ID A0A396PU01_9CLOT Unreviewed; 371 AA.
AC A0A396PU01;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ECO:0000313|EMBL:RHV62823.1};
GN Synonyms=msrA {ECO:0000256|HAMAP-Rule:MF_01401};
GN ORFNames=DXB18_15355 {ECO:0000313|EMBL:RHV62823.1};
OS Clostridium sp. OM02-18AC.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2292311 {ECO:0000313|EMBL:RHV62823.1, ECO:0000313|Proteomes:UP000266676};
RN [1] {ECO:0000313|EMBL:RHV62823.1, ECO:0000313|Proteomes:UP000266676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM02-18AC {ECO:0000313|EMBL:RHV62823.1,
RC ECO:0000313|Proteomes:UP000266676};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RHV62823.1}.
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DR EMBL; QULW01000027; RHV62823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A396PU01; -.
DR Proteomes; UP000266676; 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:SF52; METHIONINE-R-SULFOXIDE REDUCTASE B3; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..371
FT /note="Multifunctional fusion protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038612228"
FT DOMAIN 231..354
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
FT ACT_SITE 64
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
FT ACT_SITE 343
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ SEQUENCE 371 AA; 41653 MW; CFAFEA0169B3B89F CRC64;
MYRSVLALLF AAVLLGGCAA GKQTVPKEKS GQETNMDGAA FDRSDEEVTY MDTTDNVIYL
AGGCFWGMEQ LMQSIPGVID AESGYANGTC EADADYKTVC QGNTGFREAV RVEYDPGQVS
LDALLLAYFY VIDPTVENRQ GNDRGSQYQT GVYYTNESAK ETVERIAEIE RGRSEKFFVE
IGPLKNYYPA EEYHQNYLEK NPNGYCHIPR AEMELFSRLR IDPGDYQKPA AESIRDKLTA
EQYRVTQESG TERAFTGEFW DKFEKGIYVD VVTGEPLFSS TDKYESGCGW PAFTKPIEEP
AVVELEDLSH GMRRTEVRSR AGDSHLGHVF TGDPESPNGV RYCINSAALR FVPYAKMKAE
GYGYLLYLFE E
//
