ID I3M0I9_ICTTR Unreviewed; 2383 AA.
AC I3M0I9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Acetyl-CoA carboxylase 1 {ECO:0000256|ARBA:ARBA00020135};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN Name=ACACA {ECO:0000313|Ensembl:ENSSTOP00000002229.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000002229.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000002229.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11309;
CC Evidence={ECO:0000256|ARBA:ARBA00001448};
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; AGTP01022422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01022423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01022424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01022425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01022426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01022427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01022428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01022429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01022430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01022431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 43179.ENSSTOP00000002229; -.
DR Ensembl; ENSSTOT00000002492.3; ENSSTOP00000002229.3; ENSSTOG00000002468.3.
DR eggNOG; KOG0368; Eukaryota.
DR GeneTree; ENSGT00940000156706; -.
DR HOGENOM; CLU_000395_5_0_1; -.
DR InParanoid; I3M0I9; -.
DR OrthoDB; 911at2759; -.
DR TreeFam; TF300061; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:Ensembl.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; IEA:Ensembl.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:0019538; P:protein metabolic process; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
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; 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 PANTHER; PTHR45728:SF5; ACETYL-COA CARBOXYLASE 1; 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; 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; PS00866; CPSASE_1; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2383
FT /note="Acetyl-CoA carboxylase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012338989"
FT DOMAIN 154..655
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 312..503
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 782..856
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1613..1951
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1955..2271
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2383 AA; 270015 MW; FD53B55BB668C4E1 CRC64;
MWWSTLMSIL RASSFWKRIT AQTVRIIRAL RAYFERIMDE PSPLAKPLEL NQHSRFIIGS
VSEDNSEDEI SNLVKLDLLE EKEGSLSPAS VSSDTLSDLG ISSLQDGLAL HIRSSMSGLH
LVKQCRDRKK VDSQRDFTVA SPAEFVTRFG GNKVIEKVLI ANNGIAAVKC MRSIRRWSYE
MFRNERAIRF VVMVTPEDLK ANAEYIKMAD HYVPVPGGPN NNNYANVELI LDIAKRIPVQ
AVWAGWGHAS ENPKLPELLL KNGIAFMGPP SQAMWALGDK IASSIVAQTA GIPTLPWSGS
GLRVDWQEND FSKRILNVPQ ELYEKGYVKD VDDGLKAAEE VGYPVMIKAS EGGGGKGIRK
VNNADDFPNL FRQVQAEVPG SPIFVMRLAK QSRHLEVQIL ADQYGNAISL FGRDCSVQRR
HQKIIEEAPA AIATPAVFEH MEQCAVKLAK MVGYVSAGTV EYLYSQDGSF YFLELNPRLQ
VEHPCTEMVA DVNLPAAQLQ IAMGIPLFRI KDIRMMYGVS PWGDAPIDFE NSAHVPCPRG
HVIAARITSE NPDEGFKPSS GTVQELNFRS NKNVWGYFSV AAAGGLHEFA DSQFGHCFSW
GENREEAISN MVVALKELSI RGDFRTTVEY LIKLLETESF QLNRIDTGWL DRLIAEKVQA
ERPDTMLGVV CGALHVADVS LRNSISNFLH SLERGQVLPA HTLLNTVDVE LIYEGVKYVL
KVTRQSPNSY VVIMNGSCVE VDVHRLSDGG LLLSYDGSSY TTYMKEEVDR YRITIGNKTC
VFEKENDPSV MRSPSAGKLI QYIVEDGGHV FAGQCYAEIE VMKMVMTLTA AESGCIHYVK
RPGAALDPGC VIAKMQLDNP SKVQQAELHT GSLPQIQSTA LRGEKLHRVF HYVLDNLVNV
MNGYCLPDPF FSSRVKDWVE RLMKTLRDPS LPLLELQDIM TSVSGRIPLN VEKSIKKEMA
QYASNITSVL CQFPSQQIAN ILDSHAATLN RKSEREVFFM NTQSIVQLVQ RYRSGIRGHM
KAVVMDLLRQ YLRVETQFQN GHYDKCVFAL REENKSDMNT VLNYIFSHAQ VTKKNLLVTM
LIDQLCGRDP TLTDELLNIL TELTQLSKTT NAKVALRARQ VLIASHLPSY ELRHNQVESI
FLSAIDMYGH QFCIENLQKL ILSETSIFDV LPNFFYHSNQ VVRMAALEVY VRRAYIAYEL
NSVQHRQLKD NTCVVEFQFM LPTSHPNRGN IPTLNRMSFS SNLNHYGMTH VASVSDVLLD
NSFTPPCQRM GGMVSFRTFE DFIRIFDDVM GCFSDSPPQS PTFPEAGHTS LYDEDKVPRE
EPIHILNVAI KTDGDIEDDR LAAMFREFTQ QNKATLVEHG IRRLTFLVAQ KDFRKQVNCE
VDQRFHREFP KFFTFRARDK FEEDRIYRHL EPALAFQLEL NRMRNFDLTA IPCANHKMHL
YLGAAKVEVG TEVTDYRFFV RAIIRHSDLV TKEASFEYLQ NEGERLLLEA MDELEVAFNN
TNVRTDCNHI FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEL KINIRLTPTG
KAIPIRLFLT NESGYYLDIS LYKEVTDSRT AQIMFQAYGD KQGPLHGMLI NTPYVTKDLL
QSKRFQAQSL GTTYIYDIPE MFRQSLIKLW ESMSTQAFLP SPPLPSDMLT YTELVLDDQG
QLVHMNRLPG GNEIGMVAWK MSLKSPEYPE GRDIIVIGND ITYRIGSFGP QEDLLFLRAS
ELARAEGIPR IFVAANSGAR IGLAEEIRHM FHVAWVDPED PYKGYKYLYL TPQDYKRVSA
LNSVHCEHVE DEGESRYKIT DIIGKEEGLG AENLRGSGMI AGESSLAYDE IITISLVTCR
AIGIGAYLVR LGQRTIQVEN SHLILTGASA LNKVLGREVY TSNNQLGGIQ IMHNNGVTHC
TVCDDFEGVF TVLHWLSYMP KNVHSSVPLL NSKDPIDRII EFVPTKAPYD PRWMLAGRPH
PTQKGQWLSG FFDYGSFSEI MQPWAQTVVV GRARLGGIPV GVVAVETRTV ELSIPADPAN
LDSEAKIIQQ AGQVWFPDSA FKTYQAIKDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF
GAYIVDSLRE CSQPVMVYIP PQAELRGGSW VVIDPTINPR HMEMYADRES RGSVLEPEGT
VEIKFRKKDL VKTMRRVDPV YIRLAERLGT PELSPAERKE LENKLKEREE FLIPIYHQVA
VQFADLHDTP GRMQEKGVIN DILDWKTSRT FFYWRLRRLL LEDLVKKKIH NANPELTDGQ
IQAMLRRWFV EVEGTVKAYV WDNNKDLVEW LEKQLTEEDG VRSVIEENIK YISRDYVLKQ
IRSLVQANPE VAMDSIVHMT QHISPTQRAE VVRILSTMDS PST
//
