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Database: UniProt
Entry: L1ML97_9BACT
LinkDB: L1ML97_9BACT
Original site: L1ML97_9BACT 
ID   L1ML97_9BACT            Unreviewed;       328 AA.
AC   L1ML97;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   13-SEP-2023, entry version 54.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01400, ECO:0000256|HAMAP-Rule:MF_01401};
DE   Includes:
DE     RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401};
DE              Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE              EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401};
DE     AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE              Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE   Includes:
DE     RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000256|HAMAP-Rule:MF_01400};
DE              EC=1.8.4.12 {ECO:0000256|HAMAP-Rule:MF_01400};
DE     AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01400};
GN   Name=msrB {ECO:0000256|HAMAP-Rule:MF_01400};
GN   Synonyms=msrA {ECO:0000256|HAMAP-Rule:MF_01401};
GN   ORFNames=HMPREF9999_00922 {ECO:0000313|EMBL:EKX91734.1};
OS   Alloprevotella sp. oral taxon 473 str. F0040.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Alloprevotella.
OX   NCBI_TaxID=1035197 {ECO:0000313|EMBL:EKX91734.1, ECO:0000313|Proteomes:UP000010460};
RN   [1] {ECO:0000313|EMBL:EKX91734.1, ECO:0000313|Proteomes:UP000010460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0040 {ECO:0000313|EMBL:EKX91734.1,
RC   ECO:0000313|Proteomes:UP000010460};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC       that have been inactivated by oxidation. Catalyzes the reversible
CC       oxidation-reduction of methionine sulfoxide in proteins to methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_01401}.
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=1.8.4.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001063, ECO:0000256|HAMAP-
CC         Rule:MF_01401};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC         ChEBI:CHEBI:50058; EC=1.8.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001795, ECO:0000256|HAMAP-
CC         Rule:MF_01400};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC         ChEBI:CHEBI:50058; EC=1.8.4.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001497, ECO:0000256|HAMAP-
CC         Rule:MF_01401};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01401}.
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01400}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
CC       sulfoxide reductase family. {ECO:0000256|ARBA:ARBA00008076}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MsrA Met
CC       sulfoxide reductase family. {ECO:0000256|ARBA:ARBA00011017}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01400}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKX91734.1}.
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DR   EMBL; AMEK01000050; EKX91734.1; -; Genomic_DNA.
DR   AlphaFoldDB; L1ML97; -.
DR   STRING; 1035197.HMPREF9999_00922; -.
DR   PATRIC; fig|1035197.3.peg.756; -.
DR   eggNOG; COG0225; Bacteria.
DR   eggNOG; COG0229; Bacteria.
DR   HOGENOM; CLU_031040_1_0_10; -.
DR   Proteomes; UP000010460; Unassembled WGS sequence.
DR   GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR   Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   HAMAP; MF_01400; MsrB; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR   InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   NCBIfam; TIGR00401; msrA; 1.
DR   NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR   PANTHER; PTHR10173; METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR10173:SF59; PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA/MSRB 1; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; Mss4-like; 1.
DR   SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01400}; Reference proteome {ECO:0000313|Proteomes:UP000010460}.
FT   DOMAIN          182..305
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
FT   ACT_SITE        13
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
FT   ACT_SITE        294
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ   SEQUENCE   328 AA;  36931 MW;  4264AFFF6016C805 CRC64;
     MNKTATLYFA GGCFWGTEHY FKQIRGVLST KVGYANGNIE HPTYEQVCSK TTGFAEAVEV
     TYNPEILPLT LLVQLYFRSI DPTSVNRQGG DIGTQYRTGI YYKDADVRPF LIAERTKLAQ
     AIGKNVAVEI EPLRNFYAAE DYHQDYLDKN PGGYCHVSPA LFAEARKANA DTTQRKYERP
     STDTLKSKLT EIQYQVTQNA ATERPFTNEY DHEFRPGIYV DITTGEPLFL STDKFDSGCG
     WPAFSKPIDA HLLKNIKDTS HGMQRIEVRS NKGNAHLGHV FNDGPKEKGG LRYCINSASL
     RFIPQAEMEK QGYGAYLPLL ETPKAELH
//
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