ID F7VYJ4_SORMK Unreviewed; 720 AA.
AC F7VYJ4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 03-MAY-2023, entry version 59.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN Name=putative cat3 {ECO:0000313|EMBL:CCC10589.1};
GN ORFNames=SMAC_06468 {ECO:0000313|EMBL:CCC10589.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC10589.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC10589.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC10589.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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:0000256|PIRNR:PIRNR038927};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|PIRNR:PIRNR038927}.
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:CCC10589.1}.
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DR EMBL; CABT02000013; CCC10589.1; -; Genomic_DNA.
DR RefSeq; XP_003344267.1; XM_003344219.1.
DR AlphaFoldDB; F7VYJ4; -.
DR STRING; 771870.F7VYJ4; -.
DR GeneID; 10801589; -.
DR KEGG; smp:SMAC_06468; -.
DR VEuPathDB; FungiDB:SMAC_06468; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_3_0_1; -.
DR InParanoid; F7VYJ4; -.
DR OMA; YGDWSNI; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00328; catalase; 1.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF3; CATALASE B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000001881};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..720
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003364660"
FT DOMAIN 56..443
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 102
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 175
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 389
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:PIRSR038927-2"
SQ SEQUENCE 720 AA; 79239 MW; CC98724F1102B354 CRC64;
MRVNALLPLS GLIGTALAAC PFADPSALGR RAEGGEIDAR ERLKEVEVND AGQYMTTDFG
GNVGEQFSLK AGNRGSTLLE DFIFRQKLQH FDHERIPERV VHARGAGAHG IFTSYGDWSN
ITAASFLSAE GKQTPVFVRF STVAGSKGSA DTARDVHGFA TRFYTDEGNF DIVGNNIPVF
FIQDAIRFPD LVHSVKPSPD NEVPQAATAH DSAWDFFSSQ PSALHTLFWA MSGNGIPRSY
RHMDGFGVHT FRLVTEDGKS KLVKWHWKTK QGKAALVWEE AQVLAGKNAD FHRADLWDAI
ESGNAPSWEL AVQLVDEEKA QAYGFDLLDP TKFLPEEFAP LQVLGEMTLN RNPTNYFAET
EQISFQPGHI VRGVDFTEDP LLQGRLYSYL DTQLNRHKGP NFEQLPINRP VSGVHNNHRD
GQGQAWIHKN IHHYTPSYLN KGYPAQANQT VGRGFFTTPG RTASGYLNRE LSATFDDFYT
QPRLFFNSLT PVEQQFVINA IRFEASHVTN EQVKKNVLEQ LNKISNDVAK RVAVALGLEA
PQPDPTYYHN NVTRGVSIFN ETLPTIATLR VGVLATTKGD SLDKAKALKE QLEMDGLKVT
VVAEYLASGV DQTYSAADAT GFDAVVVAEG AERVFSGKGA MSPLFPAGRP SQILTDGYRW
GKPVAAIGSA KKALKSVGVK EKEAGVYSGA QDEVVKGVEE GLKVFKFLER FSVDGDDDEE
//
