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Database: UniProt
Entry: G2X056_VERDV
LinkDB: G2X056_VERDV
Original site: G2X056_VERDV 
ID   G2X056_VERDV            Unreviewed;       587 AA.
AC   G2X056;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   03-MAY-2023, entry version 43.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:EGY21639.1};
GN   ORFNames=VDAG_03079 {ECO:0000313|EMBL:EGY21639.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY21639.1, ECO:0000313|Proteomes:UP000001611};
RN   [1] {ECO:0000313|Proteomes:UP000001611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC   {ECO:0000313|Proteomes:UP000001611};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS572699; EGY21639.1; -; Genomic_DNA.
DR   RefSeq; XP_009655239.1; XM_009656944.1.
DR   AlphaFoldDB; G2X056; -.
DR   STRING; 498257.G2X056; -.
DR   EnsemblFungi; EGY21639; EGY21639; VDAG_03079.
DR   GeneID; 20704542; -.
DR   KEGG; vda:VDAG_03079; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_0_0_1; -.
DR   InParanoid; G2X056; -.
DR   OMA; QVTWLFG; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000001611; Chromosome 6.
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; IPR024708; Catalase_AS.
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:SF13; CATALASE (EUROFUNG); 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; PS00438; CATALASE_2; 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:UP000001611}.
FT   DOMAIN          69..455
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   BINDING         399
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   587 AA;  66167 MW;  F62703FF50CB715E CRC64;
     MNVNSNQVDP AQHPLRATAM AIGSQVTGER RAPRVSHMQS ANEGPADIIG KVSGAVPGGK
     REDDGAYFTN NEGHPLPDPA HSKTVGGIPV ASDIHLFQKQ QTFNRSKNLE RMVHPCGSGA
     FGFFECTHDV TDLTKADFLS SVGEKTPAFV RFSTVTFGRE FPDEGRNPRG FAIKLYTMEG
     NQDIVGLNFP VFFCRDPLQG PDVIRSQSRN PTNFLLDFDA LFDLLANTPE SNHAGLMFFS
     DHGTPQGWRF NHGYGCHAFK WVNKEGRFVY VKYHFIAKHG QKQFTDGEAV QMCGEDPDYS
     KRDLWTAIEK GEAIEWTAHV QVMQPEEADA DKLGFDPFDV TKVWPRGRFP MRPYGRLVLN
     KNPEDFHRDV EQAAFSPGSM VPGIEDAPDP LLQFRMFFYR DAQYHRIGVN LHQIPVNCPF
     MAQSYAPLNF DGALRADANH AGNKQYAPNS FAHKFRPDAA EAPYAVGDSI VSRRSHFWHE
     GKRNDYDQAT ALWTRVMSPQ ARQNTCHNTA KYLGLVQYPE IQAKYLAQLY NISPDYAQGV
     FDRLREHAFS MDEVKAKAED AHTWYREKKF LPSHESKLAG YPVSGYN
//
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