ID A0A2K6E1T4_MACNE Unreviewed; 2368 AA.
AC A0A2K6E1T4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:ENSMNEP00000042107.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000042107.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000042107.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSMNET00000066609.1; ENSMNEP00000042107.1; ENSMNEG00000043362.1.
DR GeneTree; ENSGT00940000156706; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000043362; Expressed in temporal lobe and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 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:UP000233120}.
FT DOMAIN 153..654
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 311..502
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 781..855
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1598..1936
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1940..2256
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2368 AA; 267770 MW; 1D73036E2A2B15F3 CRC64;
VKRPLLLKIQ KSSQAWWWVP VIPATWEALR AHFGGIMDEP SPLAKPLELN QHSRFIIGSV
SEDNSEDEIS NLVKLDLLEE KEGSLSPASV GSDTLSDLGI SSLQDGLALH IRSSMSGLHL
VKQGRDRKKI DSQRDFTVAS PAEFVTRFGG NKVIEKVLIA NNGIAAVKCM RSIRRWSYEM
FRNERAIRFV VMVTPEDLKA NAEYIKMADH YVPVPGGPNN NNYANVELIL DIAKRIPVQA
VWAGWGHASE NPKLPELLLK NGIAFMGPPS QAMWALGDKI ASSIVAQTAG IPTLPWSGSG
LRMDWQENDF SKRILNVPQE LYEKGYVKDV DDGLQAAEEV GYPVMIKASE GGGGKGIRKV
NNADDFPNLF RQVQAEVPGS PIFVMRLAKQ SRHLEVQILA DQYGNAISLF GRDCSVQRRH
QKIIEEAPAT IATPAVFEHM EQCAVKLAKM VGYVSAGTVE YLYSQDGSFY FLELNPRLQV
EHPCTEMVAD VNLPAAQLQI AMGIPLYRIK DIRMMYGVSP WGDSPIDFED SAHVPCPRGH
VIAARITSEN PDEGFKPSSG TVQELNFRSN KNVWGYFSVA AAGGLHEFAD SQFGHCFSWG
ENREEAISNM VVALKELSIR GDFRTTVEYL IKLLETESFQ MNRIDTGWLD RLIAEKVQAE
RPDTMLGVVC GALHVADVSL RNSVSNFLHS LERGQVLPAH TLLNTVDVEL IYEGVKYVLK
VTRQSPNSYV VIMNGSCVEV DVHRLSDGGL LLSYDGSSYT TYMKEEVDRY RITIGNKTCV
FEKENDPSVM RSPSAGKLIQ YIVEDGGHVF AGQCYAEIEV MKMVMTLTAV ESGCIHYVKR
PGAALDPGCV LARMQLDNPS KVQQAELHTG SLPRIQSTAL RGEKLHRVFH YVLDNLVNVM
NGYCLPDPFF SSKVKDWVER LMKTLRDPSL PLLELQDIMT SVSGRIPPNV EKSIKKEMAQ
YASNITSVLC QFPSQQIANI LDSHAATLNR KSEREVFFMN TQSIVQLVQR YRSGIRGHMK
AVVMDLLRQY LRVETQFQNG HYDKCVFALR EENKSDMNTV LNYIFSHAQV TKKNLLVTML
IDQLCGRDPT LTDELLNILT ELTQLSKTTN AKVALRARQV LIASHLPSYE LRHNQVESIF
LSAIDMYGHQ FCIENLQKLI LSETSIFDVL PNFFYHSNQV VRMAALEVYV RRAYIAYELN
SVQHRQLKDN TCVVEFQFML PTSHPNRGNI PTLNRMSFSS NLNHYGMTHV ASVSDVLLDN
SFTPPCQRMG GMVSFRTFED FVRIFDEVMS CFSDSPPQSP TFPEAGHTSL YDEDKVPRDE
PIHILNVAIK TDCDIEDDRL AAMFREFTQQ NKATLVDHGI RRLTFLVAQK VLTCEFCFFS
DSRTQFEEDR IYRHLEPALA FQLELNRMRN FDLTAIPCAN HKMHLYLGAA KVEVGTEVTD
YRFFVRAIIR HSDLVTKEAS FEYLQNEGER LLLEAMDELE VAFNNTNVRT DCNHIFLNFV
PTVIMDPSKI EESVRSMVMR YGSRLWKLRV LQAELKINIR LTPTGKAIPI RLFLTNESGY
YLDISLYKEV TDSRTAQIMF QAYGDKQGPL HGMLINTPYV TKDLLQSKRF QAQSLGTTYI
YDIPEMFRQS LIKLWESMST QAFLPSPPLP SDMLTYTELV LDDQGQLVHM NRLPGGNEIG
MVAWKMTFKS PEYPEGRDII VIGNDITYRI GSFGPQEDWL FLRASELARA EGIPRIYVSA
NSGARIGLAE EIRHMFHVAW VDPEDPYKGY RYLYLTPQDY KRVSALNSVH CEHVEDEGES
RYKITDIIGK EEGIGPENLR GSGMIAGESS LAYNEIITIS LVTCRAIGIG AYLVRLGQRT
IQVENSHLIL TGAGALNKVL GREVYTSNNQ LGGIQIMHNN GVTHCTVCDD FEGVFTVLHW
LSYMPKSVHS SVPLLNSKDP IDRIIEFVPT KAPYDPRWML AGRPHPTQKG QWLSGFFDYG
SFSEIMQPWA QTVVVGRARL GGIPVGVVAV ETRTVELSIP ADPANLDSEA KIIQQAGQVW
FPDSAFKTYQ AIKDFNREGL PLMVFANWRG FSGGMKDMYD QVLKFGAYIV DGLRECSQPV
LVYIPPQAEL RGGSWVVIDS SINPRHMEMY ADRESRGSVL EPEGTVEIKF RRKDLVKTMR
RVDPVYIHLA ERLGTPELST AERKELENKL KEREEFLIPI YHQVAVQFAD LHDTPGRMQE
KGVISDILDW KTSRTFFYWR LRRLLLEDLV KKKIHNANPE LTDGQIQAML RRWFVEVEGT
VKAYVWDNNK DLAEWLEKQL TEEDGVHSVI EENIKCISRD YVLKQIRSLV QANPEVAMDS
IIHMTQHISP TQRAEVVRIL STMDSPST
//
