ID D5G9V6_TUBMM Unreviewed; 756 AA.
AC D5G9V6;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 ORFNames=GSTUM_00005092001 {ECO:0000313|EMBL:CAZ81299.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ81299.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ81299.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ81299.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|RuleBase:RU004142}.
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 ECO:0000256|RuleBase:RU000498};
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 ECO:0000256|RuleBase:RU000498}.
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DR EMBL; FN430064; CAZ81299.1; -; Genomic_DNA.
DR RefSeq; XP_002837108.1; XM_002837062.1.
DR AlphaFoldDB; D5G9V6; -.
DR STRING; 656061.D5G9V6; -.
DR EnsemblFungi; CAZ81299; CAZ81299; GSTUM_00005092001.
DR GeneID; 9188542; -.
DR KEGG; tml:GSTUM_00005092001; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_3_0_1; -.
DR InParanoid; D5G9V6; -.
DR OMA; WQMSDRA; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000006911; 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; 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; IPR002226; Catalase_haem_BS.
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:SF1; 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; SSF52317; Class I glutamine amidotransferase-like; 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.
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:UP000006911}.
FT DOMAIN 51..443
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 103
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 176
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 390
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 756 AA; 84520 MW; AE1F46E4CEA2055D CRC64;
MTGVFQRLQE SLNEAKIAAA HKVNEVASTN EKIVEMWPNK VSVEKSGNRL TTDSGTGVYD
VDHWLKVVDP STGHHGPSLL EDQIARERIH RFDHERIPER VVHARGAGAH GYFNLHTPIP
EFSSATVLND TGRSTPIFAR MSTVAGSRGS ADTVRDVRGF ALKFYTEEGN WDIVGNNIPV
FFIQDAIKFP DFVHAVKPEP HNEVPQAQTA HNNFWDFMYM HSESTHMSIW AMSDRGIPRS
YRMMQGFGVN TFSLINAQGE RTFVKFVWTP ELGVHSLVWD EALKLAGQDP DFHRKDLYEA
IENGYYPKWQ FGIQTIAEKD QDKFEFDILD ATKVWPEDLV PINYIGELVL NRNVDEFFAE
TEQAAFCTSH VVPGIGFSDD PLLQGRNFSY FDTQITRLGI NWEQLPINRP VCPIMNFNRD
GALNHRIHKG KVNYWPNRFE AVPPASHKQE TDSYQECAAK VAGLKLRVNG AKFREHFAQA
QLFYNSLAKH EKKHVEAALA FELSHCDEPI VYKRMSERLA DIDLTLAQNV AKMVGGDIPK
EGRLNHGRKA PGLSQADLPA VKPSIKSRRV AMIVADGFEM GVFTAVRAAL KAEGATTWVI
APRRGMIFPA GVHPESGTGG LLADHHLEGQ RSTMFDAIFV CPGTRSTLTL RENGRAVHWV
REAFGHLKPI GVLGDAVSFL QQAVVLPGVD VAADPNSHDV VTSYGVVTGW RCSVGVLRSL
KIEPSTCAFS SAFAYEISKH RCWARELDGL HTKLAF
//
