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Database: UniProt
Entry: G1M4G3_AILME
LinkDB: G1M4G3_AILME
Original site: G1M4G3_AILME 
ID   G1M4G3_AILME            Unreviewed;      2383 AA.
AC   G1M4G3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 78.
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:ENSAMEP00000014229.2};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000014229.2, ECO:0000313|Proteomes:UP000008912};
RN   [1] {ECO:0000313|Ensembl:ENSAMEP00000014229.2, ECO:0000313|Proteomes:UP000008912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
RN   [2] {ECO:0000313|Ensembl:ENSAMEP00000014229.2}
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   RefSeq; XP_019661138.1; XM_019805579.1.
DR   STRING; 9646.ENSAMEP00000014229; -.
DR   Ensembl; ENSAMET00000014828.2; ENSAMEP00000014229.2; ENSAMEG00000013274.2.
DR   GeneID; 100474573; -.
DR   KEGG; aml:100474573; -.
DR   CTD; 31; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   GeneTree; ENSGT00940000156706; -.
DR   InParanoid; G1M4G3; -.
DR   TreeFam; TF300061; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000008912; 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:UP000008912};
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_5031419827"
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;  269827 MW;  F17725989278361A CRC64;
     MWWSTLMSIL RASSFWRWIS AQTVRIIRAL RAHFEGKMDE PSPLAKPLEL NQHSRFIIGS
     VSEDNSEDEI SNLVKLDLLE EKEGSLSPAS VGSDTLSDLG ISSLQDGLAL HMRSSMSGLH
     LVKQGRDRKK IDSQRDFTVA SPAEFVTRFG GNKVIEKVLI ANNGIAAVKC MRSIRRWSYE
     MFRNERAIRF VVMVTPEDLK ANAEYIKMAD HYVPVPGGPN NNNYANVELI LDIAKRIPVQ
     AVWAGWGHAS ENPKLPELLL KNGIAFMGPP SQAMWALGDK IASSIVAQTA GIPTLPWSGS
     GLRVDWHEND FSKRILNVPQ ELYEKGYVKD VDDGLKAAEE VGYPVMIKAS EGGGGKGIRK
     VNNADDFPNL FRQVQAEVPG SPIFVMRLAK QSRHLEVQIL ADQYGNAISL FGRDCSVQRR
     HQKIIEEAPA AIATPAVFEH MEQCAVKLAK MVGYVSAGTV EYLYSQDGSF YFLELNPRLQ
     VEHPCTEMVA DVNLPAAQLQ IAMGIPLYRI KDIRMMYGVS PWGDAPIDFE NSAHVPCPRG
     HVIAARITSE NPDEGFKPSS GTVQELNFRS NKNVWGYFSV AAAGGLHEFA DSQFGHCFSW
     GENREEAISN MVVALKELSI RGDFRTTVEY LIKLLETESF QLNRIDTGWL DRLIAEKVQA
     ERPDTMLGVV CGALHVADVS LRNSISNFLH SLERGQVLPA HTLLNTVDVE LIYGGVKYVL
     KVTRQSPNSY VVIMNGSCVE VDVHRLSDGG LLLSYDGSSY TTYMKEEVDR YRITIGNKTC
     VFEKENDPSV LRSPSAGKLI QYIVEDGGHV FAGQCYAEIE VMKMVMTLTA AESGCIHYVK
     RPGTALDPGC VIAKMQLDNP SKVQQAELHT GSLPRIQSTA LRGEKLHRVF HYVLDNLVNV
     MNGYCLPDPF FSSRVKDWVE RLMKTLRDPS LPLLELQDIM TSVSGRIPPN 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 DFVRIFDEVM GCFCDSPPQS PTFPEAGHTS LYDEDKVPRD
     EPIHILNVAI KTDCDIEDDG 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 MTLKSPEYPE GRDIIVIGND ITYRIGSFGP QEDLLFLRAS
     ELARAEGIPR IFVAANSGAR IGLAEEIRHM FHVAWVDPED PYKGYKYLYL TPQDYKRVSA
     LNSVHCEHVE DEGESRYKIT DIIGKEEGLG AENLRGSGMI AGESSLAYDE IITISLVTCR
     AIGIGAYLVR LGQRTIQVEN SHLILTGAGA LNKVLGREVY TSNNQLGGIQ IMHNNGVTHS
     IVCDDFEGVF TVLHWLSYMP KSVRSSVPLL NSKDPIDRII EFVPTKAPYD PRWMLAGRPH
     PTQKGQWLSG FFDYGSFSEI MQPWAQTVVV GRARLGGIPV GVVAVETRTV ELSIPADPAN
     LDSEAKIIQQ AGQVWFPDSA FKTYQAIKDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF
     GAYIVDSLRE CSQPVLVYIP PQAELRGGSW VVIDPTINPR HMEMYADRES RGSVLEPEGT
     VEIKFRRKDL VKTMRRVDPV YIRLAERLGT PELSPAERKE LENKLKEREE FLIPIYHQVA
     VQFADLHDTP GRMQEKGVIN DILDWKTSRT FFYWRLRRLL LEDLVKKKIH NANPELTDGQ
     IQAMLRRWFV EVEGTVKAYI WDNNKDLVEW LEKQLTEEDG VRSVIEENIK YISRDYVLKQ
     IRSLVQANPE VAMDSIVHMT QHISPTQRAE VVRILSTMDS PST
//
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