MSRB_METTH
ID MSRB_METTH Reviewed; 151 AA.
AC O26807;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000255|HAMAP-Rule:MF_01400};
DE EC=1.8.4.12 {ECO:0000255|HAMAP-Rule:MF_01400};
DE AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01400};
GN Name=msrB {ECO:0000255|HAMAP-Rule:MF_01400}; OrderedLocusNames=MTH_711;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01400};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01400};
CC Note=Binds 1 zinc ion per subunit. The zinc ion is important for the
CC structural integrity of the protein. {ECO:0000255|HAMAP-Rule:MF_01400};
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01400}.
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DR EMBL; AE000666; AAB85216.1; -; Genomic_DNA.
DR PIR; A69195; A69195.
DR RefSeq; WP_010876350.1; NC_000916.1.
DR PDB; 2K8D; NMR; -; A=1-151.
DR PDBsum; 2K8D; -.
DR AlphaFoldDB; O26807; -.
DR BMRB; O26807; -.
DR SMR; O26807; -.
DR STRING; 187420.MTH_711; -.
DR EnsemblBacteria; AAB85216; AAB85216; MTH_711.
DR GeneID; 24853853; -.
DR KEGG; mth:MTH_711; -.
DR PATRIC; fig|187420.15.peg.695; -.
DR HOGENOM; CLU_031040_8_5_2; -.
DR OMA; DEQWRAE; -.
DR BRENDA; 1.8.4.12; 3256.
DR EvolutionaryTrace; O26807; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR HAMAP; MF_01400; MsrB; 1.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR PANTHER; PTHR10173; PTHR10173; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..151
FT /note="Peptide methionine sulfoxide reductase MsrB"
FT /id="PRO_0000140320"
FT DOMAIN 25..147
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 136
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:2K8D"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:2K8D"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2K8D"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:2K8D"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2K8D"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2K8D"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2K8D"
SQ SEQUENCE 151 AA; 17303 MW; 8D11C52CEB186033 CRC64;
MKDRIPIFSV AKNRVEMVER IELSDDEWRE ILDPEAFRVA RKAGTEPPFT GKYHDLHDDG
IYRCICCGTD LFDSETKFDS GTGWPSFYDV VSEHNIKLRE DRSLGMVRCE VLCARCDAHL
GHVFDDGPRP TGKRYCMNSA ALKFIPRDQI G
