ID AHPD_MYCTU Reviewed; 177 AA. AC P0A5N4; Q57353; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Alkyl hydroperoxide reductase ahpD; DE EC=1.11.1.15; DE AltName: Full=Alkylhydroperoxidase ahpD; GN Name=ahpD; OrderedLocusNames=Rv2429, MT2504; ORFNames=MTCY428.17c; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RA Zhang Y., Dhandayuthapani S., Deretic V.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). RN [4] RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-130 AND CYS-133. RX PubMed=10766746; DOI=10.1074/jbc.M001001200; RA Hillas P.J., del Alba F.S., Oyarzabal J., Wilks A., RA Ortiz De Montellano P.R.; RT "The AhpC and AhpD antioxidant defense system of Mycobacterium RT tuberculosis."; RL J. Biol. Chem. 275:18801-18809(2000). RN [5] RP SUBUNIT, AND DISULFIDE BONDS. RX PubMed=15178486; DOI=10.1016/j.abb.2004.04.017; RA Koshkin A., Knudsen G.M., Ortiz De Montellano P.R.; RT "Intermolecular interactions in the AhpC/AhpD antioxidant defense RT system of Mycobacterium tuberculosis."; RL Arch. Biochem. Biophys. 427:41-47(2004). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), ACTIVE SITE, AND SUBUNIT. RX PubMed=11914371; DOI=10.1074/jbc.M200864200; RA Nunn C.M., Djordjevic S., Hillas P.J., Nishida C.R., RA Ortiz de Montellano P.R.; RT "The crystal structure of Mycobacterium tuberculosis RT alkylhydroperoxidase AhpD, a potential target for antitubercular drug RT design."; RL J. Biol. Chem. 277:20033-20040(2002). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, SUBUNIT, AND RP MUTAGENESIS OF CYS-130 AND CYS-133. RX PubMed=11799204; DOI=10.1126/science.1067798; RA Bryk R., Lima C.D., Erdjument-Bromage H., Tempst P., Nathan C.; RT "Metabolic enzymes of mycobacteria linked to antioxidant defense by a RT thioredoxin-like protein."; RL Science 295:1073-1077(2002). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS GLN-132 AND PHE-137, RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLU-118; RP CYS-130; HIS-132; CYS-133 AND HIS-137. RX PubMed=12761216; DOI=10.1074/jbc.M303747200; RA Koshkin A., Nunn C.M., Djordjevic S., Ortiz de Montellano P.R.; RT "The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD RT as defined by mutagenesis, crystallography, and kinetics."; RL J. Biol. Chem. 278:29502-29508(2003). CC -!- FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity. CC Required for the reduction of the ahpC active site cysteine CC residues and for the regeneration of the ahpC enzyme activity. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.2; CC -!- SUBUNIT: Homotrimer. Identified in a complex with ahpC and lpd. CC -!- SIMILARITY: Belongs to the ahpD 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; U44840; AAA86657.1; -; Genomic_DNA. DR EMBL; BX842579; CAB03767.1; -; Genomic_DNA. DR EMBL; AE000516; AAK46801.1; -; Genomic_DNA. DR PIR; C70679; C70679. DR RefSeq; NP_216945.1; -. DR RefSeq; NP_336987.1; -. DR PDB; 1GU9; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-177. DR PDB; 1KNC; X-ray; 2.00 A; A/B/C=1-177. DR PDB; 1LW1; X-ray; 2.30 A; A/B/C=1-177. DR PDB; 1ME5; X-ray; 2.40 A; A/B/C=1-177. DR PDBsum; 1GU9; -. DR PDBsum; 1KNC; -. DR PDBsum; 1LW1; -. DR PDBsum; 1ME5; -. DR PeroxiBase; 4558; MtuAhpD. DR GeneID; 885959; -. DR GeneID; 925835; -. DR GenomeReviews; AE000516_GR; MT2504. DR GenomeReviews; AL123456_GR; Rv2429. DR KEGG; mtc:MT2504; -. DR KEGG; mtu:Rv2429; -. DR TIGR; MT2504; -. DR TubercuList; Rv2429; -. DR HOGENOM; P0A5N4; -. DR OMA; P0A5N4; MAMNNVY. DR GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:HAMAP. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01676; -; 1. DR InterPro; IPR004674; AhpD. DR InterPro; IPR004675; AhpD_core. DR InterPro; IPR003779; CMD. DR Pfam; PF02627; CMD; 1. DR TIGRFAMs; TIGR00777; ahpD; 1. DR TIGRFAMs; TIGR00778; ahpD_dom; 1. PE 1: Evidence at protein level; KW 3D-structure; Antioxidant; Complete proteome; Disulfide bond; KW Oxidoreductase; Peroxidase; Redox-active center. FT CHAIN 1 177 Alkyl hydroperoxide reductase ahpD. FT /FTId=PRO_0000064507. FT ACT_SITE 130 130 Proton donor. FT ACT_SITE 133 133 Cysteine sulfenic acid (-SOH) FT intermediate. FT DISULFID 130 133 Alternate. FT DISULFID 133 133 Interchain (with C-61 in ahpC); in linked FT form. FT MUTAGEN 118 118 E->Q: Reduces protein stability. No FT effect on catalytic activity. FT MUTAGEN 130 130 C->S: Loss of activity. FT MUTAGEN 132 132 H->F: Slightly reduced catalytic FT activity. FT MUTAGEN 132 132 H->Q: Slightly reduced catalytic FT activity. FT MUTAGEN 133 133 C->S: Loss of activity. Loss of FT interchain disulfide bond with ahpC. FT MUTAGEN 137 137 H->F: Reduced catalytic activity. FT MUTAGEN 137 137 H->Q: Slightly reduced catalytic FT activity. FT HELIX 5 9 FT HELIX 12 14 FT HELIX 15 25 FT STRAND 28 30 FT HELIX 32 45 FT HELIX 49 59 FT TURN 60 62 FT HELIX 65 90 FT TURN 91 97 FT HELIX 105 108 FT HELIX 114 128 FT HELIX 131 143 FT HELIX 148 174 SQ SEQUENCE 177 AA; 18781 MW; B7DD28AA9BD9B24C CRC64; MSIEKLKAAL PEYAKDIKLN LSSITRSSVL DQEQLWGTLL ASAAATRNPQ VLADIGAEAT DHLSAAARHA ALGAAAIMGM NNVFYRGRGF LEGRYDDLRP GLRMNIIANP GIPKANFELW SFAVSAINGC SHCLVAHEHT LRTVGVDREA IFEALKAAAI VSGVAQALAT IEALSPS //