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O04983 (ACCC_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biotin carboxylase, chloroplastic

EC=6.3.4.14
Alternative name(s):
Acetyl-CoA carboxylase subunit A
Short name=ACC
EC=6.4.1.2
Gene names
Name:CAC2
Ordered Locus Names:At5g35360
ORF Names:T26D22.8
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. Ref.2

Catalytic activity

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

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

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity. Ref.2

Pathway

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

Subunit structure

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

Subcellular location

Plastidchloroplast Ref.9 Ref.10 Ref.11.

Tissue specificity

Accumulates in fatty acids synthesizing tissues. Mostly expressed in siliques, developing leaves, and flowers, present in roots and embryos (especially at torpedo stage), and, to a lower extent, in mature leaves. Ref.1 Ref.2 Ref.8

Sequence similarities

Contains 1 ATP-grasp domain.

Biophysicochemical properties

Kinetic parameters:

KM=2.3 mM for biotin Ref.2

KM=88 mM for bicarbonate

Vmax=16 nmol/min/mg enzyme

pH dependence:

Optimum pH is 8.3-8.9.

Sequence caution

The sequence CAA70282.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: O04983-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7070Chloroplast Potential
Chain71 – 537467Biotin carboxylase, chloroplastic
PRO_0000391772

Regions

Domain192 – 389198ATP-grasp
Nucleotide binding220 – 28162ATP By similarity

Sites

Active site3641 By similarity
Metal binding3471Magnesium or manganese 1 By similarity
Metal binding3601Magnesium or manganese 1 By similarity
Metal binding3601Magnesium or manganese 2 By similarity
Metal binding3621Magnesium or manganese 2 By similarity
Binding site1881ATP By similarity
Binding site2721ATP By similarity
Binding site3071ATP By similarity

Experimental info

Sequence conflict1811S → T in CAA70282. Ref.1
Sequence conflict2301K → T in CAA70282. Ref.1
Sequence conflict3141Missing in CAA70282. Ref.1
Sequence conflict4471D → N in AAK25989. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: CB57C973A2A735C8

FASTA53758,387
        10         20         30         40         50         60 
MDASMITNSK SITSPPSLAL GKSGGGGVIR SSLCNLMMPS KVNFPRQRTQ TLKVSQKKLK 

        70         80         90        100        110        120 
RATSGGLGVT CSGGDKILVA NRGEIAVRVI RTAHEMGIPC VAVYSTIDKD ALHVKLADEA 

       130        140        150        160        170        180 
VCIGEAPSNQ SYLVIPNVLS AAISRGCTML HPGYGFLSEN ALFVEMCRDH GINFIGPNPD 

       190        200        210        220        230        240 
SIRVMGDKAT ARETMKNAGV PTVPGSDGLL QSTEEAVRVA NEIGFPVMIK ATAGGGGRGM 

       250        260        270        280        290        300 
RLAKEPGEFV KLLQQAKSEA AAAFGNDGCY LEKFVQNPRH IEFQVLADKF GNVVHFGERD 

       310        320        330        340        350        360 
CSIQRRNQKL LEEAPSPALT AELRKAMGDA AVAAAASIGY IGVGTVEFLL DERGSFYFME 

       370        380        390        400        410        420 
MNTRIQVEHP VTEMIYSVDL IEEQIRVAMG EKLRYKQEDI VLRGHSIECR INAEDPFKGF 

       430        440        450        460        470        480 
RPGPGRITSY LPSGGPFVRM DSHVYSDYVV PPSYDSLLGK LIVWAPTREK AIERMKRALN 

       490        500        510        520        530 
DTIITGVPTT INYHKLILDV EDFKNGKVDT AFIVKHEEEL AEPQEIVAVK DLTNATV 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of an Arabidopsis biotin carboxylase gene and its promoter."
Bao X., Shorrosh B.S., Ohlrogge J.B.
Plant Mol. Biol. 35:539-550(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Biochemical and molecular biological characterization of CAC2, the Arabidopsis thaliana gene coding for the biotin carboxylase subunit of the plastidic acetyl-coenzyme A carboxylase."
Sun J., Ke J., Johnson J.L., Nikolau B.J., Wurtele E.S.
Plant Physiol. 115:1371-1383(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, TISSUE SPECIFICITY.
Strain: cv. Columbia and cv. Landsberg erecta.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. XI."
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[7]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Coordinate regulation of the nuclear and plastidic genes coding for the subunits of the heteromeric acetyl-coenzyme A carboxylase."
Ke J., Wen T.N., Nikolau B.J., Wurtele E.S.
Plant Physiol. 122:1057-1071(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
Strain: cv. Columbia.
[9]"Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis."
Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S.
J. Proteome Res. 2:413-425(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts."
Peltier J.-B., Cai Y., Sun Q., Zabrouskov V., Giacomelli L., Rudella A., Ytterberg A.J., Rutschow H., van Wijk K.J.
Mol. Cell. Proteomics 5:114-133(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09061 Genomic DNA. Translation: CAA70282.1. Sequence problems.
U90879 mRNA. Translation: AAC09008.1.
U91414 Genomic DNA. Translation: AAC09009.1.
AB025636 Genomic DNA. Translation: BAB11486.1.
AF058826 Genomic DNA. Translation: AAC13611.1.
CP002688 Genomic DNA. Translation: AED93956.1.
AF360279 mRNA. Translation: AAK25989.1.
AY142630 mRNA. Translation: AAN13088.1.
AY085968 mRNA. Translation: AAM63178.1.
PIRT01180.
RefSeqNP_198386.1. NM_122927.3. [O04983-1]
UniGeneAt.22848.
At.70066.

3D structure databases

ProteinModelPortalO04983.
SMRO04983. Positions 75-513.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid18751. 5 interactions.
IntActO04983. 1 interaction.

Proteomic databases

PaxDbO04983.
PRIDEO04983.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G35360.1; AT5G35360.1; AT5G35360. [O04983-1]
GeneID833497.
KEGGath:AT5G35360.

Organism-specific databases

TAIRAT5G35360.

Phylogenomic databases

eggNOGCOG0439.
HOGENOMHOG000008988.
InParanoidO04983.
KOK01961.
PhylomeDBO04983.

Enzyme and pathway databases

BioCycARA:AT5G35360-MONOMER.
ARA:GQT-2157-MONOMER.
ARA:GQT-2739-MONOMER.
UniPathwayUPA00655; UER00711.

Gene expression databases

GenevestigatorO04983.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR004549. Acetyl_CoA_COase_biotin_COase.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR00514. accC. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROO04983.

Entry information

Entry nameACCC_ARATH
AccessionPrimary (citable) accession number: O04983
Secondary accession number(s): P93650, Q9C5F8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: July 1, 1997
Last modified: June 11, 2014
This is version 112 of the entry and version 1 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names