ID M7X4E9_RHOT1 Unreviewed; 521 AA.
AC M7X4E9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Catalase {ECO:0000313|EMBL:EMS25201.1};
GN ORFNames=RHTO_02929 {ECO:0000313|EMBL:EMS25201.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS25201.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS25201.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS25201.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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}.
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DR EMBL; KB722643; EMS25201.1; -; Genomic_DNA.
DR RefSeq; XP_016276320.1; XM_016416601.1.
DR AlphaFoldDB; M7X4E9; -.
DR GeneID; 27366942; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_0_0_1; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000016926; 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; 2.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF13; CATALASE (EUROFUNG); 1.
DR Pfam; PF00199; Catalase; 2.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 2.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR038928-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022559};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559}.
FT DOMAIN 61..398
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 341
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 521 AA; 58515 MW; E527B39F1C45BEA5 CRC64;
MASLLQTAET AVLSKIPGAD PRPAQKAQAF SGMNDGPAVT ASRLTGLTQK DVARDDASLY
TTNFGQILPD SAHSLNVGGI PTTIDTALFE KQQTFNRSKT RERIVHPCGS AAFGSFTVTH
DVSKYTKADF SSQAPFFVRE PFMGPDVIRS QQRNPRNFLI DYNAWFDFLA NVPESHYAGA
VLLSDEGTPV GWKHMNGFGC HTFRWTNKEG GSVFVKHHWI CQQEKKNFTY DEAVRMCGED
PDYAKRDLWE YIENGNAARW TMKVQLMTPE EATTVDFDPF DVTKFWPESQ FPLVEVGELK
LDRNPEDYHR DVEQAAFSPG SLVPGIELSP DSLLCWRAWF YRDTQYDRLG SANIHQIPVN
CPFMAKQHSP DNYAGNMRVD GNTLSKPVYF PNSYHSKAPT TDTTPSFDVT AVETPMQVAS
NVLSRKSHYR HEGQPSEYWA AKDFYLNQLD AQGRANLHSN TGRLLKFADE IVKKNYLIQL
YAISPNYANG VYEGLPEKPK TFAMDEVAEA SKTAHLVGKN P
//
