Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q3MA36 (ACCA_ANAVT)

Last modified June 16, 2009. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
      Short name=Acetyl-CoA carboxylase carboxyltransferase subunit alpha
      Short name=ACCase subunit alpha
    EC=6.4.1.2
Gene names
Name: accA
Ordered Locus Names: Ava_2535
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA By similarity.

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP MF_00823

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP MF_00823

Subunit structure

Acetyl-CoA carboxylase is an heterohexamer composed of biotin carboxyl carrier protein (accB), biotin carboxylase (accC) and two subunits each of ACCase subunit alpha (accA) and ACCase subunit beta (accD) By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the accA family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentacetyl-CoA carboxylase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetyl-CoA carboxylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823
PRO_1000062574

Sequences

Sequence LengthMass (Da)Tools
Q3MA36-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 2B60D30FF39CF693

FASTA32635,699
        10         20         30         40         50         60 
MATTERKPLL LDFEKPLAEL ANRIDQIRQL AEENGVDVSG EIRKLETRAM QLREEIFSTL 

        70         80         90        100        110        120 
SPSQRLQVAR HPRRPSTLDY IQAISDEWME LHGDRCGGDD PALIGGVARL GGKPVVMLGH 

       130        140        150        160        170        180 
QKGRDTKDNI ARNFGMATPG GYRKAMRLME HANKFSMPIL TFIDTPGALP TVVAERQGAG 

       190        200        210        220        230        240 
EAIAYNLREM FSLDVPIICT VIGEGGSGGA LGIGVGDRLL MFEHSVYTVA TPEACAAILW 

       250        260        270        280        290        300 
KDASKSPQAA VALKIVSHDL KNLGIIDQIL PEPTGGAHSD PLTAATTLKQ ALLDNLDELD 

       310        320 
RLTSQERRQL RYDKFRKIGV FTEVAH 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000117 Genomic DNA. Translation: ABA22150.1.
RefSeqYP_323045.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3682420.
GenomeReviewsGene locus Ava_2535 in contig CP000117_GR.
KEGGava:Ava_2535.
NMPDRfig|240292.3.peg.2016.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3MA36.
OMAQ3MA36. HSVYTVA.

Enzyme and pathway databases

BioCycAVAR240292:AVA_2535-MON.

Family and domain databases

HAMAPMF_00823.
[Tree]
InterProIPR001095. Acetyl_CoA_COase_a_su.
IPR011763. COA_CT_C.
[Graphical view]
PANTHERPTHR22855:SF3. Ac-CoA_carboxylA. 1 hit.
PfamPF03255. ACCA. 1 hit.
[Graphical view]
PRINTSPR01069. ACCCTRFRASEA.
TIGRFAMsTIGR00513. accA. 1 hit.
PROSITEPS50989. COA_CT_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACCA_ANAVT
AccessionPrimary (citable) accession number: Q3MA36
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 25, 2005
Last modified: June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents