ID H2NTG4_PONAB Unreviewed; 2383 AA.
AC H2NTG4; A0A2J8RCG8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 24-JAN-2024, entry version 73.
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:ENSPPYP00000009233.3};
GN ORFNames=CR201_G0051919 {ECO:0000313|EMBL:PNJ06211.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000009233.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000009233.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ06211.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ06211.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000009233.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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; NDHI03003711; PNJ06211.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000009233; -.
DR Ensembl; ENSPPYT00000009607.3; ENSPPYP00000009233.3; ENSPPYG00000008216.3.
DR eggNOG; KOG0368; Eukaryota.
DR GeneTree; ENSGT00940000156706; -.
DR HOGENOM; CLU_000395_5_0_1; -.
DR OMA; DFEDNTI; -.
DR OrthoDB; 911at2759; -.
DR TreeFam; TF300061; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001595; Chromosome 17.
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 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:UP000001595};
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_5040055970"
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; 269802 MW; 41962805E18DD6B4 CRC64;
MWWSTLMSIL RASSFWKWIS TQTVKIIRAL RAHFGGIMDE PSALAKPLEL NQHSRFIIGS
VSEDNSEDEI SNLVKLDLLE EKEGSLSPAS VGSDTLSDLG ISSLQDGLAL HIRSSMSGLH
LVKQGRDRKK IDSQRDFTVA SPAEFVTRFG GNKVIEKVLI ANNGIAAVKC MRSIRRWSYE
MFRNERAIRF VVMVTPEDLK ANAEYIKMAD HYVPVPGGPN NNNYANVELI LDIAKRIPVQ
AVWAGWGHAS ENPKLPELLL KNGIAFMGPP SQAMWALGDK IASSIVAQTA GIPTLPWSGS
GLRVDWQEND FSKRILNVPQ ELYEKGYVKD VDDGLQAAEE VGYPVMIKAS EGGGGKGIRK
VNNADDFPNL FRQVQAEVPG SPIFVMRLAK QSRHLEVQIL ADQYGNAISL FGRDCSVQRR
HQKIIEEAPA TIATPAVFEH MEQCAVKLAK MVGYVSAGTV EYLYSQDGSF YFLELNPRLQ
VEHPCTEMVA DVNLPAAQLQ IAMGIPLYRI KDIRMMYGVS PWGDSPIDFE DSAHVPCPRG
HVIAARITSE NPDEGFKPSS GTVQELNFRS NKNVWGYFSV AAAGGLHEFA DSQFGHCFSW
GENREEAISN MVVALKELSI RGDFRTTVEY LIKLLETESF QMNRIDTGWL DRLIAEKVQA
ERPDTMLGVV CGALHVADVS LRNSVSNFLH SLERGQVLPA HTLLNTVDVE LIYEGVKYVL
KVTRQSPNSY VVIMNGSCVE VDVHRLSDGG LLLSYDGSSY TTYMKEEVDR YRITIGNKTC
VFEKENDPSV MRSPSAGKLI QYIVEDGGHV FAGQCYAEIE VMKMVMTLTA VESGCIHYVK
RPGAALDPGC VLAKMQLDNP SKVQQAELHT GSLPRIQSTA LRGEKLHRVF HYVLDNLVNV
MNGYCLPDPF FSSKVKDWVE 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 GCFSDSPPQS PTFPEAGHTS LYDEDKVPRD
EPIHILNVAI KTDCDIEDDR LAAMFREFTQ QNKATLVDHG IRRLTFLVAQ KDFRKQVNYE
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 MTFKSPEYPE GRDIIVIGND ITYRIGSFGP QEDLLFLRAS
ELARAEGIPR IYVSANSGAR IGLAEEIRHM FHVAWVDPED PYKGYRYLYL TPQDYKRVSA
LNSVHCEHVE DEGESRYKIT DIIGKEEGIG PENLRGSGMI AGESSLAYNE IITISLVTCR
AIGIGAYLVR LGQRTIQVEN SHLILTGAGA LNKVLGREVY TSNNQLGGIQ IMHNNGVTHC
TVCDDFEGVF TVLHWLSYMP KSVHSSVPLL NSKDPIDRII EFVPTKAPYD PRWMLAGRPH
PTQKGQWLSG FFDYGSFSEI MQPWAQTVVV GRARLGGIPV GVVAVETRTV ELSIPADPAN
LDSEAKIIQQ AGQVWFPDSA FKTYQAIKDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF
GAYIVDGLRE CSQPVLVYIP PQAELRGGSW VVIDSSINPR HMEMYADRES RGSVLEPEGT
VEIKFRRKDL VKTMRRVDPV YIHLAERLGT PELSTAERKE LENKLKEREE FLIPIYHQVA
VQFADLHDTP GRMQEKGVIS DILDWKTSRT FFYWRLRRLL LEDLVKKKIH NANPELTDGQ
IQAMLRRWFV EVEGTVKAYV WDNNKDLAEW LEKQLTEEDG VHSVIEENIK CISRDYVLKQ
IRSLVQANPE VAMDSIIHMT QHISPTQRAE VVRILSTMDS PST
//