Reviewed, UniProtKB/Swiss-Prot Q7W2N9 (ARGD2_BORPA)

Names and origin

Protein names

Recommended name:
    Acetylornithine aminotransferase 2
      Short name=ACOAT 2
    EC=2.6.1.11

Gene names

Name:	argD2
Ordered Locus Names:	BPP4365

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	396 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 – 396	396	Acetylornithine aminotransferase 2 HAMAP MF_01107		PRO_0000112726
Regions
	Region	219 – 222	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	134	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	137	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	276	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	248	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7W2N9-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 9CF07AF14A6378FF	FASTA	396	42,749
	10 20 30 40 50 60 MEFSQFKVNA LMEITACPDL VFVRGQGSWL EDHAGKRYLD FVQGWAVNTL GHCAPEMKRA 70 80 90 100 110 120 LAEQADKLMN PSPAFYNLPS IELAQRLTSA SCFDRVFFAN SGAEANEGAI KLARKWGRVN 130 140 150 160 170 180 RNGAYKIITM NHGFHGRTLA TMSASGKPGW DTMFAPQVEG FPKAEINDLD SVRALIDAQT 190 200 210 220 230 240 VAVMLEPVQG EAGVIPATRE FMQGLRKLAD EHGILFIVDE VQTGMGRTGS LFAYQQFDVI 250 260 270 280 290 300 PDIMTLAKGI GGGIPLAALL AREEVCVFAH GDQGGTYNGN PLCAAVGVAV FDTITAPGFM 310 320 330 340 350 360 EAAQARTRQL SEGLLALSAK RGLRGERGMG LLRALVLDRD DAPAIVEAAR MLAPEGLLLN 370 380 390 APRGNLLRFM PALNVTEADM ARMLEQLDGV IAAVRK

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640436 Genomic DNA. Translation: CAE39644.1.
RefSeq	NP_886493.1.
3D structure databases
SMR	Q7W2N9. Positions 11-394.
ModBase	Search...
Genome annotation databases
GeneID	1666162.
KEGG	bpa:BPP4365.
NMPDR	fig|257311.1.peg.4127.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG725944.
OMA	LFAYELS.
PhylomeDB	Q7W2N9.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP4365-MONOMER.
BRENDA	2.6.1.11. 263123.
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

ARGD2_BORPA

Accession

Primary (citable) accession number: Q7W2N9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 50 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)