Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

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Q31796 (ACCD_ANTFO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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 on

Plastid; Chloroplast

Organism

Anthoceros formosae (Hornwort)

Taxonomic identifier

48387 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Anthocerotophyta › Anthocerotopsida › Anthocerotidae › Anthocerotales › Anthocerotaceae › Anthoceros

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Plastid › chloroplast 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

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Chloroplast Plastid
Coding sequence diversity	RNA editing
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Ligase
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP malonyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 313

313

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic HAMAP-Rule MF_01395

PRO_0000199779

Regions

Zinc finger

51 – 73

C4-type By similarity

Sites

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q31796 [UniParc].

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

313

35,272

        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' referencesShow '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.
PIR	S71147.
RefSeq	NP_777422.1. NC_004543.1.
3D structure databases
ProteinModelPortal	Q31796.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2553479.
Phylogenomic databases
ProtClustDB	CHL00174.
Enzyme and pathway databases
UniPathway	UPA00655; UER00711.
Family and domain databases
HAMAP	MF_01395. AcetylCoA_CT_beta.
InterPro	IPR000438. Acetyl_CoA_COase_Trfase_b_su. IPR000022. Carboxyl_trans. IPR011762. COA_CT_N. [Graphical view]
Pfam	PF01039. Carboxyl_trans. 1 hit. [Graphical view]
PRINTS	PR01070. ACCCTRFRASEB.
TIGRFAMs	TIGR00515. accD. 1 hit.
PROSITE	PS50980. COA_CT_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCD_ANTFO

Accession

Primary (citable) accession number: Q31796

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 28, 2003
Last modified:	April 3, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents