Q92BC0 (ARGD_LISIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	lin1630

Organism

Listeria innocua [Complete proteome] [HAMAP]

Taxonomic identifier

1642 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	384 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: UniProtKB-KW
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: EC 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 – 384	384	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112752
Regions
	Region	94 – 95	2	Pyridoxal phosphate binding By similarity
	Region	206 – 209	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	121	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	124	1	N2-acetyl-L-ornithine By similarity
	Binding site	263	1	N2-acetyl-L-ornithine By similarity
	Binding site	264	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	235	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92BC0 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: A37DC1EFCC411F0B	FASTA	384	41,336
	10 20 30 40 50 60 MKHVFPTYNR FPVDIVKGNG TVVKDATGKT YLDFTSGIAV CNLGHCPENV TEAIQSQLAN 70 80 90 100 110 120 IWHTSNLYEC ALQDSVAELI TDGTDKLVFF CNSGTEANEA ALKLARKYTG KEKIITFEKS 130 140 150 160 170 180 FHGRTFGSMS ATGQAKIHQG FGRLVPGFTY VPYNDIESFK TELDENTAAV MLEVIQGEGG 190 200 210 220 230 240 VIPGNAAWLM EVQMLCKKAG ALLIIDEVQT GLGRTGTLFG FQQTFLDPDI FTLAKGLGNG 250 260 270 280 290 300 LPIGAMVGKE HLSSAFGPGS HGSTFGGNKL ALAAAKEILL TMKQTGFLEE VNAKAAYFRN 310 320 330 340 350 360 LLEEHFEQLE NVVAIRGEGF LIGIELGSSA APVVTELRDK GLLILTAGPN ILRILPPLTV 370 380 SYAEIDQAIS ILKSVLEKQL IGSE

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIP 11262 / Serovar 6a.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL596169 Genomic DNA. Translation: CAC96861.1.
PIR	AE1636.
RefSeq	NP_470966.1. NC_003212.1.
3D structure databases
ProteinModelPortal	Q92BC0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1130253.
GenomeReviews	Gene locus lin1630 in contig AL592022_GR.
KEGG	lin:lin1630.
NMPDR	fig|272626.1.peg.1619.
PATRIC	20299997. VBILisInn102668_1665.
Organism-specific databases
GenoList	LIN1630.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG725944.
OMA	GAMIGKA.
ProtClustDB	PRK02936.
Enzyme and pathway databases
BioCyc	LINN272626:LIN1630-MONOMER.
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. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K00818.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00707. ArgD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_LISIN

Accession

Primary (citable) accession number: Q92BC0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program