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Biotin carboxylase, chloroplastic (EC 6.3.4.14) (Acetyl-CoA carboxylase subunit A) (ACC) (EC 6.4.1.2)

 ACCC_ARATH              Reviewed;         537 AA.
O04983; P93650; Q9C5F8;
02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
22-NOV-2017, entry version 140.
RecName: Full=Biotin carboxylase, chloroplastic;
EC=6.3.4.14 {ECO:0000269|PubMed:9414551};
AltName: Full=Acetyl-CoA carboxylase subunit A;
Short=ACC;
EC=6.4.1.2 {ECO:0000269|PubMed:9414551};
Flags: Precursor;
Name=CAC2; OrderedLocusNames=At5g35360; ORFNames=T26D22.8;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=9349276; DOI=10.1023/A:1005881006620;
Bao X., Shorrosh B.S., Ohlrogge J.B.;
"Isolation and characterization of an Arabidopsis biotin carboxylase
gene and its promoter.";
Plant Mol. Biol. 35:539-550(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC
ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND TISSUE
SPECIFICITY.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=9414551; DOI=10.1104/pp.115.4.1371;
Sun J., Ke J., Johnson J.L., Nikolau B.J., Wurtele E.S.;
"Biochemical and molecular biological characterization of CAC2, the
Arabidopsis thaliana gene coding for the biotin carboxylase subunit of
the plastidic acetyl-coenzyme A carboxylase.";
Plant Physiol. 115:1371-1383(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
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.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=10759501; DOI=10.1104/pp.122.4.1057;
Ke J., Wen T.N., Nikolau B.J., Wurtele E.S.;
"Coordinate regulation of the nuclear and plastidic genes coding for
the subunits of the heteromeric acetyl-coenzyme A carboxylase.";
Plant Physiol. 122:1057-1071(2000).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=18431481; DOI=10.1371/journal.pone.0001994;
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,
Sun Q., van Wijk K.J.;
"Sorting signals, N-terminal modifications and abundance of the
chloroplast proteome.";
PLoS ONE 3:E1994-E1994(2008).
-!- 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.
{ECO:0000269|PubMed:9414551}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000269|PubMed:9414551}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000269|PubMed:9414551}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.3 mM for biotin {ECO:0000269|PubMed:9414551};
KM=88 mM for bicarbonate {ECO:0000269|PubMed:9414551};
Vmax=16 nmol/min/mg enzyme {ECO:0000269|PubMed:9414551};
pH dependence:
Optimum pH is 8.3-8.9. {ECO:0000269|PubMed:9414551};
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: 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). {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:18431481}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=O04983-1; Sequence=Displayed;
-!- 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.
{ECO:0000269|PubMed:10759501, ECO:0000269|PubMed:9349276,
ECO:0000269|PubMed:9414551}.
-!- SEQUENCE CAUTION:
Sequence=CAA70282.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Y09061; CAA70282.1; ALT_SEQ; Genomic_DNA.
EMBL; U90879; AAC09008.1; -; mRNA.
EMBL; U91414; AAC09009.1; -; Genomic_DNA.
EMBL; AB025636; BAB11486.1; -; Genomic_DNA.
EMBL; AF058826; AAC13611.1; -; Genomic_DNA.
EMBL; CP002688; AED93956.1; -; Genomic_DNA.
EMBL; AF360279; AAK25989.1; -; mRNA.
EMBL; AY142630; AAN13088.1; -; mRNA.
EMBL; AY085968; AAM63178.1; -; mRNA.
PIR; T01180; T01180.
RefSeq; NP_198386.1; NM_122927.4. [O04983-1]
UniGene; At.22848; -.
UniGene; At.70066; -.
ProteinModelPortal; O04983; -.
SMR; O04983; -.
BioGrid; 18751; 5.
IntAct; O04983; 1.
STRING; 3702.AT5G35360.3; -.
PaxDb; O04983; -.
PRIDE; O04983; -.
EnsemblPlants; AT5G35360.1; AT5G35360.1; AT5G35360. [O04983-1]
GeneID; 833497; -.
Gramene; AT5G35360.1; AT5G35360.1; AT5G35360.
KEGG; ath:AT5G35360; -.
Araport; AT5G35360; -.
eggNOG; ENOG410IU5C; Eukaryota.
eggNOG; COG0439; LUCA.
HOGENOM; HOG000008988; -.
InParanoid; O04983; -.
KO; K01961; -.
PhylomeDB; O04983; -.
BioCyc; ARA:AT5G35360-MONOMER; -.
Reactome; R-ATH-196780; Biotin transport and metabolism.
Reactome; R-ATH-70263; Gluconeogenesis.
UniPathway; UPA00655; UER00711.
PRO; PR:O04983; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; O04983; baseline and differential.
Genevisible; O04983; AT.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52440; SSF52440; 1.
TIGRFAMs; TIGR00514; accC; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00866; CPSASE_1; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Biotin; Chloroplast;
Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism;
Ligase; Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese;
Metal-binding; Nucleotide-binding; Plastid; Reference proteome;
Transit peptide.
TRANSIT 1 71 Chloroplast. {ECO:0000305}.
CHAIN 72 537 Biotin carboxylase, chloroplastic.
/FTId=PRO_0000391772.
DOMAIN 192 389 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
NP_BIND 220 281 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
ACT_SITE 364 364 {ECO:0000250}.
METAL 347 347 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 360 360 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 360 360 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 362 362 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
BINDING 188 188 ATP. {ECO:0000250}.
BINDING 272 272 ATP. {ECO:0000250}.
BINDING 307 307 ATP. {ECO:0000250}.
CONFLICT 181 181 S -> T (in Ref. 1; CAA70282).
{ECO:0000305}.
CONFLICT 230 230 K -> T (in Ref. 1; CAA70282).
{ECO:0000305}.
CONFLICT 314 314 Missing (in Ref. 1; CAA70282).
{ECO:0000305}.
CONFLICT 447 447 D -> N (in Ref. 6; AAK25989).
{ECO:0000305}.
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


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