Reviewed, UniProtKB/Swiss-Prot Q9CNT1 (ARGD_PASMU)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	PM0344

Organism

Pasteurella multocida [Complete proteome] [HAMAP]

Taxonomic identifier

747 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Pasteurella

Protein attributes

Sequence length	398 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 – 398	398	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112763
Regions
	Region	222 – 225	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	137	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	140	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	279	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	280	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	251	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9CNT1-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 42688D0E78709922	FASTA	398	43,712
	10 20 30 40 50 60 MTQYNREIFD QVMIQNYVPA QFIPVRGKGS HVWDQQGKDY IDFTSGIAVN SLGHCADEIV 70 80 90 100 110 120 DVLKQQSEKL WHSSNWFTSE PTLALATKLV EKTFAERVMF VNSGAEANEA ALKLARRYAV 130 140 150 160 170 180 DHFGYQKSKI IAFKQSFHGR TLFTVSVGGQ AKYSDGFGPK PADIVHVPFN DLAAVQAVMD 190 200 210 220 230 240 ENTCAVIVEP IQGESGILPA SQDFLQGLRE LCDQHNALLI FDEVQTGVGR TGYLYAYMKY 250 260 270 280 290 300 EVVPDILTSA KALGNGFPIG AMLTTHEIAK SFAPGVHGTT FGGNPLACAV AEKVIDIISA 310 320 330 340 350 360 PPFLQKIQRT SEKFMQKLQE INQQCGLFKE IRGEGLLIGA ELIEQYHGRA SEFVKKAADN 370 380 390 GLMILVAGPN VLRFAPALNI SEEALALGFE RLAKTLHI

References

[1]	"Complete genomic sequence of Pasteurella multocida Pm70." May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V. Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed: 11248100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pm70.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE004439 Genomic DNA. Translation: AAK02428.1.
RefSeq	NP_245281.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1243691.
GenomeReviews	Gene locus PM0344 in contig AE004439_GR.
KEGG	pmu:PM0344.
NMPDR	fig|272843.1.peg.344.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9CNT1.
OMA	EHNALLV.
Enzyme and pathway databases
BRENDA	2.6.1.11. 258935.
Family and domain databases
HAMAP	MF_01107. [Tree]
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. IPR017652. SuccinylOrn_transaminase. [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. 1 hit.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR03246. arg_catab_astC. 1 hit. TIGR00707. argD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_PASMU

Accession

Primary (citable) accession number: Q9CNT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	June 1, 2001
Last modified:	November 3, 2009
This is version 54 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)