BISC_ECOLI
ID BISC_ECOLI Reviewed; 777 AA.
AC P20099; Q2M7L2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Biotin sulfoxide reductase;
DE Short=BDS reductase;
DE Short=BSO reductase;
DE EC=1.-.-.-;
DE AltName: Full=L-methionine-(S)-sulfoxide reductase;
DE Short=Met-S-SO reductase;
DE EC=1.8.4.13;
GN Name=bisC; OrderedLocusNames=b3551, JW5940;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2180922; DOI=10.1128/jb.172.4.2194-2198.1990;
RA Pierson D.E., Campbell A.;
RT "Cloning and nucleotide sequence of bisC, the structural gene for biotin
RT sulfoxide reductase in Escherichia coli.";
RL J. Bacteriol. 172:2194-2198(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP COFACTOR.
RX PubMed=6460021; DOI=10.1128/jb.149.2.469-478.1982;
RA del Campillo-Campbell A., Campbell A.;
RT "Molybdenum cofactor requirement for biotin sulfoxide reduction in
RT Escherichia coli.";
RL J. Bacteriol. 149:469-478(1982).
RN [6]
RP FUNCTION AS A METHIONINE SULFOXIDE REDUCTASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, KINETIC PARAMETERS, COFACTOR, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15601707; DOI=10.1128/jb.187.1.231-237.2005;
RA Ezraty B., Bos J., Barras F., Aussel L.;
RT "Methionine sulfoxide reduction and assimilation in Escherichia coli: new
RT role for the biotin sulfoxide reductase BisC.";
RL J. Bacteriol. 187:231-237(2005).
CC -!- FUNCTION: This enzyme may serve as a scavenger, allowing the cell to
CC utilize biotin sulfoxide as a biotin source. It reduces a spontaneous
CC oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to
CC biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase
CC activity, acting specifically on the (S) enantiomer in the free, but
CC not the protein-bound form. It thus plays a role in assimilation of
CC oxidized methionines. {ECO:0000269|PubMed:15601707,
CC ECO:0000269|PubMed:2180922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58772; EC=1.8.4.13;
CC Evidence={ECO:0000269|PubMed:15601707};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Evidence={ECO:0000305|PubMed:15601707, ECO:0000305|PubMed:6460021};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000305|PubMed:15601707,
CC ECO:0000305|PubMed:6460021};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for L-methionine (S)-S-oxide {ECO:0000269|PubMed:15601707};
CC Note=kcat is 3.2 min(-1) for the reduction of Met-S-SO using benzyl
CC viologen as an artificial electron donor.;
CC -!- DOMAIN: The N-terminal 39 residues are essential for activity.
CC {ECO:0000269|PubMed:15601707}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene together with metB1, msrA
CC and msrB are unable to use Met-S-SO for growth but retain the ability
CC to use the enantiomer Met-R-SO, while a metB1/msrA/msrB deletion mutant
CC is able to use both compounds. {ECO:0000269|PubMed:15601707}.
CC -!- MISCELLANEOUS: Requires a small thioredoxin-like protein for activity.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18528.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE77744.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M34827; AAA23522.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00039; AAB18528.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76575.3; -; Genomic_DNA.
DR EMBL; AP009048; BAE77744.1; ALT_INIT; Genomic_DNA.
DR PIR; S47772; S47772.
DR RefSeq; NP_418007.3; NC_000913.3.
DR RefSeq; WP_000013950.1; NZ_SSZK01000068.1.
DR AlphaFoldDB; P20099; -.
DR SMR; P20099; -.
DR BioGRID; 4261247; 8.
DR STRING; 511145.b3551; -.
DR TCDB; 5.A.3.4.3; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P20099; -.
DR PaxDb; P20099; -.
DR PRIDE; P20099; -.
DR EnsemblBacteria; AAC76575; AAC76575; b3551.
DR EnsemblBacteria; BAE77744; BAE77744; BAE77744.
DR GeneID; 946915; -.
DR KEGG; ecj:JW5940; -.
DR KEGG; eco:b3551; -.
DR PATRIC; fig|1411691.4.peg.3163; -.
DR EchoBASE; EB0122; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR InParanoid; P20099; -.
DR OMA; LEPDEWH; -.
DR PhylomeDB; P20099; -.
DR BioCyc; EcoCyc:EG10124-MON; -.
DR BioCyc; MetaCyc:EG10124-MON; -.
DR SABIO-RK; P20099; -.
DR PRO; PR:P20099; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IDA:EcoCyc.
DR GO; GO:0030151; F:molybdenum ion binding; IMP:EcoCyc.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006658; BisC.
DR InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR InterPro; IPR041460; Molybdopterin_N.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR00509; bisC_fam; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Molybdenum; Oxidoreductase; Reference proteome.
FT CHAIN 1..777
FT /note="Biotin sulfoxide reductase"
FT /id="PRO_0000063219"
FT BINDING 148
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT CONFLICT 583..591
FT /note="DFCRDPLAH -> AFLPRSAGD (in Ref. 1; AAA23522)"
FT /evidence="ECO:0000305"
FT CONFLICT 596..598
FT /note="ASG -> QR (in Ref. 1; AAA23522)"
FT /evidence="ECO:0000305"
FT CONFLICT 747..777
FT /note="NGCAGNTALAWLEKYNGPELTLTAFEPPASS -> MAVRVIRRWHGWKNTTV
FT RN (in Ref. 1; AAA23522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 85851 MW; 51087D957E4FB38B CRC64;
MANSSSRYSV LTAAHWGPML VETDGETVFS SRGALATGME NSLQSAVRDQ VHSNTRVRFP
MVRKGFLASP ENPQGIRGQD EFVRVSWDEA LDLIHQQHKR IREAYGPASI FAGSYGWRSN
GVLHKASTLL QRYMALAGGY TGHLGDYSTG AAQAIMPYVV GGSEVYQQQT SWPLVLEHSD
VVVLWSANPL NTLKIAWNAS DEQGLSYFSA LRDSGKKLIC IDPMRSETVD FFGDKMEWVA
PHMGTDVALM LGIAHTLVEN GWHDEAFLAR CTTGYAVFAS YLLGESDGIA KTAEWAAEIC
GVGAAKIREL AAIFHQNTTM LMAGWGMQRQ QFGEQKHWMI VTLAAMLGQI GTPGGGFGLS
YHFANGGNPT RRSAVLSSMQ GSLPGGCDAV DKIPVARIVE ALENPGGAYQ HNGMNRHFPD
IRFIWWAGGA NFTHHQDTNR LIRAWQKPEL VVISECFWTA AAKHADIVLP ATTSFERNDL
TMTGDYSNQH LVPMKQVVPP RYEARNDFDV FAELSERWEK GGYARFTEGK SELQWLETFY
NVARQRGASQ QVELPPFAEF WQANQLIEMP ENPDSERFIR FADFCRDPLA HPLKTASGKI
EIFSQRIADY GYPDCPGHPM WLEPDEWQGN AEPEQLQVLS AHPAHRLHSQ LNYSSLRELY
AVANREPVTI HPDDAQERGI QDGDTVRLWN ARGQILAGAV ISEGIKPGVI CIHEGAWPDL
DLTADGICKN GAVNVLTKDL PSSRLGNGCA GNTALAWLEK YNGPELTLTA FEPPASS
