ID BCP_HELPJ Reviewed; 152 AA. AC Q9ZMU4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 04-NOV-2008, entry version 42. DE RecName: Full=Putative peroxiredoxin bcp; DE EC=1.11.1.15; DE AltName: Full=Thioredoxin reductase; DE AltName: Full=Bacterioferritin comigratory protein homolog; GN Name=bcp; OrderedLocusNames=jhp_0124; OS Helicobacter pylori J99 (Campylobacter pylori J99). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=99120557; PubMed=9923682; DOI=10.1038/16495; RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., RA Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., RA Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., RA Trust T.J.; RT "Genomic sequence comparison of two unrelated isolates of the human RT gastric pathogen Helicobacter pylori."; RL Nature 397:176-180(1999). CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SIMILARITY: Belongs to the ahpC/TSA family. CC -!- SIMILARITY: Contains 1 thioredoxin domain. 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; AE001439; AAD05701.1; -; Genomic_DNA. DR PIR; F71971; F71971. DR RefSeq; NP_222845.1; -. DR HSSP; P32119; 1QMV. DR GeneID; 889445; -. DR GenomeReviews; AE001439_GR; jhp_0124. DR KEGG; hpj:jhp0124; -. DR NMPDR; fig|85963.1.peg.123; -. DR HOGENOM; Q9ZMU4; -. DR BioCyc; HPYL85963:JHP0124-MON; -. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000866; AhpC-TSA. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Peroxidase; Redox-active center. FT CHAIN 1 152 Putative peroxiredoxin bcp. FT /FTId=PRO_0000135139. FT DOMAIN 4 152 Thioredoxin. FT ACT_SITE 46 46 By similarity. SQ SEQUENCE 152 AA; 17146 MW; 46DFE89F70D05DA1 CRC64; MEKLEVGQLA PDFRLKNSDG VEISLKDLLH KKVVLYFYPK DNTPGCTLEA KDFSALFSEF EKKNAVVVGV SPDNSQSHQK FISQCSLNVI LLCDEDKKVA NLYKAYGKRM LYGKEHLGII RSTFIINTQG VLEKCFYNVK AKGHAQKVLE SL //