ID   HFA1_YEAS2              Reviewed;        2273 AA.
AC   C7GRE4;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Acetyl-CoA carboxylase, mitochondrial;
DE            Short=ACC;
DE            EC=6.4.1.2;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
DE   Flags: Precursor;
GN   Name=HFA1; ORFNames=C1Q_02929;
OS   Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=574961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAY291;
RX   PubMed=19812109; DOI=10.1101/gr.091777.109;
RA   Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA   Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA   Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA   Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA   Pereira G.A.G.;
RT   "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT   bioethanol production.";
RL   Genome Res. 19:2258-2270(2009).
CC   -!- FUNCTION: Catalyzes the rate-limiting reaction in the mitochondrial
CC       fatty acid synthesis (FAS) type II pathway. Responsible for the
CC       production of the mitochondrial malonyl-CoA, used for the biosynthesis
CC       of the cofactor lipoic acid. This protein carries three functions:
CC       biotin carboxyl carrier protein, biotin carboxylase, and
CC       carboxyltransferase (By similarity). {ECO:0000250}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC         ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- CAUTION: The reading frame from which this protein is translated has no
CC       Met initiation codon near to the 5'-end. However, it is not a
CC       pseudogene. It has been shown that at least 72 residues upstream of the
CC       first in-frame start codon (Met-151) are required for function and
CC       proper subcellular location. May be translated by means of alternative
CC       initiation codon usage, programmed translational frame shifting, or
CC       mRNA editing. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEU06674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ACFL01000141; EEU06674.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C7GRE4; -.
DR   SMR; C7GRE4; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000008073; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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:SF3; ACETYL-COA CARBOXYLASE; 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   3: Inferred from homology;
KW   ATP-binding; Biotin; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Ligase; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW   Multifunctional enzyme; Nucleotide-binding; Transit peptide.
FT   TRANSIT         1..104
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           105..2273
FT                   /note="Acetyl-CoA carboxylase, mitochondrial"
FT                   /id="PRO_0000392100"
FT   DOMAIN          134..635
FT                   /note="Biotin carboxylation"
FT   DOMAIN          292..484
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          763..837
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          1532..1867
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          1871..2187
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   REGION          1532..2187
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   ACT_SITE        459
FT                   /evidence="ECO:0000250"
FT   BINDING         332..337
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         1776
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2080
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2082
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         804
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   2273 AA;  259041 MW;  E545D409FC076A1B CRC64;
     KGKTITHGQS WGARRIHSHF YITIFTITCI RIGQYKLALY LDPYRFYNIT GSQIVRLKGQ
     RPEYRKRIFA HSYRHSSRIG LNFPSRRRYS NYVDRGNIHK HTRLPPQFIG LNTVESAQPS
     ILRDFVDLRG GHTVISKILI ANNGIAAVKE MRSIRKWAYE TFNDEKIIQF VVMATPDDLH
     ANSEYIRMAD QYVQVPGGTN NNNYANIDLI LDVAEQTDVD AVWAGWGHAS ENPCLPELLA
     SSQRKILFIG PPGRAMRSLG DKISSTIVAQ SAKIPCIPWS GSHIDTIHID NKTNFVSVPD
     DVYVRGCCSS PEDALEKAKL IGFPVMIKAS EGGGGKGIRR VDNQDDFIAL YRQAVNETPG
     SPMFVMKVVT DARHLEVQLL ADQYGTNITL FGRDCSIQRR HQKIIEEAPV TITKPETFQR
     MERAAIRLGE LVGYVSAGTV EYLYSPKDDK FYFLELNPRL QVEHPTTEMI SGVNLPATQL
     QIAMGIPMHM ISDIRKLYGL DPTGTSYIDF KNLKRPSPKG HCISCRITSE DPNEGFKPST
     GKIHELNFRS SSNVWGYFSV GNNGAIHSFS DSQFGHIFAV GNDRQDAKQN MVLALKDFSI
     RGEFKTPIEY LIELLETRDF ESNNISTGWL DDLILKNLSS DSKLDPTLAI ICGAAMKAYV
     FTEKVRNKYL ELLRRGQVPP KDFLKTKFPV DFIFDNNRYL FNVAQSSEEQ FILSINKSQC
     EVNVQKLSSD CLLISVDGKC HTVYWKDDIR GTRLSIDSNT IFLEAELNPT QVISPTPGKL
     VKYLVRSGDH VFAGQQYAEI EIMKMQMPLV AKSDGVIELL RQPGSIIEAG DVIAKLTLDS
     PSKANESSLY RGELPVLGPP LIEGSRPNHK LRVLINRLEN ILNGYHENSG IETTLKELIK
     ILRDGRLPYS EWDSQISTVR NRLPRQLNEG LGNLVKKSVS FPAKELHKLM KRYLEENTND
     HVVYVALQPL LKISERYSEG LANHECEIFL KLIKKYYAVE KIFENHDIHE ERNLLNLRRK
     DLTNLKEILC ISLSHANIVA KNKLVTAILH EYEPLCQDSS KMSLKFRAVI HDLASLESKW
     AKEVSVKARS VLLRGIFPPI KKRKEHIKTL LQLHIKDTGA ENIHSRNIYS CMRDFGNLIH
     SNLIQLQDLF FFFGHQDTAL SSIASEIYAR YAYGNYQLKS IKIHKGAPDL LMSWQFSSLR
     NYLVNPDGES DGFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV YEQIHIPEER
     LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS KLKVNRITFA FIAANAPAVK
     FYSFDGTTYD EIPQIRNMDP SYEAPLELGK MSNYKIRSLP TYDSSIRIFE GISKFTPLDK
     RFFVRKIINS FMYNDQKTTE ENLKAEINAQ VVYMLEHLGA VDISNSDLNH IFLSFNTVLN
     IPVHRLEEIV STILKTHETR LFQERITDVE ICISVECLET KKPAPLRLLI SNKSGYVVKI
     ETYYEKIGKN GNLILEPCSE QSHYSQKSLS LPYSVKDWLQ PKRYKAQFMG TTYVYDFPGL
     FHQAAIQQWK RYFPKHKLND SFFSWVELIE QNGNLIKVNR EPGLNNIGMV AFEIMVQTPE
     YPEGRNMIVI SNDITYNIGS FGPREDLFFD RVTNYARERG IPRIYLAANS GAKLGIAEEL
     IPLFRVAWND PSDPTKGFQY LYLAPKDMQL LKDSGKGNSV VVEHKMVYGE ERYIIKAIVG
     FEEGLGVECL QGSGLIAGAT SKAYRDIFTI TAVTCRSVGI GSYLVRLGQR TIQVEDKPII
     LTGASAINKV LGTDIYTSNL QIGGTQIMYK NGIAHLTASN DMKAIEKIMT WLSYVPAKRD
     MSPPLLETMD RWDRDVDFKP AKQVPYEARW LIEGKWDSNN NFQSGLFDKD SFFETLSGWA
     KGVIVGRARL GGIPVGVIAV ETKTIEEIIP ADPANLDSSE FSVKEAGQVW YPNSAFKTAQ
     TINDFNYGEQ LPLIILANWR GFSGGQRDMY NEVLKYGSFI VDALVDYKQP ILIYIPPFGE
     LRGGSWVVID PTINPEQMEM YADVESRGGV LEPDGVVSIK YRKEKMIETM IRLDSTYGHL
     RRTLTEKKLS LEKQNDLTKR LKIRERQLIP IYNQISIQFA DLHDRSTRML VKGVIRNELE
     WKKSRRFLYW RLRRRLNEGQ VIKRLQKKTC DNKTKMKYDD LLKIVQSWYN DLDVNDDRAV
     VEFIERNSKK IGKNVEEFEI SLLIDELKKK FEDRRGNIAL EELTRLVDSK RKR
//