GenomeNet

Database: UniProt
Entry: F4I1L3
LinkDB: F4I1L3
Original site: F4I1L3 
ID   ACC2_ARATH              Reviewed;        2355 AA.
AC   F4I1L3; Q9C8G0; Q9FR96;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   16-JAN-2019, entry version 57.
DE   RecName: Full=Acetyl-CoA carboxylase 2;
DE            EC=6.4.1.2;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
GN   Name=ACC2; OrderedLocusNames=At1g36180; ORFNames=F15C21.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=7551584; DOI=10.1093/oxfordjournals.pcp.a078822;
RA   Yanai Y., Kawasaki T., Shimada H., Wurtele E.S., Nikolau B.J.,
RA   Ichikawa N.;
RT   "Genomic organization of 251 kDa acetyl-CoA carboxylase genes in
RT   Arabidopsis: tandem gene duplication has made two differentially
RT   expressed isozymes.";
RL   Plant Cell Physiol. 36:779-787(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=12943542; DOI=10.1046/j.1365-313X.2003.016010.x;
RA   Baud S., Guyon V., Kronenberger J., Wuilleme S., Miquel M.,
RA   Caboche M., Lepiniec L., Rochat C.;
RT   "Multifunctional acetyl-CoA carboxylase 1 is essential for very long
RT   chain fatty acid elongation and embryo development in Arabidopsis.";
RL   Plant J. 33:75-86(2003).
CC   -!- FUNCTION: Multifunctional enzyme that catalyzes the carboxylation
CC       of acetyl-CoA, forming malonyl-CoA, which is used in the plastid
CC       for fatty acid synthesis and in the cytosol in various
CC       biosynthetic pathways including fatty acid elongation.
CC       {ECO:0000250|UniProtKB:Q38970}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000250|UniProtKB:O04983};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000250|UniProtKB:O04983};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
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=F4I1L3-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Widely expressed at low levels.
CC       {ECO:0000269|PubMed:12943542, ECO:0000269|PubMed:7551584}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG40564.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG51252.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF062308; AAG40564.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC025781; AAG51252.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31851.1; -; Genomic_DNA.
DR   PIR; E86483; E86483.
DR   RefSeq; NP_174850.4; NM_103314.5. [F4I1L3-1]
DR   UniGene; At.51973; -.
DR   ProteinModelPortal; F4I1L3; -.
DR   SMR; F4I1L3; -.
DR   BioGrid; 25754; 1.
DR   STRING; 3702.AT1G36180.1; -.
DR   iPTMnet; F4I1L3; -.
DR   PaxDb; F4I1L3; -.
DR   PRIDE; F4I1L3; -.
DR   EnsemblPlants; AT1G36180.1; AT1G36180.1; AT1G36180. [F4I1L3-1]
DR   GeneID; 840522; -.
DR   Gramene; AT1G36180.1; AT1G36180.1; AT1G36180. [F4I1L3-1]
DR   KEGG; ath:AT1G36180; -.
DR   Araport; AT1G36180; -.
DR   TAIR; locus:2013190; AT1G36180.
DR   eggNOG; KOG0368; Eukaryota.
DR   eggNOG; COG0439; LUCA.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG4799; LUCA.
DR   HOGENOM; HOG000214115; -.
DR   InParanoid; F4I1L3; -.
DR   KO; K11262; -.
DR   OMA; NYENYLV; -.
DR   OrthoDB; 156081at2759; -.
DR   Reactome; R-ATH-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-ATH-196780; Biotin transport and metabolism.
DR   Reactome; R-ATH-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
DR   Reactome; R-ATH-75105; Fatty acyl-CoA biosynthesis.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:F4I1L3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4I1L3; baseline and differential.
DR   Genevisible; F4I1L3; AT.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IMP:TAIR.
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; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Alternative splicing; ATP-binding; Biotin;
KW   Complete proteome; Cytoplasm; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN         1   2355       Acetyl-CoA carboxylase 2.
FT                                /FTId=PRO_0000412212.
FT   DOMAIN      138    645       Biotin carboxylation.
FT   DOMAIN      291    485       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      772    846       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN     1593   1932       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01136}.
FT   DOMAIN     1936   2251       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01137}.
FT   NP_BIND     317    374       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION     1593   2251       Carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01138}.
FT   ACT_SITE    458    458       {ECO:0000250}.
FT   METAL       440    440       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       454    454       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       454    454       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       456    456       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   BINDING    1841   1841       Coenzyme A. {ECO:0000250}.
FT   BINDING    2142   2142       Coenzyme A. {ECO:0000250}.
FT   BINDING    2144   2144       Coenzyme A. {ECO:0000250}.
FT   MOD_RES     813    813       N6-biotinyllysine. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   MOD_RES    1133   1133       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q38970}.
FT   MOD_RES    1293   1293       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q38970}.
FT   CONFLICT   1855   1855       R -> K (in Ref. 1; AAG40564).
FT                                {ECO:0000305}.
SQ   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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