ID A0A2Y9LFG2_DELLE Unreviewed; 1998 AA.
AC A0A2Y9LFG2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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|RefSeq:XP_022408409.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022408409.1};
RN [1] {ECO:0000313|RefSeq:XP_022408409.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022408409.1};
RG RefSeq;
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 -!- 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_022408409.1; XM_022552701.1.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000248483; Unplaced.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 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; 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; 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; 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; 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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW 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 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|PROSITE-ProRule:PRU00409};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT DOMAIN 1..270
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 54..118
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 397..471
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1228..1566
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1570..1886
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1998 AA; 227312 MW; 749984E5DFD347D1 CRC64;
MRLAKQSRHL EVQILADQYG NAISLFGRDC SVQRRHQKII EEAPTAIATP AVFEHMEQCA
VKLAKMVGYV SAGTVEYLYS QDGSFYFLEL NPRLQVEHPC TEMVADVNLP AAQLQIAMGI
PLYRIKDIRM MYGVSPWGDA PIDFENSAHV PCPRGHVIAA RITSENPDEG FKPSSGTVQE
LNFRSNKNVW GYFSVAAAGG LHEFADSQFG HCFSWGENRE EAISNMVVAL KELSIRGDFR
TTVEYLIKLL ETESFQMNRI DTGWLDRLIA EKVQAERPDT MLGVVCGALH VADVSLRNSI
SNFLHSLERG QVLSAHTLLN TVDVELIYEG VKYVLKVTRQ SPNSYVVIMN GSCVEVDVHR
LSDGGLLLSY DGSSYTTYMK EEVDRYRITI GNKTCVFEKE NDPSVMRSPS AGKLIQYIVE
DGGHVFAGQC YAEIEVMKMV MTLTAAESGC IHYVKRPGAA LDPGCVIAKM QLDNPSKVQQ
AELHTGSLPR IQSTALRGEK LHRVFHYVLD NLVNVMNGYC LPDPFFSSRV KDWVERLMKT
LRDPSLPLLE LQDIMTSVSG RIPPNVEKSI KKEMAQYASN ITSVLCQFPS QQIANILDSH
AATLNRKSER EVFFMNTQSI VQLVQRYRSG IRGHMKAVVM DLLRQYLRVE TQFQNGHYDK
CVFALREENK SDMNTVLNYI FSHAQVTKKN LLVTMLIDQL CGRDPTLTDE LLNILTELTQ
LSKTTNAKVA LRARQVLIAS HLPSYELRHN QVESIFLSAI DMYGHQFCIE NLQKLILSET
SIFDVLPNFF YHSNQVVRMA ALEVYVRRAY IAYELNSVQH RQLKDNTCVV EFQFMLPTSH
PNRGNIPTLN RMSFSSNLNH YGMTHVASVS DVLLDNSFTP PCQRMGGMVS FRTFEDFVRI
FDEVMGCFCD SPPQSPTFPE AGHTSLYDED KIPRDEPIHI LNVAIKTDCD IEDDRLAAMF
REFTQQNKAT LVEHGIRRLT FLVAQKDFRK QVNYEVDQRF HREFPKFFTF RARDKFEEDR
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 MVAWKMTLKS
PEYPEGRDII VIGNDITYRI GSFGPQEDLL FLRASELARA EGIPRIYVAA NSGARIGLAE
EIRHMFHVAW VDPEDPYKGY KYLYLTPQDY KRVSALNSVH CEHVEDEGES RYKITDIIGK
EEGLGAENLR GSGMIAGESS LAYDEIITIS LVTCRAIGIG AYLVRLGQRT IQVENSHLIL
TGAGALNKVL GREVYTSNNQ LGGIQIMHNN GVTHSTVCDD FEGVFTVLHW LSYMPKSVHS
SVPLLNSKDP IDRVIEFIPT KTPYDPRWML AGRPHPTQKG QWLSGFFDYG SFSEIMQPWA
QTVAVGRARL GGIPVGVVAV ETRTVELSIP ADPANLDSEA KIIQQAGQVW FPDSAFKTYQ
AIKDFNREGL PLMVFANWRG FSGGMKDMYD QVLKFGAYIV DGLRECSQPV MVYIPPQAEL
RGGSWVVIDP TINPRHMEMY ADRESRGSVL EPEGTVEIKF RRKDLVKTMR RVDPVYIHLA
ERLGTPELSA AERKELESKL KEREDFLLPI YRQVAVQFAD LHDTPGRMQE KGVINDILDW
KTSRTFFYWR LRRLLLEDLV KKKIHNANPE LTDGQIQAML RRWFVEVEGT VKAYVWDNNK
DLVEWLEKQL AEEDGARSVI EENIKYISRD YVLKQIRSLV QANPEVAMDS IVHMTQHISP
TQRAEVVRIL STMDSPST
//
