Q8Y6U4 (ARGD_LISMO) 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:	lmo1588

Organism

Listeria monocytogenes

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	386 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 Reference 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 – 386	386	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112754
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)
	Q8Y6U4 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 797AE08F908EA328	FASTA	386	41,499
	10 20 30 40 50 60 MKHVFPTYKR FPIDLVNGTG TVVTDKNGKT YLDFTSGIAV CNLGHCPTNV AEAVQQQLGN 70 80 90 100 110 120 IWHTSNLYEC ALQDSVAELI ADGKERLVFF CNSGTESNEA ALKLARKYTG KEKIITFEKS 130 140 150 160 170 180 FHGRTFGSMS ATGQAKIHQG FGELVPGFTY VPYNDIEAFR AEIDENTAAV MLEVIQAEGG 190 200 210 220 230 240 VIPANAAFLL EVQLLCKKMG ALLIIDEVQT GLGRTGTLYG FEQIGLDPDI FTLAKGLGNG 250 260 270 280 290 300 LPIGAMVGKS DLISAFGPGS HGSTFGGNKL ALAAAKEILL TMKQTGFLEE VNAKADYFRN 310 320 330 340 350 360 LLEANLEVLD NVSDIRGGGF LIGIELENAA EPVITELRDK GLLILTAGTN VLRILPPLTV 370 380 SYAEIDQAIY LLKSVLENQL IGSEEG

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: ATCC BAA-679 / EGD-e / Serovar 1/2a.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591979 Genomic DNA. Translation: CAC99666.1.
PIR	AD1273.
RefSeq	NP_465113.1. NC_003210.1.
3D structure databases
ProteinModelPortal	Q8Y6U4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	984620.
GenomeReviews	Gene locus lmo1588 in contig AL591824_GR.
KEGG	lmo:lmo1588.
PATRIC	20312307. VBILisMon69206_1630.
Organism-specific databases
GenoList	LMO1588.
Phylogenomic databases
HOGENOM	HBG725944.
OMA	LARIYFK.
ProtClustDB	PRK02936.
Enzyme and pathway databases
BioCyc	LMON169963:LMO1588-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_LISMO

Accession

Primary (citable) accession number: Q8Y6U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program