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UniProtKB/Swiss-Prot entry Q9PI62


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

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Entry information
Entry name ACCA_CAMJE
Primary accession number Q9PI62
Secondary accession number Q0PB67
Integrated into Swiss-Prot on February 21, 2006
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 37)
Name and origin of the protein
Protein name Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Synonyms Acetyl-CoA carboxylase carboxyltransferase subunit alpha
ACCase subunit alpha
EC 6.4.1.2
Gene name
Name: accA
OrderedLocusNames: Cj0443
From
Campylobacter jejuni [TaxID: 197] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(2000).
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
AL111168; CAL34593.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A81389; A81389.
3D structure databases
ModBase Q9PI62.
Protein-protein interaction databases
IntAct Q9PI62; -.
Enzyme and pathway databases
BioCyc CJEJ192222:CJ0443-MON; -.
Ontologies
GO
GO:0009317; Cellular component: acetyl-CoA carboxylase complex (inferred from electronic annotation from InterPro).
GO:0003989; Molecular function: acetyl-CoA carboxylase activity (inferred from electronic annotation from HAMAP).
GO:0006633; Biological process: fatty acid biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00823; -; 1.
PBIL [Tree]
InterPro IPR001095; Acetyl_CoA_COase_a_su.
IPR011763; COA_CT_C.
Graphical view of domain structure.
PANTHER PTHR22855:SF3; Ac-CoA_carboxylA; 1.
Pfam PF03255; ACCA; 1.
Pfam graphical view of domain structure.
PRINTS PR01069; ACCCTRFRASEA.
TIGRFAMs TIGR00513; accA; 1.
PROSITE PS50989; COA_CT_CTER; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9PI62.
Genome annotation databases
GenomeReviews AL111168_GR; Cj0443.
KEGG cje:Cj0443; -.
CMR Q9PI62; Cj0443.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Fatty acid biosynthesis; Ligase; Lipid synthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   312  312     Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha. PRO_0000223747
Sequence information
Length: 312 AA [This is the length of the unprocessed precursor] Molecular weight: 34253 Da [This is the MW of the unprocessed precursor] CRC64: 8DDE111C042DADA4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASYLDFEKN IQQIDEDIIN AQIKGDTEAV SILKKNLEKE ISKTYKNLSD FQRLQLARHP 

        70         80         90        100        110        120 
DRPYALDYIE LILNDAHEIH GDRAFRDDPA IVCFMGYLGE KKIIVIGEQK GRGTKDKIAR 

       130        140        150        160        170        180 
NFGMPHPEGY RKALRVAGLA EKFQIPILFL IDTPGAYPGI GAEERGQSEA IARNLYELSD 

       190        200        210        220        230        240 
LKIPTIAIVI GEGGSGGALA IGVADKLAMM KNSVFSVISP EGCAAILWND PAKSEAATKA 

       250        260        270        280        290        300 
MKVTADDLKS QGLIDDVIDE PTNGAHRNKE AAAVAIADYV KKSLNELENI DVRELSANRM 

       310 
QKILKLGAYQ EA 

Q9PI62 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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