GenomeNet

Database: UniProt
Entry: C7GRE4
LinkDB: C7GRE4
Original site: C7GRE4 
  All links  
No link information was found.   
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   11-JUN-2014, entry version 21.
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;
OC   Saccharomycetes; 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.,
RA   Netto O.V.C., Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O.,
RA   Noronha M.F., Dominska M., Andrietta M.G.S., Andrietta S.R.,
RA   Cunha A.F., Gomes L.H., Tavares F.C.A., Alcarde A.R., Dietrich F.S.,
RA   McCusker J.H., Petes T.D., 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
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=EEU06674.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; ACFL01000141; EEU06674.1; ALT_INIT; Genomic_DNA.
DR   OrthoDB; EOG74J9H5; -.
DR   UniPathway; UPA00655; UER00711.
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   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.90.226.10; -; 3.
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; IPR029045; ClpP/crotonase-like_dom.
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; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   SUPFAM; SSF52440; SSF52440; 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_0000392100.
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;  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
//
DBGET integrated database retrieval system