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O14353

- BPL1_SCHPO

UniProt

O14353 - BPL1_SCHPO

Protein

Biotin--protein ligase

Gene

bpl1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase By similarity.By similarity

    Catalytic activityi

    ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] = AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase].
    ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)].
    ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)].
    ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)].

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. biotin-[acetyl-CoA-carboxylase] ligase activity Source: UniProtKB-EC
    3. biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity Source: UniProtKB-EC
    4. biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity Source: UniProtKB-EC
    5. biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity Source: UniProtKB-EC
    6. biotin-protein ligase activity Source: PomBase

    GO - Biological processi

    1. protein biotinylation Source: PomBase

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_188246. Biotin transport and metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biotin--protein ligase (EC:6.3.4.-)
    Alternative name(s):
    Biotin apo-protein ligase
    Including the following 4 domains:
    Biotin--[methylmalonyl-CoA-carboxytransferase] ligase (EC:6.3.4.9)
    Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase (EC:6.3.4.10)
    Alternative name(s):
    Holocarboxylase synthetase
    Short name:
    HCS
    Biotin--[methylcrotonoyl-CoA-carboxylase] ligase (EC:6.3.4.11)
    Biotin--[acetyl-CoA-carboxylase] ligase (EC:6.3.4.15)
    Gene namesi
    Name:bpl1
    ORF Names:SPBC30D10.07c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC30D10.07c.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 631631Biotin--protein ligasePRO_0000315970Add
    BLAST

    Proteomic databases

    MaxQBiO14353.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi4896.SPBC30D10.07c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO14353.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the biotin--protein ligase family.Curated

    Phylogenomic databases

    eggNOGiCOG0340.
    HOGENOMiHOG000214585.
    KOiK01942.
    OMAiAVVYCKV.
    OrthoDBiEOG7KQ2BG.
    PhylomeDBiO14353.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR019197. Biotin-prot_ligase_N.
    IPR004408. Biotin_CoA_COase_ligase.
    IPR003142. BPL_C.
    IPR004143. BPL_LipA_LipB.
    IPR029062. Class_I_gatase-like.
    [Graphical view]
    PANTHERiPTHR12835. PTHR12835. 1 hit.
    PfamiPF02237. BPL_C. 1 hit.
    PF03099. BPL_LplA_LipB. 1 hit.
    PF09825. BPL_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR00121. birA_ligase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O14353-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVLIYNGNG ASKICLLRTF QSLLPFVVPL YAMRFVDAST LEKEPWPAST    50
    ALLVMPGGRD MGYCSSFNET IYRKITDFVK RGGAYLGLCA GGYFGSAVVD 100
    FRMPDSDLNV VGKRKLQFFP GTCAGPTFPG FTYDSEDGAR RASIIVDGMQ 150
    SSPVHTHIYF NGGGSFLETE NYSNVKVVAR YQETDFEKSA AIIYVKVGKG 200
    NVVLTGIHPE FSAEGSPILD KRDEKTRLEL LSYILKLLGL KVPKDTSKCG 250
    QPTLTDQYLF PNNVETKRFI EKALTNKVKN QDEDTLYTFQ FSDISSEIPE 300
    HQLANLDISA DLSDSDNEIV KIWYGDEEKI CKKAKPSFDL ELYAKLINGC 350
    RFGLPIIVAP VIRSTQTLLD KNYRFLDSTN TGFTVLGNYQ TAGRGRGQNM 400
    WVSPYGTLAF SFIINVDAKN FSTTPIALFQ YLMALAVVRG IREYAPGYEN 450
    IPAFIKWPND VYVRVDKGGI NFQGKQYMKL SGIIVTSNYR KNVLHLVVGC 500
    GINVSNLGPT VSLNTLVDEW NKNSDNPRLE KFSFEKLLAS VLNQFDRYHR 550
    LLLEEGFSLI LPEYYQYWLH SNQTVNLASG GKAIIQGITS DFGFLLAQLL 600
    NENNEPTTKV VHLQPDGNSF DLMRNLITRK T 631
    Length:631
    Mass (Da):70,632
    Last modified:January 1, 1998 - v1
    Checksum:i37E08571359F5112
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAB10802.1.
    PIRiT40189.
    RefSeqiNP_596278.1. NM_001022199.2.

    Genome annotation databases

    EnsemblFungiiSPBC30D10.07c.1; SPBC30D10.07c.1:pep; SPBC30D10.07c.
    GeneIDi2540476.
    KEGGispo:SPBC30D10.07c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAB10802.1 .
    PIRi T40189.
    RefSeqi NP_596278.1. NM_001022199.2.

    3D structure databases

    ProteinModelPortali O14353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4896.SPBC30D10.07c-1.

    Proteomic databases

    MaxQBi O14353.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC30D10.07c.1 ; SPBC30D10.07c.1:pep ; SPBC30D10.07c .
    GeneIDi 2540476.
    KEGGi spo:SPBC30D10.07c.

    Organism-specific databases

    PomBasei SPBC30D10.07c.

    Phylogenomic databases

    eggNOGi COG0340.
    HOGENOMi HOG000214585.
    KOi K01942.
    OMAi AVVYCKV.
    OrthoDBi EOG7KQ2BG.
    PhylomeDBi O14353.

    Enzyme and pathway databases

    Reactomei REACT_188246. Biotin transport and metabolism.

    Miscellaneous databases

    NextBioi 20801603.
    PROi O14353.

    Family and domain databases

    Gene3Di 3.40.50.880. 1 hit.
    InterProi IPR019197. Biotin-prot_ligase_N.
    IPR004408. Biotin_CoA_COase_ligase.
    IPR003142. BPL_C.
    IPR004143. BPL_LipA_LipB.
    IPR029062. Class_I_gatase-like.
    [Graphical view ]
    PANTHERi PTHR12835. PTHR12835. 1 hit.
    Pfami PF02237. BPL_C. 1 hit.
    PF03099. BPL_LplA_LipB. 1 hit.
    PF09825. BPL_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52317. SSF52317. 1 hit.
    TIGRFAMsi TIGR00121. birA_ligase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.

    Entry informationi

    Entry nameiBPL1_SCHPO
    AccessioniPrimary (citable) accession number: O14353
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3