CATA_PICAN
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 03-AUG-2022, entry version 99.
DE RecName: Full=Peroxisomal catalase;
DE EC=1.11.1.6;
GN Name=PXP9; Synonyms=PXP-9;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; 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: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
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:0000255|PROSITE-ProRule:PRU10013};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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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 PDBsum; 2XQ1; -.
DR AlphaFoldDB; P30263; -.
DR SMR; P30263; -.
DR PeroxiBase; 5260; PangKat01.
DR PRIDE; P30263; -.
DR PhylomeDB; P30263; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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 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; PTHR11465; 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; SSF56634; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
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"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2XQ1"
FT HELIX 45..54
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..318
FT /evidence="ECO:0007829|PDB:2XQ1"
FT TURN 319..321
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 STRAND 420..422
FT /evidence="ECO:0007829|PDB:2XQ1"
FT STRAND 425..427
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
