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Database: UniProt/TrEMBL
Entry: A0A0H5NZL1_NOCFR
LinkDB: A0A0H5NZL1_NOCFR
Original site: A0A0H5NZL1_NOCFR 
ID   A0A0H5NZL1_NOCFR        Unreviewed;       719 AA.
AC   A0A0H5NZL1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   28-MAR-2018, entry version 16.
DE   RecName: Full=Catalase {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
GN   Name=katE {ECO:0000313|EMBL:CRY75546.1};
GN   ORFNames=ERS450000_01391 {ECO:0000313|EMBL:CRY75546.1};
OS   Nocardia farcinica.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=37329 {ECO:0000313|EMBL:CRY75546.1, ECO:0000313|Proteomes:UP000057820};
RN   [1] {ECO:0000313|EMBL:CRY75546.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCTC11134 {ECO:0000313|EMBL:CRY75546.1};
RA   Informatics Pathogen;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of
CC       hydrogen peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC         ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; LN868938; CRY75546.1; -; Genomic_DNA.
DR   RefSeq; WP_060591348.1; NZ_LN868938.1.
DR   EnsemblBacteria; CRY75546; CRY75546; ERS450000_01391.
DR   KEGG; nfr:ERS450000_01391; -.
DR   KO; K03781; -.
DR   Proteomes; UP000057820; Chromosome 1.
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   Gene3D; 2.40.180.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR037060; Catalase_core_sf.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56634; SSF56634; 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   Complete proteome {ECO:0000313|Proteomes:UP000057820};
KW   Heme {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|PIRSR:PIRSR038927-2, ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:CRY75546.1};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:CRY75546.1}.
FT   DOMAIN       42    431       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     89     89       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    163    163       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       377    377       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
SQ   SEQUENCE   719 AA;  79148 MW;  EB0D98BDBE0DBF04 CRC64;
     MTGHTPDTPD NAADADHAAG GADRKQRQLD AHRVDREQGH LTTQQGVRVR HTDDALSAGA
     RGPTLLDDFH AREKITHFDH ERIPERVVHA RGAGAYGYFQ PYDDRLAEYT VAKFLTDPAE
     RTPVFVRFST VAGSRGSADT VRDVRGFATK FYTSQGNYDL VGNNFPVFFI QDGIKFPDFV
     HAVKPEPHNE IPQAASAHDT LWDFVSLQPE TLHAIMWLMS DRALPRSYRM MQGFGVHTFR
     FLDAAGTPTF VKFHWTPKLG VHSLVWDECQ QIAGRDPDYN RRDLWDCIEA GHYPEWELGV
     QLIPVEKEFD FDFDLLDATK LVPEEQVPVL PVGRMVLDRN PDNFFAETEQ VAFHTANLVP
     GIDFTDDPLL QLRNFSYLDT QLIRLGGPNF AQIPINRPVA DVRNHQQDGY GQHAIPRGQA
     SYTVNSIGGG CPVVGGDGSY EHYPRQVDGR AQRRRAESFR EYYRQPRMFW RSMSAPEAEH
     IVEAFAFELG KVQRVEIRER TLGQLVRIDP DLAVRVAGRL GLPAPPPDPE AGTDAFVSPA
     LSQAHTAKDG IATRQVAVLA ADGVDAAGVR ALRSALTERG AIVEVIASHG GMVHADGGDG
     DTLPVDRTLM TVASVLYDGV VVAGGQTGVE TLTRNGEAVH FVLEAFKHAK PVAAFGAGVS
     LLRIAGILDA ARVHEADPTT GVITTDTHGD GLDERFVADL ARALANHRTW QRATSAIPA
//
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