CRPE_MYCPA
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 03-AUG-2022, entry version 100.
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; Actinobacteria; Corynebacteriales; 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 2,2'-azino-bis(3-ethylbenzthiazoline-6-
CC sulphonic acid) (ABTS) oxidation assay (at pH 7.0)
CC {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}.
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DR EMBL; AE016958; AAS05061.1; -; Genomic_DNA.
DR RefSeq; WP_003875322.1; NC_002944.2.
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 EnsemblBacteria; AAS05061; AAS05061; MAP_2744c.
DR KEGG; mpa:MAP_2744c; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_045961_0_0_11; -.
DR OMA; QTIDVMN; -.
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 InterPro; IPR018028; Catalase.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR024168; Catalase_SrpA-type_pred.
DR PANTHER; PTHR11465; PTHR11465; 1.
DR Pfam; PF00199; Catalase; 1.
DR PIRSF; PIRSF000296; SrpA; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; SSF56634; 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
