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UniProtKB/Swiss-Prot entry Q7W2N9

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARGD2_BORPA
Primary accession number Q7W2N9
Secondary accession numbers None
Integrated into Swiss-Prot on January 16, 2004
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 40)
Name and origin of the protein
Protein name Acetylornithine aminotransferase 2
Synonyms ACOAT 2
EC 2.6.1.11
Gene name
Name: argD2
OrderedLocusNames: BPP4365
From
Bordetella parapertussis [TaxID: 519] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Alcaligenaceae; Bordetella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
DOI=10.1038/ng1227; PubMed=12910271 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BX640436; CAE39644.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_886493.1; -.
3D structure databases
ModBase Q7W2N9.
Enzyme and pathway databases
BioCyc BPAR257311:BPP4365-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003992; Molecular function: acetylornithine transaminase activity (inferred from electronic annotation from HAMAP).
GO:0030170; Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0006526; Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01107; -; 1.
PBIL [Tree]
InterPro IPR005814; Aminotrans_3.
IPR004636; ArgD_aminotrans.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
Graphical view of domain structure.
Gene3D G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
PANTHER PTHR11986; Aminotrans_3; 1.
PTHR11986:SF19; ArgD_aminotrans; 1.
Pfam PF00202; Aminotran_3; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00707; argD; 1.
PROSITE PS00600; AA_TRANSFER_CLASS_3; 1.
Genome annotation databases
GeneID 1666162; -.
GenomeReviews BX470249_GR; BPP4365.
KEGG bpa:BPP4365; -.
NMPDR fig|257311.1.peg.4127; -.
Phylogenomic databases
HOGENOM Q7W2N9; -.
Genome annotation databases
CMR Q7W2N9; BPP4365.
Other
ProtoNet Q7W2N9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis; Complete proteome; Cytoplasm; Pyridoxal phosphate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   396  396     Acetylornithine aminotransferase 2. PRO_0000112726
BINDING   248   248        Pyridoxal phosphate (covalent) (By similarity). 
Sequence information
Length: 396 AA [This is the length of the unprocessed precursor] Molecular weight: 42749 Da [This is the MW of the unprocessed precursor] CRC64: 9CF07AF14A6378FF [This is a checksum on the sequence] 
        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
Q7W2N9 in FASTA format

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