Reviewed, UniProtKB/Swiss-Prot Q92SA0 (ARGD_RHIME)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	R00517
ORF Names:	SMc02138

Organism

Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	399 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 – 399	399	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112774
Regions
	Region	216 – 219	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	131	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	134	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	273	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	274	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	245	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92SA0-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 9FA90F905A073F5B	FASTA	399	42,381
	10 20 30 40 50 60 MAATTPLYDT YLRAPLRFER GEGVWLIAED GTRYLDFAAG VAVNSLGHAH PHLVEALKAQ 70 80 90 100 110 120 ADKVWHLSNL YEIAGQESLA RRLTQVTFAD RVFFTNSGAE ALECAIKTAR RYHFAKGHVE 130 140 150 160 170 180 KFHVITFEGA FHGRTLATIA AGGQQKYIEG FGPKAPGFYQ VPFGDIGAVK NAINEETAAI 190 200 210 220 230 240 LVEPIQGEGG IRTASKEFMQ GLRELCDEFG LLLILDEVQS GVGRTGKLFA HEWAGIKPDI 250 260 270 280 290 300 MAVAKGIGGG FPLGACLATE AAAAGMVAGT HGSTYGGNPL AMAVGNAVLD VVLAEGFLDQ 310 320 330 340 350 360 VREVALVFRQ GLASLKDRFP DVIEEIRGDG LMLGIKAKVP SADLLKAIRA EKLLVVPAGE 370 380 390 NVLRLLPPLI TTPAEAREGL ARLERAAEAV SGKSGNAAA

References

[1]

"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL591688 Genomic DNA. Translation: CAC45089.1.
RefSeq	NP_384623.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1232153.
GenomeReviews	Gene locus R00517 in contig AL591688_GR.
KEGG	sme:SMc02138.
NMPDR	fig|266834.1.peg.1811.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q92SA0.
OMA	GRKLWHI.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC02138-MON.
BRENDA	2.6.1.11. 142.
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_RHIME

Accession

Primary (citable) accession number: Q92SA0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 57 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)