ID A0A2K5N0Q4_CERAT Unreviewed; 2444 AA.
AC A0A2K5N0Q4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN Name=ACACB {ECO:0000313|Ensembl:ENSCATP00000031077.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000031077.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000031077.1}
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; ENSCATT00000055342.1; ENSCATP00000031077.1; ENSCATG00000038648.1.
DR GeneTree; ENSGT00940000155049; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000038648; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
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; 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:SF1; ACETYL-COA CARBOXYLASE 2; 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; 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 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:UP000233060};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..2444
FT /note="acetyl-CoA carboxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014356081"
FT DOMAIN 259..761
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 418..609
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 888..962
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1681..2011
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 2015..2331
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 45..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2444 AA; 274509 MW; 4BA9D83AE14CC441 CRC64;
MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSTSEAN FILSQEPFPA SDNSGETPQR
NGEDHSLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT
GTQGLEASDT NGLSSSARPQ GQQAGCPSKE DRKQANIKRQ LMTNFILGSF DDYSSDEDSV
AGSSRESTRK GSRASLGALS LEAALTAGEA ETHVPTMRPS MSGLHLVKRG REHKKLDLHR
DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT
PEDLKANAEY IKMADQYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL
PELLCKNGVA FLGPPSEAMW ALGDKIASTI VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK
IISVPEDVYD QGCVKDVDEG LEAAEKIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV
QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP
LAIFEFMEQC AVRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL
PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE
GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA
LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL
NVADAMFRTC MTDFLHCLER GQVLPADSLL NIVDVELIYG GIKYILKVAR QSLTMFVLIM
NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP
SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQESG RVKYIKRPGA VLEAGCVVAR
LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPIFSIK
LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP
SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLHV
EHHFQQAHYD KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD
ELTSILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP
ENLKKLIISE TTIFDVLPAF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV
VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR
NFDEVISCFA NVPKDTPLFS EARTSLYSED DCKSLREDPI HILNVSIQCA DHLEDEALVP
ILRTFVQSKK NILVDYGLRR ITFLIAQEFA EDRIYRHLEP ALAFQLELSR MRNFDLTAVP
CANHKMHLYL GAAKVKEGAE VTDHRFFIRA IIRHSDLITK EASFEYLQNE GERLLLEAMD
ELEVAFNNTS VRTDCNHIFL NFVPTVIMDP LKIEESVRSM VMRYGSRLWK LRVLQAEVKI
NIRQTTTGSA VPIRLFITNE SGYYLDISLY KEVTDSRSGN IMFHSFGNKQ GPQHGMLINT
PYVTKDLLQA KRFQAQSLGT TYIYDFPEIF RQALFKLWGS PDKYPKDILT YTELVLDSQG
QLVEMNRLPG GNEVGMVAFK MRFKTQEYPE GRDMIVIGND ITFRIGSFGP GEDLLYLRAS
EMARAEGIPK IYVAANSGAR IGMAEEIKHM FHVAWVDPED PHKGFKYLYL TPQDYTRISS
LNSVHCKHIE EGGESRYMIT DIIGKDDGLG VENLRGSGMI AGESSLAYEE IVTISLVTCR
ALGIGAYLVR LGQRVIQVEN SHIILTGASA LNKVLGREVY TSNNQLGGVQ IMHYNGVSHI
TVPDDFEGVY TILEWLSYMP KDNHSPVPII TPTDPIDREI EFLPSRAPYD PRWMLAGRPH
PTLKGTWQSG FFDHGSFKEI MAPWAQTVVT GRARLGGIPV GVIAVETRTV EVVVPADPAN
LDSEAKIIQQ AGQVWFPDSA YKTAQAIKDF NREKLPLMIF ANWRGFSGGM KDMYDQVLKF
GAYIVDGLRQ YKQPILIYIP PYAELRGGSW VVIDATINPL CIEMYADKES RGGVLEPEGT
VEIKFRKKDL IKSMRRIDPA YKKLMEQLGE PDLSDKDRKD LEGRLKARED LLLPIYHQVA
VQFADFHDTP GRMLEKGVIS DILEWKTART FLYWRLRRLL LEDQVKQEIL RASGELSHVH
IQSMLRRWFV ETEGAVKAYL WDNNQVVVQW LEQHWQVEDG PRSTIRENIT YLKHDSVLKT
IRGLVQENPE VAVDCVIHLS QHISPAERAQ VIHLLSTMDS PAST
//
