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 16-JUN-2009, entry version 58. DE RecName: Full=Peptide methionine sulfoxide reductase msrB; DE EC=1.8.4.12; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase; GN Name=msrB; OrderedLocusNames=MTH_711; OS Methanobacterium thermoautotrophicum. OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=187420; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Delta H; RX MEDLINE=98037514; PubMed=9371463; 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., RA Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., RA Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R., RA Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., RA McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., RA Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.; RT "Complete genome sequence of Methanobacterium thermoautotrophicum RT deltaH: functional analysis and comparative genomics."; RL J. Bacteriol. 179:7135-7155(1997). CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. CC -!- COFACTOR: Binds 1 zinc ion per subunit. The zinc ion is important CC for the structural integrity of the protein (By similarity). CC -!- SIMILARITY: Belongs to the msrB Met sulfoxide reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000666; AAB85216.1; -; Genomic_DNA. DR PIR; A69195; A69195. DR RefSeq; NP_275854.1; -. DR PDB; 2K8D; NMR; -; A=1-151. DR PDBsum; 2K8D; -. DR GeneID; 1470672; -. DR GenomeReviews; AE000666_GR; MTH_711. DR KEGG; mth:MTH711; -. DR NMPDR; fig|187420.1.peg.709; -. DR HOGENOM; O26807; -. DR OMA; O26807; MVERIEL. DR BioCyc; MTHE187420:MTH711-MON; -. DR BRENDA; 1.8.4.12; 270. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase ac...; IEA:EC. DR GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01400; -; 1. DR InterPro; IPR002579; Methionine_sulphoxide_MsrB. DR Gene3D; G3DSA:2.170.150.20; MsrB; 1. DR Pfam; PF01641; SelR; 1. DR ProDom; PD004057; DUF25; 1. DR TIGRFAMs; TIGR00357; MsrB; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Metal-binding; Oxidoreductase; Zinc. FT CHAIN 1 151 Peptide methionine sulfoxide reductase FT msrB. FT /FTId=PRO_0000140320. FT ACT_SITE 136 136 Nucleophile (By similarity). FT METAL 64 64 Zinc (By similarity). FT METAL 67 67 Zinc (By similarity). FT METAL 113 113 Zinc (By similarity). FT METAL 116 116 Zinc (By similarity). SQ SEQUENCE 151 AA; 17303 MW; 8D11C52CEB186033 CRC64; MKDRIPIFSV AKNRVEMVER IELSDDEWRE ILDPEAFRVA RKAGTEPPFT GKYHDLHDDG IYRCICCGTD LFDSETKFDS GTGWPSFYDV VSEHNIKLRE DRSLGMVRCE VLCARCDAHL GHVFDDGPRP TGKRYCMNSA ALKFIPRDQI G //