Reviewed, UniProtKB/Swiss-Prot Q98BB7 (ARGD_RHILO)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	mlr5646

Organism

Rhizobium loti (Mesorhizobium loti) [Complete proteome] [HAMAP]

Taxonomic identifier

381 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium

Protein attributes

Sequence length	399 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 – 399	399	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112773
Regions
	Region	215 – 218	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	130	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	133	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	272	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	273	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	244	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q98BB7-1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 5D5248D98F95DFB5	FASTA	399	42,417
	10 20 30 40 50 60 MSGSALYETF ARAPLAFDHG EGTWLVTDKG ERYLDFAGGI AVNSLGHSHP HLVAALTEQA 70 80 90 100 110 120 AKLWHVSNLY EIPGQSRLGQ RLVDATFADK VFFTNSGAEA LECAIKTARR YHFVKGHPER 130 140 150 160 170 180 FRVITFEGAF HGRTLATIAA GGQYKYLEGF GPKVEGFDQV GFDDIDAAEK AITPETAAIL 190 200 210 220 230 240 IEPVQGEGGI RPVPTQSLKR LRQLCDQHGL LLIYDEVQCG IGRTGKLFAH EWSGVAPDIM 250 260 270 280 290 300 AIAKGIGGGF PMGACLATDE AAVGMTAGVH GTTFGGNPLA MAVGNAVLDV VLEDGFLEDV 310 320 330 340 350 360 QRKALLMKQG LAAIADEFPD VVEDIRGTGL MLGLKCAMPN TKVNMALRDQ HLLAVPAGDN 370 380 390 VIRLLPPLTV TDAEIHEALN RIRAGAKGLA DAIAVAAAK

References

[1]

"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti." Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S. DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MAFF303099.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000012 Genomic DNA. Translation: BAB52055.1.
RefSeq	NP_106269.1.
3D structure databases
SMR	Q98BB7. Positions 6-388.
ModBase	Search...
Genome annotation databases
GeneID	1228930.
GenomeReviews	Gene locus mlr5646 in contig BA000012_GR.
KEGG	mlo:mlr5646.
NMPDR	fig|266835.1.peg.4373.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG725944.
OMA	GVHGTTF.
Enzyme and pathway databases
BRENDA	2.6.1.11. 3315.
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

ARGD_RHILO

Accession

Primary (citable) accession number: Q98BB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	October 1, 2001
Last modified:	February 9, 2010
This is version 55 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)