ID HFA1_YEAS7 Reviewed; 2273 AA.
AC A6ZMR9;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 06-MAR-2013, entry version 33.
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=SCY_4385;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R.,
RA Wang X., Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S.,
RA Li Y., Davis R.W., Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces
RT cerevisiae strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Catalyzes the rate-limiting reaction in the
CC mitochondrial fatty acid synthesis (FAS) type II pathway.
CC Responsible for the production of the mitochondrial malonyl-CoA,
CC used for the biosynthesis of the cofactor lipoic acid. This
CC protein carries three functions: biotin carboxyl carrier protein,
CC biotin carboxylase, and carboxyltransferase (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
CC + malonyl-CoA.
CC -!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
CC CO(2) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
CC protein].
CC -!- COFACTOR: Biotin (By similarity).
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC from acetyl-CoA: step 1/1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC -!- SIMILARITY: Contains 1 biotin carboxylation domain.
CC -!- SIMILARITY: Contains 1 biotinyl-binding domain.
CC -!- SIMILARITY: Contains 1 carboxyltransferase domain.
CC -!- CAUTION: The reading frame from which this protein is translated
CC has no Met initiation codon near to the 5'-end. However, it is not
CC a pseudogene. It has been shown that at least 72 residues upstream
CC of the first in-frame start codon (Met-151) are required for
CC function and proper subcellular location. May be translated by
CC means of alternative initiation codon usage, programmed
CC translational frame shifting, or mRNA editing.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN64143.1; Type=Erroneous initiation;
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DR EMBL; AAFW02000021; EDN64143.1; ALT_INIT; Genomic_DNA.
DR UniPathway; UPA00655; UER00711.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA: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 Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR InterPro; IPR000022; Carboxyl_trans.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF00289; CPSase_L_chain; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; Hybrid_motif; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_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; Complete proteome; Fatty acid biosynthesis;
KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW Mitochondrion; Multifunctional enzyme; Nucleotide-binding;
KW Transit peptide.
FT TRANSIT 1 104 Mitochondrion (Potential).
FT CHAIN 105 2273 Acetyl-CoA carboxylase, mitochondrial.
FT /FTId=PRO_0000392101.
FT DOMAIN 134 635 Biotin carboxylation.
FT DOMAIN 292 484 ATP-grasp.
FT DOMAIN 770 836 Biotinyl-binding.
FT DOMAIN 1648 2147 Carboxyltransferase.
FT NP_BIND 332 337 ATP (By similarity).
FT ACT_SITE 459 459 By similarity.
FT BINDING 1776 1776 Coenzyme A (By similarity).
FT BINDING 2080 2080 Coenzyme A (By similarity).
FT BINDING 2082 2082 Coenzyme A (By similarity).
FT MOD_RES 804 804 N6-biotinyllysine (By similarity).
SQ SEQUENCE 2273 AA; 259162 MW; 22AE8CD3EBB50432 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
EVNVQKLSGD 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 ISLSHANVVA KNKLVTAILH EYEPLCQDSS KMSLKFRAVI HDLASLESKW
AKEVAVKARS VLLRGIFPPI KKRKEHIKTL LQLHIKDTGA ENIHSRNIYS CMRDFGNLIH
SNLIQLQDLF FFFGHQDTAL SSIASEIYAR YAYGNYQLKS IKIHKGAPDL LMSWQFSSLR
NYLVNPDGES DEFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV YEQIHIPEER
LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS KLKVNRITFA FIAANAPTVK
FYSFDGTTYD EISQIRNMDP SYEAPLELGK MSNYKIRSLP TYDSSIRIFE GISKFTPLDK
RFFVRKIINS SMYNDQKTTE ENLKAEINAQ VVYMLEHLGA VDTSNSDLNH 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 LKDYGKGNSV VVEHKMVYGE ERYIIKAIVG
FEEGLGVECL QGSGLIAGAT SKAYRDIFTI TAVTCRSVGI GSYLVRLGQR TIQVEDKPII
LTGASAINKV LGTDIYTSNL QIGGTQIMYK NGIAHLTAGN 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 VKGVIRKELE
WKKSRRFLYW RLRRRLNEGQ VIKRLQKKTC DNKTKMKYDD LLKIVQSWYN DLDVNDDRAV
VEFIERNSKK IDKNIEEFEI SLLIDELKKK FEDRRGNIVL EELTRLVDSK RKR
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