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UniProtKB/Swiss-Prot entry P63568


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

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Entry information
Entry name ARGD_MYCTU
Primary accession number P63568
Secondary accession number P94990
Integrated into Swiss-Prot on October 11, 2004
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 31)
Name and origin of the protein
Protein name Acetylornithine aminotransferase
Synonyms ACOAT
EC 2.6.1.11
Gene name
Name: argD
OrderedLocusNames: Rv1655, MT1693
ORFNames: MTCY06H11.20
From
Mycobacterium tuberculosis [TaxID: 1773] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
DOI=10.1038/31159; PubMed=9634230 [NCBI, ExPASy, EBI, Israel, Japan]
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.";
Nature 393:537-544(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC 1551 / Oshkosh;
DOI=10.1128/JB.184.19.5479-5490.2002; PubMed=12218036 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains.";
J. Bacteriol. 184:5479-5490(2002).
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
BX842577; CAB06649.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000516; AAK45962.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B70621; B70621.
RefSeq NP_216171.1; -.
NP_336148.1; -.
3D structure databases
HSSP P12995; 1QJ3. [HSSP ENTRY / PDB]
ModBase P63568.
Organism-specific databases
TubercuList Rv1655; -.
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.
ProtoNet P63568.
Genome annotation databases
GeneID 885187; -.
925079; -.
GenomeReviews AE000516_GR; MT1693.
AL123456_GR; Rv1655.
KEGG mtc:MT1693; -.
mtu:Rv1655; -.
TIGR MT1693; -.
Phylogenomic databases
HOGENOM P63568; -.
Other
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   400  400     Acetylornithine aminotransferase. PRO_0000112756
BINDING   253   253        Pyridoxal phosphate (covalent) (By similarity). 
Sequence information
Length: 400 AA [This is the length of the unprocessed precursor] Molecular weight: 40910 Da [This is the MW of the unprocessed precursor] CRC64: 833846D529795019 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTGASTTTAT MRQRWQAVMM NNYGTPPIAL ASGDGAVVTD VDGRTYIDLL GGIAVNVLGH 

        70         80         90        100        110        120 
RHPAVIEAVT RQMSTLGHTS NLYATEPGIA LAEELVALLG ADQRTRVFFC NSGAEANEAA 

       130        140        150        160        170        180 
FKLSRLTGRT KLVAAHDAFH GRTMGSLALT GQPAKQTPFA PLPGDVTHVG YGDVDALAAA 

       190        200        210        220        230        240 
VDDHTAAVFL EPIMGESGVV VPPAGYLAAA RDITARRGAL LVLDEVQTGM GRTGAFFAHQ 

       250        260        270        280        290        300 
HDGITPDVVT LAKGLGGGLP IGACLAVGPA AELLTPGLHG STFGGNPVCA AAALAVLRVL 

       310        320        330        340        350        360 
ASDGLVRRAE VLGKSLRHGI EALGHPLIDH VRGRGLLLGI ALTAPHAKDA EATARDAGYL 

       370        380        390        400 
VNAAAPDVIR LAPPLIIAEA QLDGFVAALP AILDRAVGAP 

P63568 in FASTA format

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