4582-MONOMER.
BRENDA	2.6.1.11. 280.
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. [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

ARGD2_BRAJA

Accession

Primary (citable) accession number: Q89LG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
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)