KATG_NOCFA
ID KATG_NOCFA Reviewed; 739 AA.
AC Q5YVJ4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=NFA_29500;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD57797.1; -; Genomic_DNA.
DR RefSeq; WP_011209482.1; NC_006361.1.
DR AlphaFoldDB; Q5YVJ4; -.
DR SMR; Q5YVJ4; -.
DR STRING; 247156.NFA_29500; -.
DR PeroxiBase; 2380; NfaCP01_IFM10152.
DR EnsemblBacteria; BAD57797; BAD57797; NFA_29500.
DR GeneID; 61133670; -.
DR KEGG; nfa:NFA_29500; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_11; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000006820; 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..739
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354851"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Polar residues"
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 270
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 103
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 106..229
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 255)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 229..255
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 106)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 739 AA; 80210 MW; 51B7275E2C4651CB CRC64;
MSVEHPPIGE ANTEPAAGGC PVTGRLRHPL QGGGNHEWWP NQLNLKVLAK NPAEGNPLGD
FDYKAAFNSL DLAAVKADIA EVLTTSQDWW PADFGNYGPL MIRMAWHSAG TYRSSDGRGG
ANTGQQRFAP LNSWPDNGNL DKARRLLWPV KKKYGQNISW ADLMILAGNV ALETMGFKTF
GFAGGRVDVW EPEEDVYWGP EAEWLGDKRY SGERDLENPL AAVQMGLIYV NPEGPNGNPD
PLAAAVDIKD TFGRMGMTVE ETVALIAGGH TFGKTHGAGD AALVGAEPEA APLEQMGLGW
KSSHGTGKGA DAITSGLEVV WTTKPTQWSN DFFEILFGYE WELTKSPAGA NQWVAKDAQP
IIPDPFDPAK KRLPTMLTTD LSLRVDPEME VISRRFKDNP DEFADAFARA WFKLTHRDLG
PVTRYLGPEV PSEVQLWQDP IPAVDHELVD AADIAALKEQ ILASELSISQ LVKTAWAAAS
SFRGSDYRGG ANGGRIRLQP QLGWEVNEPD ELARVIAVLE GIQEQFNAAQ TGNKKVSFAD
LVVLGGVAAV EQAARNAGVA VEVPFTPGRA DTTQELTDPE GFAVLEPKAD GFRNYLGKAN
PLPAEYLLVD KANLLTLTAP EMTVLVGGLR VLNANYQRSP LGVLTETPES LTNDFFVNLL
DMGVVWEPSP ADDGTYVGKD AATGAQKWTG SRVDLLFGSN SVLRSLAEVY ATDDAKPKFV
QDFVAAWNKV MNLDRFDLA
