ACCC_ARATH
ID ACCC_ARATH Reviewed; 537 AA.
AC O04983; P93650; Q9C5F8;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Biotin carboxylase, chloroplastic;
DE EC=6.3.4.14 {ECO:0000269|PubMed:9414551};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000305};
DE Flags: Precursor;
GN Name=CAC2; OrderedLocusNames=At5g35360; ORFNames=T26D22.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9349276; DOI=10.1023/a:1005881006620;
RA Bao X., Shorrosh B.S., Ohlrogge J.B.;
RT "Isolation and characterization of an Arabidopsis biotin carboxylase gene
RT and its promoter.";
RL Plant Mol. Biol. 35:539-550(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=9414551; DOI=10.1104/pp.115.4.1371;
RA Sun J., Ke J., Johnson J.L., Nikolau B.J., Wurtele E.S.;
RT "Biochemical and molecular biological characterization of CAC2, the
RT Arabidopsis thaliana gene coding for the biotin carboxylase subunit of the
RT plastidic acetyl-coenzyme A carboxylase.";
RL Plant Physiol. 115:1371-1383(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10759501; DOI=10.1104/pp.122.4.1057;
RA Ke J., Wen T.N., Nikolau B.J., Wurtele E.S.;
RT "Coordinate regulation of the nuclear and plastidic genes coding for the
RT subunits of the heteromeric acetyl-coenzyme A carboxylase.";
RL Plant Physiol. 122:1057-1071(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC carboxylase complex; first, biotin carboxylase catalyzes the
CC carboxylation of the carrier protein and then the transcarboxylase
CC transfers the carboxyl group to form malonyl-CoA.
CC {ECO:0000269|PubMed:9414551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000269|PubMed:9414551};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00969};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00969};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00969};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 mM for biotin {ECO:0000269|PubMed:9414551};
CC KM=88 mM for bicarbonate {ECO:0000269|PubMed:9414551};
CC Vmax=16 nmol/min/mg enzyme {ECO:0000269|PubMed:9414551};
CC pH dependence:
CC Optimum pH is 8.3-8.9. {ECO:0000269|PubMed:9414551};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein, biotin carboxylase and two subunits each of
CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O04983-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Accumulates in fatty acids synthesizing tissues.
CC Mostly expressed in siliques, developing leaves, and flowers, present
CC in roots and embryos (especially at torpedo stage), and, to a lower
CC extent, in mature leaves. {ECO:0000269|PubMed:10759501,
CC ECO:0000269|PubMed:9349276, ECO:0000269|PubMed:9414551}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA70282.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y09061; CAA70282.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U90879; AAC09008.1; -; mRNA.
DR EMBL; U91414; AAC09009.1; -; Genomic_DNA.
DR EMBL; AB025636; BAB11486.1; -; Genomic_DNA.
DR EMBL; AF058826; AAC13611.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93956.1; -; Genomic_DNA.
DR EMBL; AF360279; AAK25989.1; -; mRNA.
DR EMBL; AY142630; AAN13088.1; -; mRNA.
DR EMBL; AY085968; AAM63178.1; -; mRNA.
DR PIR; T01180; T01180.
DR RefSeq; NP_198386.1; NM_122927.4. [O04983-1]
DR AlphaFoldDB; O04983; -.
DR SMR; O04983; -.
DR BioGRID; 18751; 5.
DR IntAct; O04983; 1.
DR STRING; 3702.AT5G35360.3; -.
DR MetOSite; O04983; -.
DR PaxDb; O04983; -.
DR PRIDE; O04983; -.
DR ProteomicsDB; 244341; -. [O04983-1]
DR EnsemblPlants; AT5G35360.1; AT5G35360.1; AT5G35360. [O04983-1]
DR GeneID; 833497; -.
DR Gramene; AT5G35360.1; AT5G35360.1; AT5G35360. [O04983-1]
DR KEGG; ath:AT5G35360; -.
DR Araport; AT5G35360; -.
DR eggNOG; KOG0238; Eukaryota.
DR InParanoid; O04983; -.
DR OMA; ITHFHTP; -.
DR PhylomeDB; O04983; -.
DR BioCyc; ARA:AT5G35360-MON; -.
DR BioCyc; MetaCyc:AT5G35360-MON; -.
DR UniPathway; UPA00655; UER00711.
DR PRO; PR:O04983; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O04983; baseline and differential.
DR Genevisible; O04983; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR00514; accC; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Biotin; Chloroplast;
KW Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..71
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 72..537
FT /note="Biotin carboxylase, chloroplastic"
FT /id="PRO_0000391772"
FT DOMAIN 192..389
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT ACT_SITE 364
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 236..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 272..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 309
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 360
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 360
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 362
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 364
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 367
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 410
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 410
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT CONFLICT 181
FT /note="S -> T (in Ref. 1; CAA70282)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="K -> T (in Ref. 1; CAA70282)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="Missing (in Ref. 1; CAA70282)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="D -> N (in Ref. 6; AAK25989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 58387 MW; CB57C973A2A735C8 CRC64;
MDASMITNSK SITSPPSLAL GKSGGGGVIR SSLCNLMMPS KVNFPRQRTQ TLKVSQKKLK
RATSGGLGVT CSGGDKILVA NRGEIAVRVI RTAHEMGIPC VAVYSTIDKD ALHVKLADEA
VCIGEAPSNQ SYLVIPNVLS AAISRGCTML HPGYGFLSEN ALFVEMCRDH GINFIGPNPD
SIRVMGDKAT ARETMKNAGV PTVPGSDGLL QSTEEAVRVA NEIGFPVMIK ATAGGGGRGM
RLAKEPGEFV KLLQQAKSEA AAAFGNDGCY LEKFVQNPRH IEFQVLADKF GNVVHFGERD
CSIQRRNQKL LEEAPSPALT AELRKAMGDA AVAAAASIGY IGVGTVEFLL DERGSFYFME
MNTRIQVEHP VTEMIYSVDL IEEQIRVAMG EKLRYKQEDI VLRGHSIECR INAEDPFKGF
RPGPGRITSY LPSGGPFVRM DSHVYSDYVV PPSYDSLLGK LIVWAPTREK AIERMKRALN
DTIITGVPTT INYHKLILDV EDFKNGKVDT AFIVKHEEEL AEPQEIVAVK DLTNATV
