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A6ZMR9

- HFA1_YEAS7

UniProt

A6ZMR9 - HFA1_YEAS7

Protein

Acetyl-CoA carboxylase, mitochondrial

Gene

HFA1

Organism
Saccharomyces cerevisiae (strain YJM789) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 2 (02 Mar 2010)
      Previous versions | rss
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    Functioni

    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 By similarity.By similarity

    Catalytic activityi

    ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
    ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

    Cofactori

    Biotin.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei459 – 4591By similarity
    Binding sitei1776 – 17761Coenzyme ABy similarity
    Binding sitei2080 – 20801Coenzyme ABy similarity
    Binding sitei2082 – 20821Coenzyme ABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi332 – 3376ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA carboxylase activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW
    3. biotin carboxylase activity Source: UniProtKB-EC
    4. metal ion binding Source: InterPro

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW
    2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Biotin, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA carboxylase, mitochondrial (EC:6.4.1.2)
    Short name:
    ACC
    Including the following 1 domains:
    Biotin carboxylase (EC:6.3.4.14)
    Gene namesi
    Name:HFA1
    ORF Names:SCY_4385
    OrganismiSaccharomyces cerevisiae (strain YJM789) (Baker's yeast)
    Taxonomic identifieri307796 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000007060: Unassembled WGS sequence

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 104104MitochondrionSequence AnalysisAdd
    BLAST
    Chaini105 – 22732169Acetyl-CoA carboxylase, mitochondrialPRO_0000392101Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei804 – 8041N6-biotinyllysineBy similarity

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini134 – 635502Biotin carboxylationAdd
    BLAST
    Domaini292 – 484193ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini770 – 83667Biotinyl-bindingAdd
    BLAST
    Domaini1648 – 2147500CarboxyltransferaseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated
    Contains 1 carboxyltransferase domain.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    OrthoDBiEOG74J9H5.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProiIPR013537. AcCoA_COase_cen.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF08326. ACC_central. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view]
    SMARTiSM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A6ZMR9-1 [UniParc]FASTAAdd to Basket

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    KGKTITHGQS WGARRIHSHF YITIFTITCI RIGQYKLALY LDPYRFYNIT     50
    GSQIVRLKGQ RPEYRKRIFA HSYRHSSRIG LNFPSRRRYS NYVDRGNIHK 100
    HTRLPPQFIG LNTVESAQPS ILRDFVDLRG GHTVISKILI ANNGIAAVKE 150
    MRSIRKWAYE TFNDEKIIQF VVMATPDDLH ANSEYIRMAD QYVQVPGGTN 200
    NNNYANIDLI LDVAEQTDVD AVWAGWGHAS ENPCLPELLA SSQRKILFIG 250
    PPGRAMRSLG DKISSTIVAQ SAKIPCIPWS GSHIDTIHID NKTNFVSVPD 300
    DVYVRGCCSS PEDALEKAKL IGFPVMIKAS EGGGGKGIRR VDNEDDFIAL 350
    YRQAVNETPG SPMFVMKVVT DARHLEVQLL ADQYGTNITL FGRDCSIQRR 400
    HQKIIEEAPV TITKPETFQR MERAAIRLGE LVGYVSAGTV EYLYSPKDDK 450
    FYFLELNPRL QVEHPTTEMI SGVNLPATQL QIAMGIPMHM ISDIRKLYGL 500
    DPTGTSYIDF KNLKRPSPKG HCISCRITSE DPNEGFKPST GKIHELNFRS 550
    SSNVWGYFSV GNNGAIHSFS DSQFGHIFAV GNDRQDAKQN MVLALKDFSI 600
    RGEFKTPIEY LIELLETRDF ESNNISTGWL DDLILKNLSS DSKLDPTLAI 650
    ICGAAMKAYV FTEKVRNKYL ELLRRGQVPP KDFLKTKFPV DFIFDNNRYL 700
    FNVAQSSEEQ FILSINKSQC EVNVQKLSGD CLLISVDGKC HTVYWKDDIR 750
    GTRLSIDSNT IFLEAELNPT QVISPTPGKL VKYLVRSGDH VFAGQQYAEI 800
    EIMKMQMPLV AKSDGVIELL RQPGSIIEAG DVIAKLTLDS PSKANESSLY 850
    RGELPVLGPP LIEGSRPNHK LRVLINRLEN ILNGYHENSG IETTLKELIK 900
    ILRDGRLPYS EWDSQISTVR NRLPRQLNEG LGNLVKKSVS FPAKELHKLM 950
    KRYLEENTND HVVYVALQPL LKISERYSEG LANHECEIFL KLIKKYYAVE 1000
    KIFENHDIHE ERNLLNLRRK DLTNLKEILC ISLSHANVVA KNKLVTAILH 1050
    EYEPLCQDSS KMSLKFRAVI HDLASLESKW AKEVAVKARS VLLRGIFPPI 1100
    KKRKEHIKTL LQLHIKDTGA ENIHSRNIYS CMRDFGNLIH SNLIQLQDLF 1150
    FFFGHQDTAL SSIASEIYAR YAYGNYQLKS IKIHKGAPDL LMSWQFSSLR 1200
    NYLVNPDGES DEFTKLSKPP STSGKSSANS FGLLVNMRAL ESLEKTLDEV 1250
    YEQIHIPEER LSSGENSLIV NILSPIRYRS ENDLIKTLKI KLHENERGLS 1300
    KLKVNRITFA FIAANAPTVK FYSFDGTTYD EISQIRNMDP SYEAPLELGK 1350
    MSNYKIRSLP TYDSSIRIFE GISKFTPLDK RFFVRKIINS SMYNDQKTTE 1400
    ENLKAEINAQ VVYMLEHLGA VDTSNSDLNH IFLSFNTVLN IPVHRLEEIV 1450
    STILKTHETR LFQERITDVE ICISVECLET KKPAPLRLLI SNKSGYVVKI 1500
    ETYYEKIGKN GNLILEPCSE QSHYSQKSLS LPYSVKDWLQ PKRYKAQFMG 1550
    TTYVYDFPGL FHQAAIQQWK RYFPKHKLND SFFSWVELIE QNGNLIKVNR 1600
    EPGLNNIGMV AFEIMVQTPE YPEGRNMIVI SNDITYNIGS FGPREDLFFD 1650
    RVTNYARERG IPRIYLAANS GAKLGIAEEL IPLFRVAWND PSDPTKGFQY 1700
    LYLAPKDMQL LKDYGKGNSV VVEHKMVYGE ERYIIKAIVG FEEGLGVECL 1750
    QGSGLIAGAT SKAYRDIFTI TAVTCRSVGI GSYLVRLGQR TIQVEDKPII 1800
    LTGASAINKV LGTDIYTSNL QIGGTQIMYK NGIAHLTAGN DMKAIEKIMT 1850
    WLSYVPAKRD MSPPLLETMD RWDRDVDFKP AKQVPYEARW LIEGKWDSNN 1900
    NFQSGLFDKD SFFETLSGWA KGVIVGRARL GGIPVGVIAV ETKTIEEIIP 1950
    ADPANLDSSE FSVKEAGQVW YPNSAFKTAQ TINDFNYGEQ LPLIILANWR 2000
    GFSGGQRDMY NEVLKYGSFI VDALVDYKQP ILIYIPPFGE LRGGSWVVID 2050
    PTINPEQMEM YADVESRGGV LEPDGVVSIK YRKEKMIETM IRLDSTYGHL 2100
    RRTLTEKKLS LEKQNDLTKR LKIRERQLIP IYNQISIQFA DLHDRSTRML 2150
    VKGVIRKELE WKKSRRFLYW RLRRRLNEGQ VIKRLQKKTC DNKTKMKYDD 2200
    LLKIVQSWYN DLDVNDDRAV VEFIERNSKK IDKNIEEFEI SLLIDELKKK 2250
    FEDRRGNIVL EELTRLVDSK RKR 2273
    Length:2,273
    Mass (Da):259,162
    Last modified:March 2, 2010 - v2
    Checksum:i22AE8CD3EBB50432
    GO

    Sequence cautioni

    The sequence EDN64143.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFW02000021 Genomic DNA. Translation: EDN64143.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFW02000021 Genomic DNA. Translation: EDN64143.1 . Different initiation.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    OrthoDBi EOG74J9H5.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProi IPR013537. AcCoA_COase_cen.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF08326. ACC_central. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view ]
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: YJM789.

    Entry informationi

    Entry nameiHFA1_YEAS7
    AccessioniPrimary (citable) accession number: A6ZMR9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 2, 2010
    Last sequence update: March 2, 2010
    Last modified: October 1, 2014
    This is version 37 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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 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.Curated

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3