KATG2_MYCFO
ID KATG2_MYCFO Reviewed; 733 AA.
AC O08405;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=katGII;
OS Mycolicibacterium fortuitum (Mycobacterium fortuitum).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1766;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6841 / DSM 46621 / CIP 104534 / JCM 6387 / KCTC 9510 / NBRC
RC 13159 / NCTC 10394;
RX PubMed=9371430; DOI=10.1128/jb.179.22.6880-6886.1997;
RA Menendez M.C., Ainsa J.A., Martin C., Garcia M.J.;
RT "katGI and katGII encode two different catalases-peroxidases in
RT Mycobacterium fortuitum.";
RL J. Bacteriol. 179:6880-6886(1997).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. May play a role in the intracellular survival of
CC mycobacteria (By similarity). {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; Y07866; CAA69193.1; -; Genomic_DNA.
DR STRING; 1766.XA26_57680; -.
DR PeroxiBase; 3128; MfoCP02.
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.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..733
FT /note="Catalase-peroxidase 2"
FT /id="PRO_0000345093"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 275
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 /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT SITE 103
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 106..234
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 260)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 234..260
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 106)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 733 AA; 80596 MW; 20C8BCB076F9E58F CRC64;
MAEAETHPPI GESQTEPAES GCPMRIKPPV EGGSNRDWWP NAVNLKILQK NPPAIDPSDE
GYDSEAVKSL DVEAFQRDFD ELLTNSQDWW PADFGHYGPL FVRMSWHAAG TYRVEDGRGG
GGRGMQPFAP LNSWPDNVSL DKARRLLWPL KKKYGKQISW SDLIVYSGNR AMEHMGFKTA
GFAFGRPDYW EPEEDIYWGA EAEWLGSQDR YAGANGDRTK LENPPXXPHM GLIYVNPEGP
EGNPDYLAAA IDIRETFGRM AMNDIETAAL IVGGHTFGKT HGATDIENGV EPEXXPLEQM
GLGWANPGLG NDTVSSGLEV TWTQHPTKWD NSFLEILYSN EWELTKSPAG ANQWKPKDNG
WANSWPMAQG TGKTHPSMLT TDLSMRFDPI YGEITRRWLD HPEELAEEYA KAWFKLIHRD
MGPVTRYLGP LVPKQTWLWQ DIIPAGKQLS DADVATLKAA IADSGLSIQQ LVNTAWKAAA
SYRSSDMRGG NGGRIRLQPQ LGWEVNEPEE LAPVIAKLEE IQAASDSGVS FADLVVLGGV
VGLEKAIKAA GFDVAVPFTS GPRDALQEQT DVDSFAYLEP KGDGFRNFVA KGDSVPAEYR
LIDRANLLGL SAPQMTVLIG GLRVLGANHG GSELGVLTDK VGQLTNDYFV NLTDMGTKWA
PAPADDGTYV GTDRATGSPK WTASRVDLLF GSNSQLRALA EVYAEDDSKE KFVKDFVAAW
TKVMNADRFD LEA
