ID MSRAB_HELPY Reviewed; 359 AA. AC O25011; O85224; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 64. DE RecName: Full=Peptide methionine sulfoxide reductase msrA/msrB; DE Includes: DE RecName: Full=Peptide methionine sulfoxide reductase msrA; DE Short=Protein-methionine-S-oxide reductase; DE EC=1.8.4.11; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase; DE Short=Peptide Met(O) reductase; DE Includes: 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=msrAB; Synonyms=msrA; OrderedLocusNames=HP_0224; OS Helicobacter pylori (Campylobacter pylori). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=210; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., RA Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., RA Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., RA Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., RA Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., RA Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., RA Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., RA Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 49503 / 60190; RX MEDLINE=98261556; PubMed=9596777; RA Cao P., McClain M.S., Forsyth M.H., Cover T.L.; RT "Extracellular release of antigenic proteins by Helicobacter pylori."; RL Infect. Immun. 66:2984-2986(1998). CC -!- FUNCTION: Has an important function as a repair enzyme for CC proteins that have been inactivated by oxidation. Catalyzes the CC reversible oxidation-reduction of methionine sulfoxide in proteins CC to methionine (By similarity). CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O = CC L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. CC -!- SIMILARITY: In the N-terminal section; belongs to the msrA Met CC sulfoxide reductase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the msrB Met CC 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; AE000511; AAD07291.1; -; Genomic_DNA. DR EMBL; AF053709; AAC24211.1; -; Genomic_DNA. DR PIR; H64547; H64547. DR RefSeq; NP_207022.1; -. DR HSSP; P14930; 1L1D. DR DIP; DIP:3282N; -. DR GeneID; 900130; -. DR GenomeReviews; AE000511_GR; HP_0224. DR KEGG; hpy:HP0224; -. DR NMPDR; fig|85962.1.peg.220; -. DR TIGR; HP_0224; -. DR HOGENOM; O25011; -. DR OMA; O25011; DERVIYL. DR BRENDA; 1.8.4.11; 1131. DR BRENDA; 1.8.4.12; 1131. 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:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006464; P:protein modification process; IEA:HAMAP. DR HAMAP; MF_01400; fused; 1. DR HAMAP; MF_01401; fused; 1. DR InterPro; IPR002579; Methionine_sulphoxide_MsrB. DR InterPro; IPR002569; MsrA. DR Gene3D; G3DSA:3.30.1060.10; MsrA; 1. DR Gene3D; G3DSA:2.170.150.20; MsrB; 1. DR Pfam; PF01625; PMSR; 1. DR Pfam; PF01641; SelR; 1. DR ProDom; PD004057; DUF25; 1. DR ProDom; PD003489; PMSR; 1. DR TIGRFAMs; TIGR00401; msrA; 1. DR TIGRFAMs; TIGR00357; MsrB; 1. PE 3: Inferred from homology; KW Complete proteome; Multifunctional enzyme; Oxidoreductase. FT CHAIN 1 359 Peptide methionine sulfoxide reductase FT msrA/msrB. FT /FTId=PRO_0000138515. FT REGION 36 189 Peptide methionine sulfoxide reductase A. FT REGION 206 329 Peptide methionine sulfoxide reductase B. FT ACT_SITE 44 44 By similarity. FT ACT_SITE 318 318 By similarity. FT CONFLICT 9 9 N -> I (in Ref. 2; AAC24211). FT CONFLICT 15 15 A -> L (in Ref. 2; AAC24211). FT CONFLICT 23 23 S -> N (in Ref. 2; AAC24211). FT CONFLICT 135 135 A -> T (in Ref. 2; AAC24211). FT CONFLICT 142 142 H -> N (in Ref. 2; AAC24211). FT CONFLICT 170 170 E -> K (in Ref. 2; AAC24211). FT CONFLICT 181 181 S -> G (in Ref. 2; AAC24211). FT CONFLICT 198 198 D -> S (in Ref. 2; AAC24211). FT CONFLICT 346 346 K -> R (in Ref. 2; AAC24211). FT CONFLICT 354 354 N -> Q (in Ref. 2; AAC24211). FT CONFLICT 358 358 S -> T (in Ref. 2; AAC24211). SQ SEQUENCE 359 AA; 41275 MW; D481FAC5C60927B3 CRC64; MKVLSYLKNF YLFLAIGAIM QASENMGSQH QKTDERVIYL AGGCFWGLEA YMERIYGVID ASSGYANGKT SSTNYEKLHE SDHAESVKVI YDPKKISLDK LLRYYFKVVD PVSVNKQGND VGRQYRTGIY YVNSADKEVI DHALKALQKE VKGKIAIEVE PLKNYVRAEE YHQDYLKKHP SGYCHIDLKK ADEVIVDDDK YTKPSDEVLK KKLTKLQYEV TQNKHTEKPF ENEYYNKEEE GIYVDITTGE PLFSSADKYD SGCGWPSFSK PINKDVVKYE DDESLNRKRI EVLSRIGKAH LGHVFNDGPK ELGGLRYCIN SAALRFIPLK DMEKEGYGEF IPYIKKGELK KYINDKKSH //