ID B2ZGK8_AEGTA Unreviewed; 2311 AA.
AC B2ZGK8;
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:ACD46679.1};
OS Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=37682 {ECO:0000313|EMBL:ACD46679.1};
RN [1] {ECO:0000313|EMBL:ACD46679.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AL8/78 {ECO:0000313|EMBL:ACD46679.1};
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|EnsemblPlants:EMT24251}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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; EU660897; ACD46679.1; -; Genomic_DNA.
DR EnsemblPlants; EMT24251; EMT24251; F775_20574.
DR OMA; CLLLKEM; -.
DR UniPathway; UPA00655; UER00711.
DR ExpressionAtlas; B2ZGK8; baseline.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-KW.
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}.
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 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2311 AA; 254876 MW; EAC10E4E46B453DC CRC64;
MGSTHLPIVG LNASTTPSLS TIRPVNSAGA AFQPSAPSRT SKKKSRRVQS LRDGGDGGVS
DPNQSIRQGL AGIIDLPKEG TSAPEVDISH GSEEPRGSYQ MNGILNEAHN GRHASLSKVV
EFCMALGGKT PIHSVLVANN GMAAAKFMRS VRTWANETFG SEKAIQLIAM ATPEDMRINA
EHIRIADQFV EVPGGTNNNN YANVQLIVEI AVRTGVSAVW PGWGHASENP ELPDALNANG
IVFLGPPSSS MNALGDKVGS ALIAQAAGVP TLPWSGSQVE IPLEVCLDSI PADMYRKACV
STTEEALASC QMIGYPAMIK ASWGGGGKGI RKVNNDDDVR ALFKQVQGEV PGSPIFIMRL
ASQSRHLEVQ LLCDQYGNVA ALHSRDCSVQ RRHQKIIEEG PVTVAPRETV KELEQAARRL
AKAVGYVGAA TVEYLYSMET GEYYFLELNP RLQVEHPVTE WIAEVNLPAA QVAVGMGIPL
WQVPEIRRFY GMDNGGGYDI WRKTAALATP 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 QTLQQRVIET YISRLYQPHL VKDSIQLKYQ ESGVIALWEF AEAHSEKRLG
AMVIVKSLES VSAAIGAALK GTSRYASSEG NIMHIALLGA DNQMHGTEDS GDNDQAQVRI
DKLSATLEQN TVTADLRAAG VKVISCIVQR DGALMPMRHT FLLSDEKLCY EEEPVLRHVE
PPLSALLELG KLKVKGYNEV KYTPSRDRQW NIYTLRNTEN PKMLHRVFFR TLVRQPGASN
KFTSGNISDV EVGGAEESLS FTSSSILRSL MTAIEELELH AIRTGHSHMF LCILKEQKLL
DLVPVSGNKV VDIGQDEATA CLLLKEMALQ IHELVGARMH HLSVCQWEVK LKLDSDGPAS
GTWRVVTTNV TSHTCTVDIY REVEDTESQK LVYHSAPSSS GPLHGVALNT PYQPLSVIDL
KRCSARNNRT TYCYDFPLAF ETAVQKSWSN ISSDTNRCYV KATELVFAHK NGSWGTPVIP
MERPAGLNDI GMVAWILDMS TPEYPNGRQI VVIANDITFR AGSFGPREDA FFETVTNLAC
ERKLPLIYLA ANSGARIGIA DEVKSCFRVG WSDDGSPERG FQYIYLTEED HARISASVIA
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 EDSRSFFYKR LRRRISEDVL AKEIRGVSGK QFSHQSAIEL
IQKWYLASKG AETGNTEWDD DDAFVAWREN PENYQEYIKE LRAQRVSQLL SDVADSSPDL
EALPQGLSML LEKMDPSRRA QFVEEVKKAL K
//