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Database: UniProt
Entry: B2ZGL2_WHEAT
LinkDB: B2ZGL2_WHEAT
Original site: B2ZGL2_WHEAT 
ID   B2ZGL2_WHEAT            Unreviewed;      2311 AA.
AC   B2ZGL2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE            EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN   Name=Acc-1 {ECO:0000313|EMBL:ACD46683.1};
GN   ORFNames=CFC21_015064 {ECO:0000313|EMBL:KAF6998991.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EMBL:ACD46683.1};
RN   [1] {ECO:0000313|EMBL:ACD46683.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18599450; DOI=10.1073/pnas.0803981105;
RA   Chalupska D., Lee H.Y., Faris J.D., Evrard A., Chalhoub B., Haselkorn R.,
RA   Gornicki P.;
RT   "Acc homoeoloci and the evolution of wheat genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:9691-9696(2008).
RN   [2] {ECO:0000313|EMBL:KAF6998991.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF6998991.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [3] {ECO:0000313|EnsemblPlants:TraesCS2A02G069400.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS2A02G069400.1};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [4] {ECO:0000313|EnsemblPlants:TraesCS2A02G069400.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [5] {ECO:0000313|EMBL:KAF6998991.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF6998991.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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DR   EMBL; EU660900; ACD46683.1; -; Genomic_DNA.
DR   EMBL; CM022214; KAF6998991.1; -; Genomic_DNA.
DR   SMR; B2ZGL2; -.
DR   STRING; 4565.B2ZGL2; -.
DR   PaxDb; 4565-Traes_2AS_5A5258192-1; -.
DR   EnsemblPlants; TraesCS2A02G069400.1; TraesCS2A02G069400.1; TraesCS2A02G069400.
DR   Gramene; TraesCS2A02G069400.1; TraesCS2A02G069400.1; TraesCS2A02G069400.
DR   Gramene; TraesCS2A03G0134700.1; TraesCS2A03G0134700.1.CDS; TraesCS2A03G0134700.
DR   Gramene; TraesKAR2A01G0028100.1; cds.TraesKAR2A01G0028100.1; TraesKAR2A01G0028100.
DR   HOGENOM; CLU_000395_5_2_1; -.
DR   OMA; EEPILRH; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000019116; Chromosome 2A.
DR   Proteomes; UP000815260; Chromosome 2A.
DR   ExpressionAtlas; B2ZGL2; baseline and differential.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR   Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR   InterPro; IPR049076; ACCA.
DR   InterPro; IPR049074; ACCA_BT.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
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; 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   PANTHER; PTHR45728:SF4; ACETYL-COA CARBOXYLASE 2; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF21385; ACCA_BT; 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; SSF52096; ClpP/crotonase; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000019116}.
FT   DOMAIN          131..638
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          284..478
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          765..839
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1551..1886
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          1890..2206
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          27..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2311 AA;  254949 MW;  967AEB540BFA7BF2 CRC64;
     MGSTHLPIVG FNASTTPSLS TIRPVNSAGA AFQPSAPSRT SKKKSRRVQS LRDGGDGGVS
     DPNQSIRHGL AGIIDLPKEG TSAPEVDISH GSEEPRGSYQ MNGILNEAHN GRHASLSKVV
     EFCTALGGKT PIHSVLVANN GMAAAKFMRS VRTWANETFG SEKAIQLIAM ATPEDMRINA
     EHIRIADQFV EVPGGTNNNN YANVQLIVEI AVRTGVSAVW PGWGHASENP ELPDALNANG
     IVFLGPPSSS MNALGDKVGS ALIAQAAGVP TLPWSGSQVE IPLEVCLDSI PAEMYRKACV
     STTEEALASC QMIGYPAMIK ASWGGGGKGI RKVNNDDDVR ALFKQVQGEV PGSPIFIMRL
     ASQSRHLEVQ LLCDQYGNVA ALHSRDCSVQ RRHQKIIEEG PVTVAPRETV KELEQAARRL
     AKAVGYVGAA TVEYLYSMET GEYYFLELNP RLQVEHPVTE WIAEVNLPAA QVAVGMGIPL
     WQVPEIRRFY GMDNGGGYDI WRTTAALATP FNFDEVDSQW PKGHCVAVRI TSEDPDDGFK
     PTGGKVKEIS FKSKPNVWAY FSVKSGGGIH EFADSQFGHV FAYGVSRAAA ITNMSLALKE
     IQIRGEIHSN VDYTVDLLNA SDFKENRIHT GWLDNRIAMR VQAERPPWYI SVVGGALYKT
     ITSNTDTVSE YVSYLVKGQI PPKHISLVHS TVSLNIEESK YTIETIRSGQ GSYRLRMNGS
     VIEANVQTLC DGGLLMQLDG NSHVIYAEEE AGGTRLLIDG KTCLLQNDHD PSRLLAETPC
     KLLRFLVADG AHVEADVPYA EVEVMKMCMP LLSPAAGVIN VLLSEGQPMQ AGDLIARLDL
     DDPSAVKRAE PFNGSFPEMS LPIAASGQVH KRCATSLNAA RMVLAGYDHP INKVVQDLVS
     CLDAPELPFL QWEELMSVLA TRLPRLLKSE LEGKYSEYKL NVGHGKSKDF PSKMLREIIE
     ENLAHGSEKE IATNERLVEP LMSLLKSYEG GRESHAHFIV KSLFEDYLSV EELFSDGIQS
     DVIERLRQQH SKDLQKVVDI VLSHQGVRNK TKLILTLMEK LVYPNPAAYK DQLTRFSSLN
     HKRYYKLALK ASELLEQTKL SELRTSIARS LSELEMFTEE RTAISEIMGD LVTAPLPVED
     ALVSLFDCSD HTLQQRVIET YISRLYQPHL VKDSIQLKYQ ESGVIALWEF AEAHSEKRLG
     AMVIVKSLES VSAAIGAALK DTSRYASSEG NIMHIALLGA DNQMHGTEDS GDNDQAQVRI
     DKLSATLEQN TVTADLCDAG VKVISCIVQR DGALMPMRHT FLLSDEKLCY EEEPVLRHVE
     PPLSALLELG KLKVKGYNEV KYTPSRDRQW NIYTLRNTEN PKMLHRVFFR TLVRQPGASN
     KFTSGHISDV EVGGAEESLS FTSSSILRSL MTAIEELELH AIRTGHSHMF LCILKEQKLL
     DLVPVSGNKV VDIGQDEATA CSLLKEMALQ IHELVGARMH HLSVCQWEVK LKLDSDGPAS
     GTWRVVTTNV TSHTCTVDIY REVEDTESQK LVYHSAPSSS GPLHGVALNT PYQPLSVIDL
     KRCSARNNRT TYCYDFPLAF ETAVQKSWSN ISSDNNRCYV KATELVFAQK NGSWGTPVIP
     MERPAGLNDI GMVAWILDMS TPEYPNGRQI VVIANDITFR AGSFGPREDA FFETVTNLAC
     ERKLPLIYLA ANSGARIGIA DEVKSCFRVG WSDDGSPERG FQYIYLTEED HARISTSVIA
     HKMQLDNGEI RWVIDSVVGK EDGLGVENIH GSAAIASAYS RAYEETFTLT FVTGRTVGIG
     AYLARLGIRC IQRTDQPIIL TGFSALNKLL GREVYSSHMQ LGGPKIMATN GVVHLTVSDD
     LEGVSNILRW LSYVPANIGG PLPITKSLDP PDRPVAYIPE NTCDPRAAIS GIDDSQGKWL
     GGMFDKDSFV ETFEGWAKSV VTGRAKLGGI PVGVIAVETQ TMMQLIPADP GQLDSHERSV
     PRAGQVWFPD SATKTAQAML DFNREGLPLF ILANWRGFSG GQRDLFEGIL QAGSTIVENL
     RTYNQPAFVY IPKAAELRGG AWVVIDSKIN PDRIEFYAER TAKGNVLEPQ GLIEIKFRSE
     ELQECMGRLD PELINLKAKL LGAKHENGSL SESESLQKSI EARKKQLLPL YTQIAVRFAE
     LHDTSLRMAA KGVIKKVVDW KDSRSFFYKR LRRRISEDVL AKEIRGVSGK QFSHQSAIEL
     IQKWYLASKG AEAASTEWDD DDAFVAWREN PENYQEYIKE LRAQRVSQLL SDVADSSPDL
     EALPQGLSML LEKMDPSRRA QFVEEVKKVL K
//
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