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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