ID CATA_PICAN Reviewed; 507 AA. AC P30263; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 02-SEP-2026, entry version 107. DE RecName: Full=Peroxisomal catalase; DE EC=1.11.1.6 {ECO:0000255|PROSITE-ProRule:PRU10013}; GN Name=PXP9; Synonyms=PXP-9; OS Pichia angusta (Yeast) (Hansenula polymorpha). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes; OC Pichiales; Pichiaceae; Ogataea. OX NCBI_TaxID=870730; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL RC Y-5445; RX PubMed=1607006; DOI=10.1016/0014-5793(92)80500-g; RA Didion T., Roggenkamp R.O.; RT "Targeting signal of the peroxisomal catalase in the methylotrophic yeast RT Hansenula polymorpha."; RL FEBS Lett. 303:113-116(1992). CC -!- FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) CC generated by peroxisomal oxidases to water and oxygen, thereby CC protecting cells from the toxic effects of hydrogen peroxide. CC {ECO:0000250|UniProtKB:P04040}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H2O2 = O2 + 2 H2O; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000250|UniProtKB:P15202}; CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P15202}. CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}. 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; X56501; CAA39856.1; -; Genomic_DNA. DR PIR; S23422; S23422. DR PDB; 2XQ1; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-507. DR AlphaFoldDB; P30263; -. DR SMR; P30263; -. DR PeroxiBase; 5260; PangKat01. DR PhylomeDB; P30263; -. DR EvolutionaryTrace; P30263; -. DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter. DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB. DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter. DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:TreeGrafter. DR CDD; cd08157; catalase_fungal; 1. DR FunFam; 2.40.180.10:FF:000001; Catalase; 1. DR Gene3D; 2.40.180.10; Catalase core domain; 1. DR InterPro; IPR018028; Catalase. DR InterPro; IPR024708; Catalase_AS. DR InterPro; IPR024711; Catalase_clade1/3. DR InterPro; IPR011614; Catalase_core. DR InterPro; IPR002226; Catalase_haem_BS. DR InterPro; IPR010582; Catalase_immune_responsive. DR InterPro; IPR020835; Catalase_sf. DR PANTHER; PTHR11465; CATALASE; 1. DR PANTHER; PTHR11465:SF9; CATALASE; 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; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. DR PROSITE; PS51402; CATALASE_3; 1. DR PDBsum; 2XQ1; -. PE 1: Evidence at protein level; KW 3D-structure; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; KW Peroxidase; Peroxisome. FT CHAIN 1..507 FT /note="Peroxisomal catalase" FT /id="PRO_0000084926" FT MOTIF 505..507 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255" FT ACT_SITE 65 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013" FT ACT_SITE 138 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013" FT BINDING 348 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:0000250|UniProtKB:P04040" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 45..54 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 67..77 FT /evidence="ECO:0007829|PDB:2XQ1" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 96..104 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 121..128 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 131..141 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 151..158 FT /evidence="ECO:0007829|PDB:2XQ1" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 169..178 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 183..190 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 210..213 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 219..228 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 237..246 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 250..261 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 266..274 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 276..279 FT /evidence="ECO:0007829|PDB:2XQ1" FT TURN 295..297 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 301..310 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 315..320 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 339..355 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 364..366 FT /evidence="ECO:0007829|PDB:2XQ1" FT TURN 388..391 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 405..407 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 420..422 FT /evidence="ECO:0007829|PDB:2XQ1" FT STRAND 425..427 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 433..436 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 437..445 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 452..464 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 469..479 FT /evidence="ECO:0007829|PDB:2XQ1" FT TURN 480..482 FT /evidence="ECO:0007829|PDB:2XQ1" FT HELIX 484..499 FT /evidence="ECO:0007829|PDB:2XQ1" SQ SEQUENCE 507 AA; 57849 MW; 3536ED0A49539CC3 CRC64; MSNPPVFTTS QGCPVSDPFT TQRIPLDSTG YKYAPPIGPL LLQDFKLIDT LSHFDRERIP ERVVHAKGAG AYGVFEVTDD ITDVCSAKFL DTVGKKTRIF TRFSTVGGEK GSADTARDPR GFATKFYTED GNLDLVYNNT PIFFIRDPIK FPHFIHTQKR NPATNLKDPN MFWDYLTAND ESLHQVMYLF SNRGTPASYR TMNGYSGHTY KWYNSKGEWV YVQVHFIANQ GVHNLLDEEA GRLAGEDPDH STRDLWEAIE KGDYPSWECY IQTMTLEQSK KLPFSVFDLT KVWPHKDFPL RHFGRFTLNE NPKNYYAETE QIAFSPSHTV PGMEPSNDPV LQSRLFSYPD THRHRLGPNY HQIPVNCPLK SGSFNPINRD GPMCVDGNLG GTPNYANAYN CPIQYAVSPK ASGNKPDEKY TGEVVPYHWE HTDYDYFQPK MFWKVLGRTP GEQESLVKNV ANHVSAADEF IQDRVYEYFS KAEPIIGDLI RKKVQELKRK ASSPSKI //