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
//