ID MSRA2_CAUCR Reviewed; 196 AA. AC Q9A9E9; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 16-JUN-2009, entry version 45. DE RecName: Full=Peptide methionine sulfoxide reductase msrA 2; DE Short=Protein-methionine-S-oxide reductase 2; DE EC=1.8.4.11; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase 2; DE Short=Peptide Met(O) reductase 2; GN Name=msrA2; OrderedLocusNames=CC_1039; OS Caulobacter crescentus (Caulobacter vibrioides). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=155892; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19089 / CB15; RX MEDLINE=21173698; PubMed=11259647; DOI=10.1073/pnas.061029298; RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., RA Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J., RA Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J., RA Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L., RA Fraser C.M.; RT "Complete genome sequence of Caulobacter crescentus."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001). 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 -!- SIMILARITY: Belongs to the msrA 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; AE005673; AAK23023.1; -; Genomic_DNA. DR PIR; C87378; C87378. DR RefSeq; NP_419855.1; -. DR HSSP; P96814; 1NWA. DR GeneID; 940574; -. DR GenomeReviews; AE005673_GR; CC_1039. DR KEGG; ccr:CC_1039; -. DR NMPDR; fig|190650.1.peg.1035; -. DR TIGR; CC_1039; -. DR HOGENOM; Q9A9E9; -. DR OMA; Q9A9E9; HFYKKNP. DR BRENDA; 1.8.4.11; 2191. 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_01401; -; 1. DR InterPro; IPR002569; MsrA. DR Gene3D; G3DSA:3.30.1060.10; MsrA; 1. DR Pfam; PF01625; PMSR; 1. DR ProDom; PD003489; PMSR; 1. DR TIGRFAMs; TIGR00401; msrA; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase. FT CHAIN 1 196 Peptide methionine sulfoxide reductase FT msrA 2. FT /FTId=PRO_0000138537. FT ACT_SITE 36 36 By similarity. SQ SEQUENCE 196 AA; 21916 MW; A5A50429EA8D1217 CRC64; MRRLIVLFAA ALAVLGATAP ALAAPKTETA VFAGGCFWCM EHDMQGVPGV LKVESGYTGG HLKNPTYRDV TSETSGHYEA VRVTYDPAKL DYGFLLYRYW RLVDPTDDGG QFCDRGPSYR PAVFVTPAQR PIAEKSRTEA AKRLKTGTMK TQILPAQTFY LAEEYHRDYA KRNKLNYFAY RTGCGRDARL KQVWGG //