Q7VTJ7 (ARGD1_BORPE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylornithine aminotransferase 1
Short name=ACOAT 1
EC=2.6.1.11

Gene names

Name:	argD1
Ordered Locus Names:	BP3539

Organism

Bordetella pertussis

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	393 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 – 393	393	Acetylornithine aminotransferase 1 HAMAP MF_01107		PRO_0000112727
Regions
	Region	215 – 218	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	131	1	N2-acetyl-L-ornithine By similarity
	Binding site	272	1	N2-acetyl-L-ornithine By similarity
	Binding site	273	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	244	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VTJ7 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 90442EA116445BD3	FASTA	393	41,438
	10 20 30 40 50 60 MSSALANIYA RLPVSFTHGR GVWLWDTGER RYLDALAGIG VSCLGHGHPG LVAAISEQAA 70 80 90 100 110 120 RLIHTSNIYE VPQQAALARR LAELSGMSEV LFNNSGSEAN EAAIKLARYY GYKQGNTHAH 130 140 150 160 170 180 IITMDSSWHG RTLATLAATG SDKARQGFGP MPSGFIQVPY NDLPAIRAAG EAEPRVTAVL 190 200 210 220 230 240 LEVLQGEGGI RPSDMAFLQG VRQLCTERGW LLMIDEVQSG IGRTGKWFAH QWADIRPDVM 250 260 270 280 290 300 TLAKGLAGGV PIGAMLAAGP AAGVFAPGSH GTTFGGGPLA CAAGLAVIDA IEQEGLLGNA 310 320 330 340 350 360 HEVGAHLHAA LASELAGAPG VIEVRGRGLM LGIELDRPCG ILATRAMEAG LLINVTRERV 370 380 390 VRLLPPLILS GEEADQIVRI LVPLIKQFLA QQQ

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: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640421 Genomic DNA. Translation: CAE43798.1.
RefSeq	NP_882054.1. NC_002929.2.
3D structure databases
ProteinModelPortal	Q7VTJ7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2665147.
GenomeReviews	Gene locus BP3539 in contig BX470248_GR.
KEGG	bpe:BP3539.
NMPDR	fig|257313.1.peg.3124.
PATRIC	21160732. VBIBorPer7866_3831.
Phylogenomic databases
HOGENOM	HBG725944.
OMA	WFAFQHT.
PhylomeDB	Q7VTJ7.
ProtClustDB	PRK02627.
Enzyme and pathway databases
BioCyc	BPER257313:BP3539-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

ARGD1_BORPE

Accession

Primary (citable) accession number: Q7VTJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program