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Protein

Biotin sulfoxide reductase

Gene

bisC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase activity, acting specifically on the (S) enantiomer in the free, but not the protein-bound form. It thus plays a role in assimilation of oxidized methionines.2 Publications

Catalytic activityi

L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.1 Publication

Cofactori

Mo-bis(molybdopterin guanine dinucleotide)2 PublicationsNote: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.2 Publications

Kineticsi

kcat is 3.2 min(-1) for the reduction of Met-S-SO using benzyl viologen as an artificial electron donor.

  1. KM=17 µM for L-methionine (S)-S-oxide1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi148 – 1481MolybdenumBy similarity

    GO - Molecular functioni

    • electron carrier activity Source: InterPro
    • L-methionine:thioredoxin-disulfide S-oxidoreductase activity Source: EcoCyc
    • molybdenum ion binding Source: EcoCyc
    • NADH dehydrogenase activity Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, Molybdenum

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10124-MONOMER.
    ECOL316407:JW5940-MONOMER.
    MetaCyc:EG10124-MONOMER.

    Protein family/group databases

    TCDBi5.A.3.4.3. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biotin sulfoxide reductase (EC:1.-.-.-)
    Short name:
    BDS reductase
    Short name:
    BSO reductase
    Alternative name(s):
    L-methionine-(S)-sulfoxide reductase (EC:1.8.4.13)
    Short name:
    Met-S-SO reductase
    Gene namesi
    Name:bisC
    Ordered Locus Names:b3551, JW5940
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10124. bisC.

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene together with metB1, msrA and msrB are unable to use Met-S-SO for growth but retain the ability to use the enantiomer Met-R-SO, while a metB1/msrA/msrB deletion mutant is able to use both compounds.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 777777Biotin sulfoxide reductasePRO_0000063219Add
    BLAST

    Proteomic databases

    PaxDbiP20099.
    PRIDEiP20099.

    Interactioni

    Protein-protein interaction databases

    BioGridi4261247. 8 interactions.
    STRINGi511145.b3551.

    Structurei

    3D structure databases

    ProteinModelPortaliP20099.
    SMRiP20099. Positions 10-777.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The N-terminal 39 residues are essential for activity.1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4107QY8. Bacteria.
    COG0243. LUCA.
    HOGENOMiHOG000284391.
    InParanoidiP20099.
    KOiK08351.
    OMAiLEPDEWH.
    OrthoDBiEOG6NWBKD.
    PhylomeDBiP20099.

    Family and domain databases

    InterProiIPR009010. Asp_de-COase-like_dom.
    IPR006658. BisC.
    IPR006657. MoPterin_dinucl-bd_dom.
    IPR006656. Mopterin_OxRdtase.
    IPR006655. Mopterin_OxRdtase_prok_CS.
    [Graphical view]
    PfamiPF00384. Molybdopterin. 1 hit.
    PF01568. Molydop_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF50692. SSF50692. 1 hit.
    TIGRFAMsiTIGR00509. bisC_fam. 1 hit.
    PROSITEiPS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
    PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P20099-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MANSSSRYSV LTAAHWGPML VETDGETVFS SRGALATGME NSLQSAVRDQ
    60 70 80 90 100
    VHSNTRVRFP MVRKGFLASP ENPQGIRGQD EFVRVSWDEA LDLIHQQHKR
    110 120 130 140 150
    IREAYGPASI FAGSYGWRSN GVLHKASTLL QRYMALAGGY TGHLGDYSTG
    160 170 180 190 200
    AAQAIMPYVV GGSEVYQQQT SWPLVLEHSD VVVLWSANPL NTLKIAWNAS
    210 220 230 240 250
    DEQGLSYFSA LRDSGKKLIC IDPMRSETVD FFGDKMEWVA PHMGTDVALM
    260 270 280 290 300
    LGIAHTLVEN GWHDEAFLAR CTTGYAVFAS YLLGESDGIA KTAEWAAEIC
    310 320 330 340 350
    GVGAAKIREL AAIFHQNTTM LMAGWGMQRQ QFGEQKHWMI VTLAAMLGQI
    360 370 380 390 400
    GTPGGGFGLS YHFANGGNPT RRSAVLSSMQ GSLPGGCDAV DKIPVARIVE
    410 420 430 440 450
    ALENPGGAYQ HNGMNRHFPD IRFIWWAGGA NFTHHQDTNR LIRAWQKPEL
    460 470 480 490 500
    VVISECFWTA AAKHADIVLP ATTSFERNDL TMTGDYSNQH LVPMKQVVPP
    510 520 530 540 550
    RYEARNDFDV FAELSERWEK GGYARFTEGK SELQWLETFY NVARQRGASQ
    560 570 580 590 600
    QVELPPFAEF WQANQLIEMP ENPDSERFIR FADFCRDPLA HPLKTASGKI
    610 620 630 640 650
    EIFSQRIADY GYPDCPGHPM WLEPDEWQGN AEPEQLQVLS AHPAHRLHSQ
    660 670 680 690 700
    LNYSSLRELY AVANREPVTI HPDDAQERGI QDGDTVRLWN ARGQILAGAV
    710 720 730 740 750
    ISEGIKPGVI CIHEGAWPDL DLTADGICKN GAVNVLTKDL PSSRLGNGCA
    760 770
    GNTALAWLEK YNGPELTLTA FEPPASS
    Length:777
    Mass (Da):85,851
    Last modified:May 30, 2000 - v3
    Checksum:i51087D957E4FB38B
    GO

    Sequence cautioni

    The sequence AAB18528.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAE77744.1 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti583 – 5919DFCRDPLAH → AFLPRSAGD in AAA23522 (PubMed:2180922).Curated
    Sequence conflicti596 – 5983ASG → QR in AAA23522 (PubMed:2180922).Curated
    Sequence conflicti747 – 77731NGCAG…PPASS → MAVRVIRRWHGWKNTTVRN in AAA23522 (PubMed:2180922).CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M34827 Genomic DNA. Translation: AAA23522.1. Frameshift.
    U00039 Genomic DNA. Translation: AAB18528.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76575.3.
    AP009048 Genomic DNA. Translation: BAE77744.1. Different initiation.
    PIRiS47772.
    RefSeqiNP_418007.3. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC76575; AAC76575; b3551.
    BAE77744; BAE77744; BAE77744.
    GeneIDi946915.
    KEGGiecj:JW5940.
    eco:b3551.
    PATRICi32122574. VBIEscCol129921_3664.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M34827 Genomic DNA. Translation: AAA23522.1. Frameshift.
    U00039 Genomic DNA. Translation: AAB18528.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76575.3.
    AP009048 Genomic DNA. Translation: BAE77744.1. Different initiation.
    PIRiS47772.
    RefSeqiNP_418007.3. NC_000913.3.

    3D structure databases

    ProteinModelPortaliP20099.
    SMRiP20099. Positions 10-777.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261247. 8 interactions.
    STRINGi511145.b3551.

    Protein family/group databases

    TCDBi5.A.3.4.3. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

    Proteomic databases

    PaxDbiP20099.
    PRIDEiP20099.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76575; AAC76575; b3551.
    BAE77744; BAE77744; BAE77744.
    GeneIDi946915.
    KEGGiecj:JW5940.
    eco:b3551.
    PATRICi32122574. VBIEscCol129921_3664.

    Organism-specific databases

    EchoBASEiEB0122.
    EcoGeneiEG10124. bisC.

    Phylogenomic databases

    eggNOGiENOG4107QY8. Bacteria.
    COG0243. LUCA.
    HOGENOMiHOG000284391.
    InParanoidiP20099.
    KOiK08351.
    OMAiLEPDEWH.
    OrthoDBiEOG6NWBKD.
    PhylomeDBiP20099.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10124-MONOMER.
    ECOL316407:JW5940-MONOMER.
    MetaCyc:EG10124-MONOMER.

    Miscellaneous databases

    PROiP20099.

    Family and domain databases

    InterProiIPR009010. Asp_de-COase-like_dom.
    IPR006658. BisC.
    IPR006657. MoPterin_dinucl-bd_dom.
    IPR006656. Mopterin_OxRdtase.
    IPR006655. Mopterin_OxRdtase_prok_CS.
    [Graphical view]
    PfamiPF00384. Molybdopterin. 1 hit.
    PF01568. Molydop_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF50692. SSF50692. 1 hit.
    TIGRFAMsiTIGR00509. bisC_fam. 1 hit.
    PROSITEiPS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
    PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in Escherichia coli."
      Pierson D.E., Campbell A.
      J. Bacteriol. 172:2194-2198(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
      Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
      Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Molybdenum cofactor requirement for biotin sulfoxide reduction in Escherichia coli."
      del Campillo-Campbell A., Campbell A.
      J. Bacteriol. 149:469-478(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR.
    6. "Methionine sulfoxide reduction and assimilation in Escherichia coli: new role for the biotin sulfoxide reductase BisC."
      Ezraty B., Bos J., Barras F., Aussel L.
      J. Bacteriol. 187:231-237(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A METHIONINE SULFOXIDE REDUCTASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, COFACTOR, DOMAIN, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiBISC_ECOLI
    AccessioniPrimary (citable) accession number: P20099
    Secondary accession number(s): Q2M7L2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: May 30, 2000
    Last modified: February 17, 2016
    This is version 132 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Requires a small thioredoxin-like protein for activity.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.