ID D2D0D8_PIG Unreviewed; 2346 AA.
AC D2D0D8; A0A4X1T021; F1S1B5;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-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|EMBL:ACM42414.1,
GN ECO:0000313|Ensembl:ENSSSCP00005023284.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ACM42414.1};
RN [1] {ECO:0000313|EMBL:ACM42414.1}
RP NUCLEOTIDE SEQUENCE.
RA Lin L., Scharfe M., Severitt S., Bloecker H., Fries R.;
RT "Genomic characterization and polymorphism analysis of genes involved in
RT fatty acid metabolism in pigs.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HCZ94714.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00005023284.1}
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 EMBL; FJ263680; ACM42414.1; -; Genomic_DNA.
DR EMBL; DQIR01039239; HCZ94714.1; -; Transcribed_RNA.
DR EMBL; DQIR01072306; HDA27782.1; -; Transcribed_RNA.
DR EMBL; DQIR01075357; HDA30833.1; -; Transcribed_RNA.
DR EMBL; DQIR01075358; HDA30834.1; -; Transcribed_RNA.
DR EMBL; DQIR01077479; HDA32955.1; -; Transcribed_RNA.
DR EMBL; DQIR01087774; HDA43250.1; -; Transcribed_RNA.
DR EMBL; DQIR01088884; HDA44360.1; -; Transcribed_RNA.
DR EMBL; DQIR01089736; HDA45212.1; -; Transcribed_RNA.
DR EMBL; DQIR01090487; HDA45963.1; -; Transcribed_RNA.
DR EMBL; DQIR01253703; HDC09181.1; -; Transcribed_RNA.
DR EMBL; DQIR01255912; HDC11390.1; -; Transcribed_RNA.
DR EMBL; DQIR01317759; HDC73233.1; -; Transcribed_RNA.
DR EMBL; DQIR01317848; HDC73322.1; -; Transcribed_RNA.
DR EMBL; DQIR01317925; HDC73399.1; -; Transcribed_RNA.
DR Ensembl; ENSSSCT00005037977.1; ENSSSCP00005023284.1; ENSSSCG00005019036.1.
DR Ensembl; ENSSSCT00005038262.1; ENSSSCP00005023487.1; ENSSSCG00005019036.1.
DR Ensembl; ENSSSCT00005038386.1; ENSSSCP00005023551.1; ENSSSCG00005019036.1.
DR Ensembl; ENSSSCT00005038503.1; ENSSSCP00005023624.1; ENSSSCG00005019036.1.
DR Ensembl; ENSSSCT00005038603.1; ENSSSCP00005023692.1; ENSSSCG00005019036.1.
DR eggNOG; KOG0368; Eukaryota.
DR UniPathway; UPA00655; UER00711.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 117..618
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 275..466
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 745..819
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1576..1914
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1918..2234
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2346 AA; 265347 MW; D7910A0B58FD1B3F CRC64;
MDEPSPLAKP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVSSDTLS
DLGISSLQDG LALHMRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK
VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG
GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL
GDKIASSIVA QTAGIPTLPW SGSGLRVDWH ENDFSKRILN VPQDLYEKGY VKDVDDGLKA
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV
QILADQYGNA ISLFGRDCSV QRRHQKIIEE APAAIATPAV FEHMEQCAVK LARMVGYVSA
GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGVPL YRIKDIRMMY
GVSPWGDAPI DFENSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY
FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
ESFQLNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSISN FLHSLERGQV
LSAHTLLNTV DVELIYGGVK YVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDG
SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA
EIEVMKMVMT LTAAESGCIH YVKRPGAALD PGCVIAKMQL DNPSKVQQAE LHTGSLPQIQ
STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSRVKD WVERLMKTLR DPSLPLLELQ
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV
FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD
MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELL NILTELTQLS KTTNAKVALR
ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH
SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM
SFSSNLNHYG MTHVASVSDV LLDNAFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFCDSP
PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDRLAAMFRE FTQQNKATLV
EHGIRRLTFL VAQKDFRKQV NYEVDQRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ
LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE
YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG
SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA
YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSTQA
YLPPPPLPSD MLTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMSLKSPE YPEGRDIIVI
GNDITYRIGS FGPQEDVLFL RASELARAEG IPRIYVAANS GARIGLAEEI RHMFHVAWVD
PEDPYKGYKY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GLGAENLRGS
GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR
EVYTSNNQLG GIQIMHNNGV THSTVCDDFE GVFTVLHWLS YMPKSVCSSV PLLNSKDPID
RVIEFVPTKA PYDPRWMLAG RAHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG
IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL
MVFANWRGFS GGMKDMYDQM LKFGAYIVDG LRECSQPVMV YIPPQAELRG GSWVVIDPTI
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSTAE
RKELESKLKE REEFLLPIYH QVAVQFADLH DTPGRMQEKG VINDILDWKT SRTFFYWRLR
RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL VEWLEKQLTE
EDGVRSVIEE NIKYISRDYV LKQIRSLVQA NPEVAMDSIV HMTQHISPTQ RAEVVRILST
MDSPST
//