ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9PKC9


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ACCA_CHLMU
Primary accession number Q9PKC9
Secondary accession numbers None
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 42)
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: TC_0536
From
Chlamydia muridarum [TaxID: 83560] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MoPn / Nigg;
DOI=10.1093/nar/28.6.1397; PubMed=10684935 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(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
AE002160; AAF39376.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D81691; D81691.
RefSeq NP_296913.1; -.
3D structure databases
ModBase Q9PKC9.
Enzyme and pathway databases
BioCyc CMUR243161:TC_0536-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 Q9PKC9.
Genome annotation databases
GeneID 1245896; -.
GenomeReviews AE002160_GR; TC_0536.
KEGG cmu:TC0536; -.
TIGR TC_0536; -.
Phylogenomic databases
HOGENOM Q9PKC9; -.
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   324  324     Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha. PRO_0000223751
Sequence information
Length: 324 AA [This is the length of the unprocessed precursor] Molecular weight: 36346 Da [This is the MW of the unprocessed precursor] CRC64: F0679CDAF82FC2B8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MELLPHEKQV VEYEKTIADF KEKNKENSLL SSSEIQKLEN RLDRLKEKIY SNLTPWERVQ 

        70         80         90        100        110        120 
ICRHPSRPRT INYIEGMCEE FVELCGDRTF RDDPAVVGGF AKIQGQRFML IGQEKGCDTT 

       130        140        150        160        170        180 
SRMHRNFGML CPEGFRKALR LAKMAEKFGL PIIFLVDTPG AFPGLTAEER GQGWAIATNL 

       190        200        210        220        230        240 
FELARLATPI IVVVIGEGCS GGALGMAIGD VVAMLEHSYY SVISPEGCAS ILWKDPKKNS 

       250        260        270        280        290        300 
DAAAMLKMHG EDLKGFAIVD AVIKEPIGGA HHNPVATYRS VQEYVLQEWL KLKDLPVEEL 

       310        320 
LEKRYQKFRT IGLYETSSES SSEA 

Q9PKC9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

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

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!