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Q85FL3 (ACCD_ADICA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Short name=ACCase subunit beta
Short name=Acetyl-CoA carboxylase carboxyltransferase subunit beta
EC=6.4.1.2
Gene names
Name:accD
Encoded onPlastid; Chloroplast
OrganismAdiantum capillus-veneris (Maidenhair fern)
Taxonomic identifier13818 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaMoniliformopsesPolypodiopsidacore leptosporangiate fernsPolypodialesPteridaceaeAdiantum

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA By similarity. HAMAP-Rule MF_01395

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP-Rule MF_01395

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01395

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP-Rule MF_01395

Subunit structure

Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD) By similarity.

Subcellular location

Plastidchloroplast stroma By similarity HAMAP-Rule MF_01395.

Sequence similarities

Belongs to the AccD/PCCB family.

RNA editing

Edited at positions 1, 3, 59, 63, 73, 88, 115, 139, 146, 180, 184, 260 and 284.
The initiator methionine is created by RNA editing. The nonsense codon at position 260 is modified to a sense codon. Ref.2

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic HAMAP-Rule MF_01395
PRO_0000199777

Regions

Zinc finger51 – 7323C4-type By similarity

Sites

Metal binding511Zinc By similarity
Metal binding541Zinc By similarity
Metal binding701Zinc By similarity
Metal binding731Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q85FL3 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 2C5B38A8CDCB054E

FASTA31034,417
        10         20         30         40         50         60 
MVMSVINWFE DRQKFGGLIG AFLEEATRSS MTNERDRRIS VNANKGLWAR CDNCGNMLYV 

        70         80         90        100        110        120 
KFLKQNRSVC EECGYHLSMS SMERIELLID PNTWIPLDED MSARDILSFS DEDSYETRIL 

       130        140        150        160        170        180 
LSQEKTGLTD AVQTGIGYLN GTLIALGVMD FHFMGGSMGS VVGEKITRLI EYATQRLLPL 

       190        200        210        220        230        240 
VLICASGGAR MQEGTLSLMQ MAKISSVLQL YQVQNKLLYI SVLTYPTTGG VTASFGMLGD 

       250        260        270        280        290        300 
IIIAEPKAYI AFAGKRVIEQ TLRQKIPDGF QAAESLFDNG LLDLIVPRNL LKGVLSEISG 

       310 
LYLSVPYNKN 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of the chloroplast genome from a leptosporangiate fern, Adiantum capillus-veneris L."
Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.
DNA Res. 10:59-65(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"High levels of RNA editing in a vascular plant chloroplast genome: analysis of transcripts from the fern Adiantum capillus-veneris."
Wolf P.G., Rowe C.A., Hasebe M.
Gene 339:89-97(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], RNA EDITING.
Tissue: Frond.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY178864 Genomic DNA. Translation: AAP29400.2.
RefSeqNP_848069.2. NC_004766.1.

3D structure databases

ProteinModelPortalQ85FL3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID807410.

Phylogenomic databases

ProtClustDBCHL00174.

Enzyme and pathway databases

UniPathwayUPA00655; UER00711.

Family and domain databases

HAMAPMF_01395. AcetylCoA_CT_beta.
InterProIPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR011762. COA_CT_N.
[Graphical view]
PfamPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PRINTSPR01070. ACCCTRFRASEB.
TIGRFAMsTIGR00515. accD. 1 hit.
PROSITEPS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACCD_ADICA
AccessionPrimary (citable) accession number: Q85FL3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: August 16, 2004
Last modified: February 19, 2014
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways