ID B6H2P6_PENRW Unreviewed; 575 AA. AC B6H2P6; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 24-JAN-2024, entry version 76. DE SubName: Full=Pc13g14950 protein {ECO:0000313|EMBL:CAP92564.1}; GN ORFNames=Pc13g14950 {ECO:0000313|EMBL:CAP92564.1}, PCH_Pc13g14950 GN {ECO:0000313|EMBL:CAP92564.1}; 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:CAP92564.1, ECO:0000313|Proteomes:UP000000724}; RN [1] {ECO:0000313|EMBL:CAP92564.1, 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 -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971, CC ECO:0000256|PIRSR:PIRSR038928-2}; CC -!- SIMILARITY: Belongs to the catalase family. CC {ECO:0000256|ARBA:ARBA00005329}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM920428; CAP92564.1; -; Genomic_DNA. DR RefSeq; XP_002559897.1; XM_002559851.1. DR AlphaFoldDB; B6H2P6; -. DR STRING; 500485.B6H2P6; -. DR GeneID; 8314000; -. DR KEGG; pcs:Pc13g14950; -. DR VEuPathDB; FungiDB:PCH_Pc13g14950; -. DR eggNOG; KOG0047; Eukaryota. DR HOGENOM; CLU_010645_0_0_1; -. DR OMA; QVTWLFG; -. DR OrthoDB; 3198922at2759; -. DR BioCyc; PCHR:PC13G14950-MONOMER; -. DR Proteomes; UP000000724; Contig Pc00c13. DR GO; GO:0004096; F:catalase activity; IEA:InterPro. 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 Gene3D; 2.40.180.10; Catalase core domain; 1. DR InterPro; IPR018028; Catalase. DR InterPro; IPR024711; Catalase_clade1/3. DR InterPro; IPR011614; Catalase_core. DR InterPro; IPR010582; Catalase_immune_responsive. DR InterPro; IPR020835; Catalase_sf. DR PANTHER; PTHR11465; CATALASE; 1. DR PANTHER; PTHR11465:SF13; CATALASE (EUROFUNG); 1. DR Pfam; PF00199; Catalase; 1. DR Pfam; PF06628; Catalase-rel; 1. DR PIRSF; PIRSF038928; Catalase_clade1-3; 1. DR PRINTS; PR00067; CATALASE. DR SMART; SM01060; Catalase; 1. DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1. DR PROSITE; PS51402; CATALASE_3; 1. PE 3: Inferred from homology; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2}; KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR038928-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559}; KW Reference proteome {ECO:0000313|Proteomes:UP000000724}. FT DOMAIN 60..439 FT /note="Catalase core" FT /evidence="ECO:0000259|SMART:SM01060" FT REGION 442..467 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 383 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:PIRSR038928-2" SQ SEQUENCE 575 AA; 64807 MW; CCBFFE6BB1A6D4ED CRC64; MATHPLQAIG EAIGAAGADP RVVQRSSLFQ GANDGPAKTA AKITGVQGIA KRADDGPYFT NNEGIPFPDP SHSKTAGGLP LVSDAFLLQK QQHFNRSKNL ERMVHPSEHL GFLRPPRICP PLQKSSNIKT PVFVRFSTVT LGREFPDLAR NPRGFAVKFY TGEGNYDLVG LNFPVFFCRD PIQGPDVIRS QYRNPKNFLL DYNSLFDLLA NTPEGNHAGL MFFSDHGTPA GWRNQHGYGC HTFKWVNASG EFVYVKYHFL VDTGQKQFNA EEALKYGGED PDYSKRDLWS AIEKGEQISY TAHVQIMQPD EADPAKLGFD PFDVTKVWPK KQFPLHEFGR LVLNKNPENF HRDVEQAAFS PGSMVPGIED SPDPLLQFRM FFYRDAQYHR IGVNLHQVPV NCPFMSSSYS SLNFDGPMRV DANHGMNPQY TPNSFTHKFR PDTAETPYQL GDNTVGRKSH FYHEGSPSEY DQPRVLYRDV MDDKARAHLH SNTARLLKLV EYTEIQVKYL AQLARIAPGY AKSVYDLLPE KKFDFMEVEQ RTGGAERAGK EAKFLPSQET DVLRGSCPMK PVYNV //