Reviewed, UniProtKB/Swiss-Prot Q71Z79 (ARGD_LISMF)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	LMOf2365_1610

Organism

Listeria monocytogenes serotype 4b (strain F2365) [Complete proteome] [HAMAP]

Taxonomic identifier

265669 [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
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 – 386	386	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112753
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	N(2)-acetyl-L-ornithine By similarity
	Binding site	263	1	N(2)-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)
	Q71Z79-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: DBD1A9ADA2666900	FASTA	386	41,488
	10 20 30 40 50 60 MKHVFPTYKR FPIDLVNGTG TVVTDKNGKT YLDFTSGIAV CNLGHCPANV AEAVQQQLTN 70 80 90 100 110 120 IWHTSNLYEC ALQDSVAELI ADGKDRLVFF CNSGTEANEA ALKLARKYTG KEKIITFEKS 130 140 150 160 170 180 FHGRTFGSMS ATAQAKIHQG FGGLVPGFTY VPYNDIEAFR AEIDEHTAAV MLEVIQGEGG 190 200 210 220 230 240 VIPANAAFLL EVQLLCKKMG VLLIIDEVQT GLGRTGTLYG FEQIGLEPDI FTLAKGLGNG 250 260 270 280 290 300 LPIGAMVGKA NLSSAFGPGS HGSTFGGNKL ALAAAKEILR TMKQAGFLEE VNAKADYFRY 310 320 330 340 350 360 LLEVHLEALD NVSVIRGGGF LIGIELENTA EPVVTELRDK GLLILTAGAN VLRILPPLTV 370 380 SYAEIDQAIY LLKSVLENQL IGSEEG

References

[1]

"Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species." Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., Daugherty S.C., Dodson R.J. , Durkin A.S., Madupu R., Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., Luchansky J.B., Fraser C.M. Nucleic Acids Res. 32:2386-2395(2004) [PubMed: 15115801] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017262 Genomic DNA. Translation: AAT04385.1.
RefSeq	YP_014208.1.
3D structure databases
SMR	Q71Z79. Positions 3-376.
ModBase	Search...
Protein-protein interaction databases
STRING	Q71Z79.
Genome annotation databases
GeneID	2797889.
GenomeReviews	Gene locus LMOf2365_1610 in contig AE017262_GR.
KEGG	lmf:LMOf2365_1610.
TIGR	LMOf2365_1610.
Phylogenomic databases
eggNOG	COG4992.
HOGENOM	HBG725944.
OMA	ILNAPAD.
Enzyme and pathway databases
BioCyc	LMON265669:LMOF2365_1610-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. [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_LISMF

Accession

Primary (citable) accession number: Q71Z79

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	July 5, 2004
Last modified:	February 9, 2010
This is version 46 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)