ID A0A2N5RXY7_9BASI Unreviewed; 537 AA.
AC A0A2N5RXY7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=Catalase core domain-containing protein {ECO:0000259|SMART:SM01060};
GN ORFNames=PCANC_26767 {ECO:0000313|EMBL:PLW05792.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW05792.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW05792.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW05792.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:PLW05792.1}.
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DR EMBL; PGCJ01001388; PLW05792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5RXY7; -.
DR STRING; 200324.A0A2N5RXY7; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
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: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; 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:UP000235388}.
FT DOMAIN 63..435
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 110
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 184
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 392
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 537 AA; 59153 MW; AE88E042E9E9C2D1 CRC64;
MFRISTQVLI CTASYNLLPY IIQHCSGSSI LLNETTPSPN LQAGQGTLNI SSFTIPKLSS
VLPSINSSAI ALKSVSGLID KPTPTTPLSA DALAKQSEFN HKNIPARPVH ASGAGAHGTF
TVTTNFAQSH TMMDLFSNVS KKTPVTVRLS NGLGEKGSFD TARNLRGFAV KFQTRQGDWD
LVSNNAPVFF VRDPAKFPPL FQSQGRDPVT NFGNPDAAFN YFPENPETMN LFLRIFSSAG
TSKGWIHTNA WSTNTYRWYK SDGTWSYVRI NLEAKQEVSN FSAAEQSQIT DPSYGARELY
TSIQSGQFPR WTMFSQVLSP KDAENFRYNV LDDTKEWPAS LVAPQEIGIL ELNKNPDNYF
NDVEKLAFSP ANVVPGWAAS QDPVLQMRLF AYGDSSRYRL SERSAPLKTQ RRSLLKDQML
NSPAQILKNS AHILNNSPSI VNTSTATTAP NYDPAHILWI NQALKSMIQI SPIDFEQPAF
FYGNLTQNER LELVQNVAGG LSVVSSPDIK TNLISWLAKA SPDLSQAVSS TLKSITA
//
