ID CRPE_MYCPA Reviewed; 313 AA. AC Q73WB6; DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=Catalase-related peroxidase {ECO:0000303|PubMed:19827095}; DE EC=1.11.1.- {ECO:0000269|PubMed:19827095}; GN OrderedLocusNames=MAP_2744c; OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) OS (Mycobacterium paratuberculosis). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium avium complex (MAC). OX NCBI_TaxID=262316; RN [1] {ECO:0000312|EMBL:AAS05061.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10; RX PubMed=16116077; DOI=10.1073/pnas.0505662102; RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., RA Kanjilal S., Kapur V.; RT "The complete genome sequence of Mycobacterium avium subspecies RT paratuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005). RN [2] {ECO:0000305} RP MAGNETIC CIRCULAR DICHROISM, AND COFACTOR. RX PubMed=22104301; DOI=10.1016/j.jinorgbio.2011.09.026; RA Bandara D.M., Sono M., Bruce G.S., Brash A.R., Dawson J.H.; RT "Coordination modes of tyrosinate-ligated catalase-type heme enzymes: RT magnetic circular dichroism studies of Plexaura homomalla allene oxide RT synthase, Mycobacterium avium ssp. paratuberculosis protein-2744c, and RT bovine liver catalase in their ferric and ferrous states."; RL J. Inorg. Biochem. 105:1786-1794(2011). RN [3] {ECO:0000305, ECO:0000312|PDB:3E4W} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION, RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=19827095; DOI=10.1002/pro.265; RA Pakhomova S., Gao B., Boeglin W.E., Brash A.R., Newcomer M.E.; RT "The structure and peroxidase activity of a 33-kDa catalase-related protein RT from Mycobacterium avium ssp. paratuberculosis."; RL Protein Sci. 18:2559-2568(2009). CC -!- FUNCTION: Has an organic peroxide-dependent peroxidase activity. CC Exhibits strong peroxidase activity using organic hydroperoxides as CC cosubstrates, weak peroxidase activity using hydrogen peroxide and CC negligible catalase activity. May have a role in elimination of CC reactive oxygen species, in particular by deactivating hydroperoxides. CC {ECO:0000269|PubMed:19827095}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000269|PubMed:19827095, ECO:0000269|PubMed:22104301}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=30 mM for H(2)O(2) in CC 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) CC oxidation assay (at pH 7.0) {ECO:0000269|PubMed:19827095}; CC KM=22 mM for t-butyl hydroperoxide in ABTS oxidation assay (at pH CC 7.0) {ECO:0000269|PubMed:19827095}; CC KM=3 mM for cumene hydroperoxide in ABTS oxidation assay (at pH 7.0) CC {ECO:0000269|PubMed:19827095}; CC KM=49 uM for 9S-hydroperoxy-octadecadienoic acid (9S-HPODE) used as a CC cosubstrate with ABTS (at pH 7.0) {ECO:0000269|PubMed:19827095}; CC Note=kcat is 13 sec(-1) for H(2)O(2). kcat is 320 sec(-1) for t-butyl CC hydroperoxide. kcat is 330 sec(-1) for cumene hydroperoxide. kcat is CC 529 sec(-1) for 9S-HPODE. {ECO:0000269|PubMed:19827095}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19827095}. CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016958; AAS05061.1; -; Genomic_DNA. DR RefSeq; WP_003875322.1; NZ_CP106873.1. DR PDB; 3E4W; X-ray; 1.80 A; A/B=1-313. DR PDB; 3E4Y; X-ray; 2.60 A; A=1-313. DR PDBsum; 3E4W; -. DR PDBsum; 3E4Y; -. DR AlphaFoldDB; Q73WB6; -. DR SMR; Q73WB6; -. DR STRING; 262316.MAP_2744c; -. DR KEGG; mpa:MAP_2744c; -. DR eggNOG; COG0753; Bacteria. DR HOGENOM; CLU_045961_0_0_11; -. DR EvolutionaryTrace; Q73WB6; -. DR Proteomes; UP000000580; Chromosome. DR GO; GO:0004096; F:catalase activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB. DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB. DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IDA:UniProtKB. DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IDA:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR CDD; cd08153; srpA_like; 1. DR Gene3D; 1.20.1280.120; -; 1. DR Gene3D; 2.40.180.10; Catalase core domain; 1. DR InterPro; IPR018028; Catalase. DR InterPro; IPR011614; Catalase_core. DR InterPro; IPR020835; Catalase_sf. DR InterPro; IPR024168; Catalase_SrpA-type_pred. DR PANTHER; PTHR11465; CATALASE; 1. DR PANTHER; PTHR11465:SF9; CATALASE; 1. DR Pfam; PF00199; Catalase; 1. DR PIRSF; PIRSF000296; SrpA; 1. DR PRINTS; PR00067; CATALASE. DR SMART; SM01060; Catalase; 1. DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1. DR PROSITE; PS51402; CATALASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Heme; Iron; Metal-binding; Oxidoreductase; Peroxidase; KW Reference proteome. FT CHAIN 1..313 FT /note="Catalase-related peroxidase" FT /id="PRO_0000424152" FT ACT_SITE 28 FT /evidence="ECO:0000250|UniProtKB:P04040" FT BINDING 294 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT HELIX 7..16 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 30..40 FT /evidence="ECO:0007829|PDB:3E4W" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:3E4W" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 57..69 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 81..88 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 94..101 FT /evidence="ECO:0007829|PDB:3E4W" FT HELIX 110..119 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:3E4W" FT HELIX 126..136 FT /evidence="ECO:0007829|PDB:3E4W" FT HELIX 138..141 FT /evidence="ECO:0007829|PDB:3E4W" FT HELIX 144..150 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:3E4W" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 162..171 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 177..188 FT /evidence="ECO:0007829|PDB:3E4W" FT HELIX 195..199 FT /evidence="ECO:0007829|PDB:3E4W" FT HELIX 205..216 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 219..227 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 246..257 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 260..263 FT /evidence="ECO:0007829|PDB:3E4W" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:3E4W" FT HELIX 285..302 FT /evidence="ECO:0007829|PDB:3E4W" SQ SEQUENCE 313 AA; 33321 MW; 7EE2BE95125CD14E CRC64; MSGGLTPDQA IDAIRGTGGA QPGCRALHAK GTLYRGTFTA TRDAVMLSAA PHLDGSTVPA LIRFSNGSGN PKQRDGAPGV RGMAVKFTLP DGSTTDVSAQ TARLLVSSTP EGFIDLLKAM RPGLTTPLRL ATHLLTHPRL LGALPLLREA NRIPASYATT EYHGLHAFRW IAADGSARFV RYHLVPTAAE EYLSASDARG KDPDFLTDEL AARLQDGPVR FDFRVQIAGP TDSTVDPSSA WQSTQIVTVG TVTITGPDTE REHGGDIVVF DPMRVTDGIE PSDDPVLRFR TLVYSASVKL RTGVDRGAQA PPV //