ACC2_ARATH
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 03-AUG-2022, entry version 69.
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; 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=7551584; DOI=10.1093/oxfordjournals.pcp.a078822;
RA Yanai Y., Kawasaki T., Shimada H., Wurtele E.S., Nikolau B.J., Ichikawa N.;
RT "Genomic organization of 251 kDa acetyl-CoA carboxylase genes in
RT Arabidopsis: tandem gene duplication has made two differentially expressed
RT 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., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 reference
RT 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., Caboche M.,
RA Lepiniec L., Rochat C.;
RT "Multifunctional acetyl-CoA carboxylase 1 is essential for very long chain
RT fatty acid elongation and embryo development in Arabidopsis.";
RL Plant J. 33:75-86(2003).
CC -!- FUNCTION: Multifunctional enzyme that catalyzes the carboxylation of
CC acetyl-CoA, forming malonyl-CoA, which is used in the plastid for fatty
CC acid synthesis and in the cytosol in various biosynthetic pathways
CC including fatty acid elongation. {ECO:0000250|UniProtKB:Q38970}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, 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] + 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:0000250|UniProtKB:O04983};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01066};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-
CC ProRule:PRU00969};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC 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};
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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 AlphaFoldDB; F4I1L3; -.
DR SMR; F4I1L3; -.
DR BioGRID; 25754; 1.
DR STRING; 3702.AT1G36180.1; -.
DR iPTMnet; F4I1L3; -.
DR PaxDb; F4I1L3; -.
DR PRIDE; F4I1L3; -.
DR ProteomicsDB; 244567; -. [F4I1L3-1]
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 HOGENOM; CLU_000395_5_2_1; -.
DR InParanoid; F4I1L3; -.
DR OMA; ERIKEWH; -.
DR OrthoDB; 156081at2759; -.
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; IBA:GO_Central.
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; Cytoplasm;
KW Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Manganese; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..2355
FT /note="Acetyl-CoA carboxylase 2"
FT /id="PRO_0000412212"
FT DOMAIN 138..645
FT /note="Biotin carboxylation"
FT DOMAIN 291..485
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 772..846
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 1593..1932
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 1936..2251
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1593..2251
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT ACT_SITE 458
FT /evidence="ECO:0000250"
FT BINDING 317..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 440
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 440
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 454
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 454
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 456
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 1841
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 2142
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 2144
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 813
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 1133
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38970"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q38970"
FT CONFLICT 1855
FT /note="R -> K (in Ref. 1; AAG40564)"
FT /evidence="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
