ID B6H094_PENRW Unreviewed; 744 AA.
AC B6H094;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=Catalase-peroxidase {ECO:0000256|HAMAP-Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
DE Short=CP {ECO:0000256|HAMAP-Rule:MF_03108};
DE EC=1.11.1.21 {ECO:0000256|HAMAP-Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
DE AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_03108};
GN Name=katG {ECO:0000256|HAMAP-Rule:MF_03108};
GN ORFNames=Pc12g13740 {ECO:0000313|EMBL:CAP81001.1}, PCH_Pc12g13740
GN {ECO:0000313|EMBL:CAP81001.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP81001.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP81001.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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:0000256|ARBA:ARBA00001378, ECO:0000256|HAMAP-
CC Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
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:0000256|HAMAP-
CC Rule:MF_03108, ECO:0000256|RuleBase:RU003451};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03108};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC {ECO:0000256|HAMAP-Rule:MF_03108};
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:0000256|HAMAP-Rule:MF_03108}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03108,
CC ECO:0000256|RuleBase:RU003451}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03108}.
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DR EMBL; AM920427; CAP81001.1; -; Genomic_DNA.
DR RefSeq; XP_002558181.1; XM_002558135.1.
DR AlphaFoldDB; B6H094; -.
DR STRING; 500485.B6H094; -.
DR PeroxiBase; 6601; PEchCP01.
DR GeneID; 8313752; -.
DR KEGG; pcs:Pc12g13740; -.
DR VEuPathDB; FungiDB:PCH_Pc12g13740; -.
DR eggNOG; ENOG502QTDY; Eukaryota.
DR HOGENOM; CLU_025424_2_0_1; -.
DR OMA; EEIFWGP; -.
DR OrthoDB; 317402at2759; -.
DR BioCyc; PCHR:PC12G13740-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c12.
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 CDD; cd00649; catalase_peroxidase_1; 1.
DR CDD; cd08200; catalase_peroxidase_2; 1.
DR Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
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 NCBIfam; TIGR00198; cat_per_HPI; 1.
DR PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
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 {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_03108};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP-
KW Rule:MF_03108};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03108};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03108};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03108};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_03108}; Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT DOMAIN 126..438
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT BINDING 270
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:0000256|HAMAP-Rule:MF_03108"
FT SITE 89
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
FT CROSSLNK 229..255
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 92)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03108"
SQ SEQUENCE 744 AA; 82347 MW; 8A2C710C2A0A0E27 CRC64;
MSECPVAHKR SNVAGGGTRN TDWWPNSLKL GILRQHTDAT NPQTKDFDYA AAFKTLDYWG
LKKDLHALMT DSQEFWPADF GHYGGLFIRM AWHSAGTYRV FDGRGGGGQG QQRFAPLNSW
PDNVSLDKAR RLLWPIKQKY GNKISWADLL LLTGNVALES MGFKTFGFAG GRPDVWEADE
SVYWGSENVW FTNKARYEAE TAEEEAKQGN IKTRDLEDPL AAVVMGLIYV NPEGPDGNGD
PLSAARDIRI TFGRMAMNDE ETVALIAGGH TFGKTHGAAP ADNVGTEPEA AGIESQGLGW
HNKHGSGVGP HAITSGLEVT WTSTPTKWSN SFLDYLFKFE WEQTKSPAGA TQWVAKNAGD
IVPDAFDSSK KHRPHMLTTD LSLRYDPAYE KISRRFLENP DEFADAFARA WFKLLHRDMG
PRARWLGPEI PKEVSLWEDP IPAPTYALID NGDIIALKNE ILSAGIEPTK LIATAWASAS
TFRGGDKRGG ANGAHIRLAP QKDWDVNNPA QLQEVLGLLE SIQGRFNKAQ NGEKRVSIAD
LIVLAGSAAL ERAAGIPVPF TPGRNDATQE QTDVESFGWL RPFADGFRNY GNSTRRVRTE
QLLIDKAQQL TLSAPELTVL LGGLRSLNAN WDGSSHGVFT SRPGQLSNDF FVNLLDMSTV
WKPTDADSEK FEGFDRKTGA KKWSATRVDL IFGHHAELRA LSELYASSDA QDKFKKDFVA
AWDKVMNLDR YDIPCFPATG RPRL
//
