ID A0A0A2KVR0_PENIT Unreviewed; 725 AA.
AC A0A0A2KVR0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 03-MAY-2023, entry version 33.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN ORFNames=PITC_065770 {ECO:0000313|EMBL:KGO71003.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO71003.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO71003.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO71003.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|RuleBase:RU004142}.
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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=1.11.1.6;
CC Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO71003.1}.
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DR EMBL; JQGA01000985; KGO71003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KVR0; -.
DR STRING; 40296.A0A0A2KVR0; -.
DR HOGENOM; CLU_010645_3_0_1; -.
DR OMA; TTHMQQW; -.
DR OrthoDB; 3198922at2759; -.
DR PhylomeDB; A0A0A2KVR0; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 31..422
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 81
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 368
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|PIRSR:PIRSR038927-2"
SQ SEQUENCE 725 AA; 81595 MW; 0CFA25358B85E9A2 CRC64;
MATNLNSKAA DGKHADLLKD TVDVHAKQHM TTDHGVKISN PDQWLRVVDE KKTGPSLLED
QIAREKIMRF DHERIPERVV HARGTGAFGK FKLFESAADV TTAGVLTDTS RETPLFLRFS
TVQGSRGSAD TVRDVRGFAI KMYTAEGNWD IVGNNIPVFF IQDSIKFPDV IHSVKPEPHN
EVPQGQSAHN NFWDFQYLHS EVTHMNQWIM SDRAIPRSFR MMQGFGVNTY SLINKAGKRH
FVKFHFTPEL GVHSLVWDEA LKIGGQDPDF HRKDLMEAIE AGHFPRWKFG LQLIPEEKAD
NFEFDPLDAT KVWPEELVPI RYIGELELNR NIDEFFPQTE QVAFCTSHIV PGIDFSDDPL
LQGRNFSYFD TQISRLGPNW EELPINRPVC PYMSLVNRDG QGRHRITKGK VNYWPNRFEA
NPPATAEQGG FVSYPQKQQG PKKRALSDKF KEHFNQAQVF YNSLSPIEKM HVAKAFSFEL
DHCDDPVVYK RMTERLSAID LDLAKTVAKN VGGDTPVKAL KENKGIKAKG LSQLEFMPEK
PIIATRRIAI LLADGFDFNQ YTTMKEVLSE RGAFVFTIGA QRQGVTAESG QKVIPDHFYS
GARSTLFDAV YVPGGKHIQA LLKNGVFKHW ISEAFAHLKA IAGANEAVPF IERQIGLPEV
EVAKAGSPLK ESYGVVTGYG DAVSLLKVGT VGPDSKGLAE QFIWHISRHR NWARELDGLS
DQIAA
//
