KATG_MYCPA
ID KATG_MYCPA Reviewed; 748 AA.
AC Q73ZD5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=MAP_1668c;
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]
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).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01961};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC for the catalase, but not the peroxidase activity of the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR EMBL; AE016958; AAS03985.1; -; Genomic_DNA.
DR RefSeq; WP_003877970.1; NC_002944.2.
DR AlphaFoldDB; Q73ZD5; -.
DR SMR; Q73ZD5; -.
DR STRING; 262316.MAP_1668c; -.
DR PeroxiBase; 2712; MavpCP01.
DR PRIDE; Q73ZD5; -.
DR EnsemblBacteria; AAS03985; AAS03985; MAP_1668c.
DR KEGG; mpa:MAP_1668c; -.
DR PATRIC; fig|262316.17.peg.1762; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_11; -.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000000580; Chromosome.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR HAMAP; MF_01961; Catal_peroxid; 1.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR30555; PTHR30555; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..748
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354839"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 279
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT SITE 110
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 113..238
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 264)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 238..264
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 113)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 748 AA; 81750 MW; 4413057EF877C69F CRC64;
MSSDTSASRP PQPDTRTASK SESENPAIPS PHPKSNAPLT NRDWWPNQID VSRLHPHVAE
ANPLGEDFDY AEEFAKLDVE ALKADVISVM TTSQDWWPAD YGHYGGLFIR MSWHAAGTYR
IHDGRGGGGQ GMQRFAPLNS WPDNVSLDKA RRLLWPVKKK YGNKISWADL IIFAGNCALE
SMGFKTFGFA FGREDVWEPE EILWGEEDEW LGTDKRYPGT GERELAQPYG ATTMGLIYVN
PEGPEGKPDP IAAAIDIRET FGRMAMNDEE TAALIVGGHS FGKTHGAGDA DLVGPEPEAA
PIEQQGLGWK SSHGTGVGKD AITSGLEVVW TPTPTKWDNT FLETLYGYEW ELTKSPAGAW
QFTAKDGAGA GTIPDPFGGP GRAPTMLVTD ISLRESPIYR DITRRWLDHP EELADAFAKA
WYKLLHRDMG LVSRFLGPWV PEPQLWQDPV PPVDHPLVDD NDVAALKDKV LASGLSVPQL
VKTAWSAAGS YRNTDKRGGA NGGRLRLQPQ RNWEANEPSE LDKVLPVLEK IQQDFNASAS
GGKKISLADL IVLAGSAAVE KAAKDAGYEI SVHFAPGRTD ASQESTDVDS FAVLEPRADG
FRNFARPGEK APLEQLLLER AYLLGVTGPE MTVLVGGLRA LGANHGGSKH GVFTDRPGAL
TNDFFVNLLD MGTEWKASET AENVYEGHDR ATGALKWTAT ANDLVFGSNS VLRALAEVYA
QDDNQGKFVE DFVAAWVKVM NNDRFDLK
