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O04983

- ACCC_ARATH

UniProt

O04983 - ACCC_ARATH

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Protein

Biotin carboxylase, chloroplastic

Gene

CAC2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].
ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

Cofactori

Binds 2 magnesium or manganese ions per subunit.By similarity

Kineticsi

  1. KM=2.3 mM for biotin1 Publication
  2. KM=88 mM for bicarbonate1 Publication

Vmax=16 nmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.3-8.9.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei188 – 1881ATPBy similarity
Binding sitei272 – 2721ATPBy similarity
Binding sitei307 – 3071ATPBy similarity
Metal bindingi347 – 3471Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi360 – 3601Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi360 – 3601Magnesium or manganese 2PROSITE-ProRule annotation
Metal bindingi362 – 3621Magnesium or manganese 2PROSITE-ProRule annotation
Active sitei364 – 3641By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi220 – 28162ATPPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. acetyl-CoA carboxylase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. biotin carboxylase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Biotin, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G35360-MONOMER.
ARA:GQT-2157-MONOMER.
ARA:GQT-2739-MONOMER.
ReactomeiREACT_185257. Defective HLCS causes multiple carboxylase deficiency.
REACT_187915. Biotin transport and metabolism.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin carboxylase, chloroplastic (EC:6.3.4.14)
Alternative name(s):
Acetyl-CoA carboxylase subunit A (EC:6.4.1.2)
Short name:
ACC
Gene namesi
Name:CAC2
Ordered Locus Names:At5g35360
ORF Names:T26D22.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G35360.

Subcellular locationi

Plastidchloroplast 3 Publications

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7070ChloroplastSequence AnalysisAdd
BLAST
Chaini71 – 537467Biotin carboxylase, chloroplasticPRO_0000391772Add
BLAST

Proteomic databases

PaxDbiO04983.
PRIDEiO04983.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

GenevestigatoriO04983.

Interactioni

Subunit structurei

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).Curated

Protein-protein interaction databases

BioGridi18751. 5 interactions.
IntActiO04983. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliO04983.
SMRiO04983. Positions 75-513.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini192 – 389198ATP-graspPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0439.
HOGENOMiHOG000008988.
InParanoidiO04983.
KOiK01961.
PhylomeDBiO04983.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR004549. 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]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR00514. accC. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O04983) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDASMITNSK SITSPPSLAL GKSGGGGVIR SSLCNLMMPS KVNFPRQRTQ
60 70 80 90 100
TLKVSQKKLK RATSGGLGVT CSGGDKILVA NRGEIAVRVI RTAHEMGIPC
110 120 130 140 150
VAVYSTIDKD ALHVKLADEA VCIGEAPSNQ SYLVIPNVLS AAISRGCTML
160 170 180 190 200
HPGYGFLSEN ALFVEMCRDH GINFIGPNPD SIRVMGDKAT ARETMKNAGV
210 220 230 240 250
PTVPGSDGLL QSTEEAVRVA NEIGFPVMIK ATAGGGGRGM RLAKEPGEFV
260 270 280 290 300
KLLQQAKSEA AAAFGNDGCY LEKFVQNPRH IEFQVLADKF GNVVHFGERD
310 320 330 340 350
CSIQRRNQKL LEEAPSPALT AELRKAMGDA AVAAAASIGY IGVGTVEFLL
360 370 380 390 400
DERGSFYFME MNTRIQVEHP VTEMIYSVDL IEEQIRVAMG EKLRYKQEDI
410 420 430 440 450
VLRGHSIECR INAEDPFKGF RPGPGRITSY LPSGGPFVRM DSHVYSDYVV
460 470 480 490 500
PPSYDSLLGK LIVWAPTREK AIERMKRALN DTIITGVPTT INYHKLILDV
510 520 530
EDFKNGKVDT AFIVKHEEEL AEPQEIVAVK DLTNATV
Length:537
Mass (Da):58,387
Last modified:July 1, 1997 - v1
Checksum:iCB57C973A2A735C8
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811S → T in CAA70282. (PubMed:9349276)Curated
Sequence conflicti230 – 2301K → T in CAA70282. (PubMed:9349276)Curated
Sequence conflicti314 – 3141Missing in CAA70282. (PubMed:9349276)Curated
Sequence conflicti447 – 4471D → N in AAK25989. (PubMed:14593172)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiT01180.
RefSeqiNP_198386.1. NM_122927.3. [O04983-1]
UniGeneiAt.22848.
At.70066.

Genome annotation databases

EnsemblPlantsiAT5G35360.1; AT5G35360.1; AT5G35360. [O04983-1]
GeneIDi833497.
KEGGiath:AT5G35360.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi T01180.
RefSeqi NP_198386.1. NM_122927.3. [O04983-1 ]
UniGenei At.22848.
At.70066.

3D structure databases

ProteinModelPortali O04983.
SMRi O04983. Positions 75-513.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 18751. 5 interactions.
IntActi O04983. 1 interaction.

Proteomic databases

PaxDbi O04983.
PRIDEi O04983.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G35360.1 ; AT5G35360.1 ; AT5G35360 . [O04983-1 ]
GeneIDi 833497.
KEGGi ath:AT5G35360.

Organism-specific databases

TAIRi AT5G35360.

Phylogenomic databases

eggNOGi COG0439.
HOGENOMi HOG000008988.
InParanoidi O04983.
KOi K01961.
PhylomeDBi O04983.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
BioCyci ARA:AT5G35360-MONOMER.
ARA:GQT-2157-MONOMER.
ARA:GQT-2739-MONOMER.
Reactomei REACT_185257. Defective HLCS causes multiple carboxylase deficiency.
REACT_187915. Biotin transport and metabolism.

Miscellaneous databases

PROi O04983.

Gene expression databases

Genevestigatori O04983.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProi IPR004549. 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 ]
Pfami PF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view ]
SMARTi SM00878. Biotin_carb_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsi TIGR00514. accC. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiACCC_ARATH
AccessioniPrimary (citable) accession number: O04983
Secondary accession number(s): P93650, Q9C5F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3