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Acetyl-CoA carboxylase, mitochondrial (ACC) (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 HFA1_YEAST              Reviewed;        2273 AA.
P32874; D6W032; O42823;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
13-FEB-2019, entry version 173.
RecName: Full=Acetyl-CoA carboxylase, mitochondrial;
Short=ACC;
EC=6.4.1.2;
Includes:
RecName: Full=Biotin carboxylase;
EC=6.3.4.14;
Flags: Precursor;
Name=HFA1; OrderedLocusNames=YMR207C; ORFNames=YM8261.01C, YM8325.08C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SP1;
Saito A., Kazuta Y., Kondo H., Tanabe T.;
"Occurrence of an acetyl-CoA carboxylase-like gene in Saccharomyces
serevisiae.";
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-949.
PubMed=7906156; DOI=10.3109/10425179309015625;
Kearsey S.E.;
"Identification of a Saccharomyces cerevisiae gene closely related to
FAS3 (acetyl-CoA carboxylase).";
DNA Seq. 4:69-70(1993).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14761959; DOI=10.1074/jbc.M401071200;
Hoja U., Marthol S., Hofmann J., Stegner S., Schulz R., Meier S.,
Greiner E., Schweizer E.;
"HFA1 encoding an organelle-specific acetyl-CoA carboxylase controls
mitochondrial fatty acid synthesis in Saccharomyces cerevisiae.";
J. Biol. Chem. 279:21779-21786(2004).
-!- FUNCTION: Catalyzes the rate-limiting reaction in the
mitochondrial fatty acid synthesis (FAS) type II pathway.
Responsible for the production of the mitochondrial malonyl-CoA,
used for the biosynthesis of the cofactor lipoic acid. This
protein carries three functions: biotin carboxyl carrier protein,
biotin carboxylase, and carboxyltransferase.
{ECO:0000269|PubMed:14761959}.
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
ChEBI:CHEBI:456216; EC=6.4.1.2;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
= ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:14761959}.
-!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- CAUTION: The reading frame from which this protein is translated
has no Met initiation codon near to the 5'-end. However, it is not
a pseudogene. It has been shown (PubMed:14761959) that at least 72
residues upstream of the first in-frame start codon (Met-151) are
required for function and proper subcellular location. May be
translated by means of alternative initiation codon usage,
programmed translational frame shifting, or mRNA editing.
{ECO:0000305|PubMed:14761959}.
-!- SEQUENCE CAUTION:
Sequence=DAA10106.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D78165; BAA24410.1; -; Genomic_DNA.
EMBL; Z49809; CAA89922.1; -; Genomic_DNA.
EMBL; Z48755; CAA88647.1; -; Genomic_DNA.
EMBL; Z22558; CAA80280.1; -; Genomic_DNA.
EMBL; BK006946; DAA10106.1; ALT_INIT; Genomic_DNA.
PIR; S55089; S55089.
RefSeq; NP_013934.1; NM_001182714.1.
ProteinModelPortal; P32874; -.
SMR; P32874; -.
BioGrid; 35385; 254.
DIP; DIP-2568N; -.
IntAct; P32874; 2.
MINT; P32874; -.
STRING; 4932.YMR207C; -.
MaxQB; P32874; -.
PaxDb; P32874; -.
PeptideAtlas; P32874; -.
PRIDE; P32874; -.
GeneID; 855247; -.
KEGG; sce:YMR207C; -.
EuPathDB; FungiDB:YMR207C; -.
SGD; S000004820; HFA1.
HOGENOM; HOG000214115; -.
InParanoid; P32874; -.
KO; K11262; -.
BioCyc; MetaCyc:YMR207C-MONOMER; -.
BioCyc; YEAST:YMR207C-MONOMER; -.
UniPathway; UPA00655; UER00711.
PRO; PR:P32874; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005737; C:cytoplasm; HDA:SGD.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IGI:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:InterPro.
GO; GO:0006633; P:fatty acid biosynthetic process; IGI:SGD.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR013537; AcCoA_COase_cen.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR001882; Biotin_BS.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF08326; ACC_central; 1.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF01039; Carboxyl_trans; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52096; SSF52096; 2.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00188; BIOTIN; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS50989; COA_CT_CTER; 1.
PROSITE; PS50980; COA_CT_NTER; 1.
PROSITE; PS00866; CPSASE_1; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
ATP-binding; Biotin; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
Mitochondrion; Multifunctional enzyme; Nucleotide-binding;
Reference proteome; Transit peptide.
TRANSIT 1 104 Mitochondrion. {ECO:0000255}.
CHAIN 105 2273 Acetyl-CoA carboxylase, mitochondrial.
/FTId=PRO_0000146771.
DOMAIN 134 635 Biotin carboxylation.
DOMAIN 292 484 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 763 837 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1532 1867 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 1871 2187 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 332 337 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1532 2187 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
ACT_SITE 459 459 {ECO:0000250}.
BINDING 1776 1776 Coenzyme A. {ECO:0000250}.
BINDING 2080 2080 Coenzyme A. {ECO:0000250}.
BINDING 2082 2082 Coenzyme A. {ECO:0000250}.
MOD_RES 804 804 N6-biotinyllysine. {ECO:0000250,
ECO:0000255|PROSITE-ProRule:PRU01066}.
CONFLICT 661 661 F -> L (in Ref. 4; CAA80280).
{ECO:0000305}.
CONFLICT 1027 1027 K -> E (in Ref. 1; BAA24410).
{ECO:0000305}.
SEQUENCE 2273 AA; 259163 MW; 08727A301549DA92 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 VDNEDDFIAL 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
DLTNLKKILC ISLSHANVVA KNKLVTAILH EYEPLCQDSS KMSLKFRAVI HDLASLESKW
AKEVAVKARS VLLRGIFPPI KKRKEHIKTL LQLHIKDTGA ENIHSRNIYS CMRDFGNLIH
SNLIQLQDLF FFFGHQDTAL SSIASEIYAR YAYGNYQLKS IKIHKGAPDL LMSWQFSSLR
NYLVNSDGES DEFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV YEQIHIPEER
LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS KLKVNRITFA FIAANAPAVK
FYSFDGTTYD EISQIRNMDP 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 IDKNIEEFEI SLLIDELKKK FEDRRGNIVL EELTRLVDSK RKR


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