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Q31796 (ACCD_ANTFO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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
OrganismAnthoceros formosae (Hornwort)
Taxonomic identifier48387 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaAnthocerotophytaAnthocerotopsidaAnthocerotidaeAnthocerotalesAnthocerotaceaeAnthoceros

Protein attributes

Sequence length313 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 50, 59, 78, 87, 104, 132, 139, 146, 149, 160, 170, 177, 185, 198, 208, 223, 226, 228, 243, 246, 252, 260, 264, 277, 285 and 295.
The nonsense codons at positions 50, 78, 104, 260 and 264 are modified to sense codons. Ref.1 Ref.2

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic HAMAP-Rule MF_01395
PRO_0000199779

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
Q31796 [UniParc].

Last modified February 28, 2003. Version 2.
Checksum: 6881B7B5FF780126

FASTA31335,272
        10         20         30         40         50         60 
MSLMNWFEDR RKFSGLIGAF IEKATKGYIL SERRKDRHIK IDTTKGLWTR CDNCENMLYI 

        70         80         90        100        110        120 
RFLRQNKRIC EECGYHLQMS STERIESLID RGTWHPMDED MVARDALKFS DEDSYKNRVL 

       130        140        150        160        170        180 
FYQKRTGLTD AIQTGIGKLN GIPIALGVMD FQFMGGSMGS VVGEKITRLI EYGTRESMPV 

       190        200        210        220        230        240 
IIVCSSGGAR MQEGTLSLMQ MAKISAVLQI HQAQKKLLYI AILTYPTTGG VTASFGMLGD 

       250        260        270        280        290        300 
VIIAEPKAYI AFAGKRVIEQ TLRQKIPDGS QVAESLFDHG LLDLIVPRNL LRGVLSEIFE 

       310 
LYSSAPCRRS NNS 

« Hide

References

« Hide 'large scale' references
[1]"The complete nucleotide sequence of the hornwort (Anthoceros formosae) chloroplast genome: insight into the earliest land plants."
Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.
Nucleic Acids Res. 31:716-721(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], RNA EDITING.
[2]"RNA editing in hornwort chloroplasts makes more than half the genes functional."
Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.
Nucleic Acids Res. 31:2417-2423(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA EDITING.
Tissue: Thallus.
[3]"Extensive RNA editing of U to C in addition to C to U substitution in the rbcL transcripts of hornwort chloroplasts and the origin of RNA editing in green plants."
Yoshinaga K., Iinuma H., Masuzawa T., Ueda K.
Nucleic Acids Res. 24:1008-1014(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-91.
Tissue: Thallus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB086179 Genomic DNA. Translation: BAC55358.1.
AB087450 mRNA. Translation: BAC55454.1.
D43695 Genomic DNA. Translation: BAA07797.1. Sequence problems.
PIRS71147.
RefSeqNP_777422.1. NC_004543.1.

3D structure databases

ProteinModelPortalQ31796.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2553479.

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_ANTFO
AccessionPrimary (citable) accession number: Q31796
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 28, 2003
Last modified: February 19, 2014
This is version 75 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