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Acetyl-CoA carboxylase 2 (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 ACC2_ARATH              Reviewed;        2355 AA.
F4I1L3; Q9C8G0; Q9FR96;
21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
22-NOV-2017, entry version 50.
RecName: Full=Acetyl-CoA carboxylase 2;
EC=6.4.1.2;
Includes:
RecName: Full=Biotin carboxylase;
EC=6.3.4.14;
Name=ACC2; OrderedLocusNames=At1g36180; ORFNames=F15C21.2;
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=7551584; DOI=10.1093/oxfordjournals.pcp.a078822;
Yanai Y., Kawasaki T., Shimada H., Wurtele E.S., Nikolau B.J.,
Ichikawa N.;
"Genomic organization of 251 kDa acetyl-CoA carboxylase genes in
Arabidopsis: tandem gene duplication has made two differentially
expressed isozymes.";
Plant Cell Physiol. 36:779-787(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
TISSUE SPECIFICITY.
STRAIN=cv. Wassilewskija;
PubMed=12943542; DOI=10.1046/j.1365-313X.2003.016010.x;
Baud S., Guyon V., Kronenberger J., Wuilleme S., Miquel M.,
Caboche M., Lepiniec L., Rochat C.;
"Multifunctional acetyl-CoA carboxylase 1 is essential for very long
chain fatty acid elongation and embryo development in Arabidopsis.";
Plant J. 33:75-86(2003).
-!- FUNCTION: Multifunctional enzyme that catalyzes the carboxylation
of acetyl-CoA, forming malonyl-CoA, which is used in the plastid
for fatty acid synthesis and in the cytosol in various
biosynthetic pathways including fatty acid elongation.
{ECO:0000250|UniProtKB:Q38970}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000250|UniProtKB:O04983}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000250|UniProtKB:O04983}.
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
-!- 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};
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=F4I1L3-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Widely expressed at low levels.
{ECO:0000269|PubMed:12943542, ECO:0000269|PubMed:7551584}.
-!- SEQUENCE CAUTION:
Sequence=AAG40564.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAG51252.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF062308; AAG40564.1; ALT_SEQ; Genomic_DNA.
EMBL; AC025781; AAG51252.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE31851.1; -; Genomic_DNA.
PIR; E86483; E86483.
RefSeq; NP_174850.4; NM_103314.5. [F4I1L3-1]
UniGene; At.51973; -.
ProteinModelPortal; F4I1L3; -.
SMR; F4I1L3; -.
BioGrid; 25754; 1.
STRING; 3702.AT1G36180.1; -.
iPTMnet; F4I1L3; -.
PaxDb; F4I1L3; -.
PRIDE; F4I1L3; -.
EnsemblPlants; AT1G36180.1; AT1G36180.1; AT1G36180. [F4I1L3-1]
GeneID; 840522; -.
Gramene; AT1G36180.1; AT1G36180.1; AT1G36180.
KEGG; ath:AT1G36180; -.
Araport; AT1G36180; -.
TAIR; locus:2013190; AT1G36180.
eggNOG; KOG0368; Eukaryota.
eggNOG; COG0439; LUCA.
eggNOG; COG0511; LUCA.
eggNOG; COG4799; LUCA.
HOGENOM; HOG000214115; -.
InParanoid; F4I1L3; -.
KO; K11262; -.
OMA; LIVKVAR; -.
OrthoDB; EOG0936001E; -.
Reactome; R-ATH-163765; ChREBP activates metabolic gene expression.
Reactome; R-ATH-196780; Biotin transport and metabolism.
Reactome; R-ATH-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-ATH-75105; Fatty acyl-CoA biosynthesis.
UniPathway; UPA00655; UER00711.
PRO; PR:F4I1L3; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; F4I1L3; baseline and differential.
Genevisible; F4I1L3; AT.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IMP:TAIR.
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.
Gene3D; 3.30.450.40; -; 1.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR013537; AcCoA_COase_cen.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR001882; Biotin_BS.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR029016; GAF-like_dom_sf.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF08326; ACC_central; 1.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF01039; Carboxyl_trans; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52096; SSF52096; 2.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00188; BIOTIN; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS50989; COA_CT_CTER; 1.
PROSITE; PS50980; COA_CT_NTER; 1.
PROSITE; PS00867; CPSASE_2; 1.
2: Evidence at transcript level;
Allosteric enzyme; Alternative splicing; ATP-binding; Biotin;
Complete proteome; Cytoplasm; Fatty acid biosynthesis;
Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
Nucleotide-binding; Phosphoprotein; Reference proteome.
CHAIN 1 2355 Acetyl-CoA carboxylase 2.
/FTId=PRO_0000412212.
DOMAIN 138 645 Biotin carboxylation.
DOMAIN 291 485 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 772 846 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1593 1932 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 1936 2251 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 317 374 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1593 2251 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
ACT_SITE 458 458 {ECO:0000250}.
METAL 440 440 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 454 454 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 454 454 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 456 456 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
BINDING 1841 1841 Coenzyme A. {ECO:0000250}.
BINDING 2142 2142 Coenzyme A. {ECO:0000250}.
BINDING 2144 2144 Coenzyme A. {ECO:0000250}.
MOD_RES 813 813 N6-biotinyllysine. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
MOD_RES 1133 1133 Phosphothreonine.
{ECO:0000250|UniProtKB:Q38970}.
MOD_RES 1293 1293 Phosphoserine.
{ECO:0000250|UniProtKB:Q38970}.
CONFLICT 1855 1855 R -> K (in Ref. 1; AAG40564).
{ECO:0000305}.
SEQUENCE 2355 AA; 262729 MW; D3E322E33E847E0A CRC64;
MEMRALGSSC STGNGGSAPI TLTNISPWIT TVFPSTVKLR SSLRTFKGVS SRVRTFKGVS
STRVLSRTKQ QFPLFCFLNP DPISFLENDV SEAERTVVLP DGSVNGAGSV NGYHSDVVPG
RNVAEVNEFC KALGGKRPIH SILVATNGMA AVKFIRSVRT WAYETFGSEK AVKLVAMATP
EDMRINAEHI RIADQFVEVP GGTNNNNYAN VQLIVEMAEV TRVDAVWPGW GHASENPELP
DALKEKGIIF LGPPADSMIA LGDKIGSSLI AQAADVPTLP WSGSHVKIPP GRSLVTVPEE
IYKKACVYTT EEAIASCQVV GYPAMIKASW GGGGKGIRKV HNDDEVRALF KQVQGEVPGS
PIFIMKVASQ SRHLEAQLLC DQYGNVAALH SRDCSVQRRH QKIIEEGPIT VAPQETIKKL
EQAARRLAKS VNYVGAATVE YLYSMDTGEY YFLELNPRLQ VEHPVTEWIA EVNLPAAQVA
VGMGIPLWQI PEIRRFYGME HGGGYDSWRK TSVVASPFDF DEAESLRPKG HCVAVRVTSE
DPDDGFKPTS GEIQELSFKS KPNMWSYFSV KSGGGIHEFS DSQFGHVFAF GESRSVAIAN
MVLALKEIQI RGDIRTNVDY TIDLLHASDY RENKIHTGWL DSRIAMRVRA ERPPWYLSVV
GGALYKASTT SSAVVSDYVG YLEKGQIPPK HISLVHSQVS LNIEGSKYTI DVVRGGSGTY
RLRMSNSEVV AEIHTLRDGG LLMQLDGKSH VIYAKEEATG TRLLIDGRTC LLQNDHDPSK
LMAETPCKLL RYLVSDNSSI DTDTPYAEVE VMKMCMPLIS PASGVIHFKL SEGQAMQAGE
LIAKLDLDDP SAVRKAKPFR GSFPRLGLPT AISGKVHQRC AATLNAARMI LAGYDHKVDE
VLQDLLNCLD SPELPFLQWQ ECFAVLATRL PKDLRNMLEL KYKEFEIISK TSLTPDFPAK
LLKGILEAHL SSCDEKERGS LERLIEPLMS LVKSYEGGRE SHARLIVHSL FEEYLSVEEL
FNDNMLADVI ERMRQQYKKD RLKIVDIVLS HQGIIHKNKL VLRLMEQLVY PNPAAYREKL
IRFSALNHTN YSQLALKASQ LLEQTKRSEL RSNIARSLSE LEMFTEAGEN MDTPKRKSAI
SETMENLVSS SLAVEDALVG LFDHSDHTLQ RRVVETYIHR LYQPYVVKES VRMQWHQSGV
IASWEFLEHF ERKNTGPDDH EISEKGIVAK SSKRKRGTMV IIKSLQFLPS IINASLRETN
HSHCEYARAP LSGNMMHIAV VGINNQMSLL QDSGDEDQTQ ERVNKLAKIL KEEEVSLTLC
SAGVGVISCI IQRDEGRTPM RHSFHWLMEK QYYVEEPLLR HVEPPLSVYL ELDKLKGYSN
IQYSPSRDRQ WHMYSVTDRP VPIKRMFLRS LVRQTTMNDG FLLQQGQDYQ LSQTVLSMAF
TSKCILRSLM NAMEELELNA HNAAMKPDHA HMFLCILREQ QIDDLVPYPR RFEVNAEDEE
TTVETILEEA TQEIHRSVGV RMHALGVCEW EVRLWLVSSG LANGAWRVVV ANVTGRTCTV
HIYREVEATG RNSLIYHSIT KKGPLHGTLI NGQYKPLNNL DRKRLAARRS NTTYCYDFPL
AFETALELNW ASQHSGVRKP CKNRLINVKE LVFSNTEGSL GTSLIPVERP AGLNDIGMVA
WILEMSTPEF PMGRKLLIVA NDVTFKAGSF GPREDAFFLA VTELACTKKL PLIYLAANSG
ARLGVAEEVK ACFKVGWSDE VSPGNDFQYI YLSSEDYARI GSSVIAHEVK LPSGETRWVI
DTIVGKEDGL GVENLTGSGA IAGAYSRAYN ETFTLTFVSG RSVGIGAYLA RLGMRCIQRL
DQPIILTGFS TLNKLLGREV YSSHMQLGGP KIMGTNGVVH LTVSDDLEGV SAILNWLSYI
PAYVGGPLPV LAPLDPPERT VEYIPENSCD PRAAIAGIND NTGKWLGGIF DKNSFVETLE
GWARTVVTGR AKLGGIPIGV VAVETQTVMH VIPADPGQLD SHERVVPQAG QVWFPDSAAK
TAQALMDFNR EQLPLFIIAN WRGFSGGQRD LFEGILQAGS AIVENLRTYR QPVFVYIPMM
GELRGGAWVV VDSQINSDYI EMYADETARG NVLEPEGMIE IKFRRKELLE CMGRLDQTLI
NLKANIQDAK RNKAYANIEL LQKQIKTREK QLLPVYTQIA TKFAELHDTS MRMAAKGVIK
SVVEWSGSRS FFYKKLYRRI AESSLVRNIR KASGDILSYK SAMGLIQDWF RKSEIAKGKE
EAWTDDQLFF TWKDNVSNYE QKLSELRTQK LLNQLAEIGN SSDLQALPQG LANLLNKVDL
SRREELVDAI RKVLG


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