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Database: UniProt/TrEMBL
Entry: Q5YW87_NOCFA
LinkDB: Q5YW87_NOCFA
Original site: Q5YW87_NOCFA 
ID   Q5YW87_NOCFA            Unreviewed;       719 AA.
AC   Q5YW87;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   20-JUN-2018, entry version 98.
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=katB {ECO:0000313|EMBL:BAD57554.1};
GN   OrderedLocusNames=NFA_27070 {ECO:0000313|EMBL:BAD57554.1};
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD57554.1, ECO:0000313|Proteomes:UP000006820};
RN   [1] {ECO:0000313|EMBL:BAD57554.1, ECO:0000313|Proteomes:UP000006820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD57554.1,
RC   ECO:0000313|Proteomes:UP000006820};
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD57554.1; -; Genomic_DNA.
DR   RefSeq; WP_011209239.1; NC_006361.1.
DR   ProteinModelPortal; Q5YW87; -.
DR   STRING; 247156.nfa27070; -.
DR   PeroxiBase; 6295; NfaKat01.
DR   EnsemblBacteria; BAD57554; BAD57554; NFA_27070.
DR   KEGG; nfa:NFA_27070; -.
DR   eggNOG; ENOG4105CH6; Bacteria.
DR   eggNOG; COG0753; LUCA.
DR   KO; K03781; -.
DR   OMA; VMWQMSD; -.
DR   OrthoDB; POG091H0424; -.
DR   BioCyc; NFAR247156:NFA_RS13540-MONOMER; -.
DR   Proteomes; UP000006820; Chromosome.
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:UP000006820};
KW   Heme {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-3,
KW   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};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006820}.
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}.
FT   BINDING      86     86       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     127    127       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     176    176       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     373    373       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     384    384       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
SQ   SEQUENCE   719 AA;  79112 MW;  BE926E882CC2EC08 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
     LSQAHTAKDS IATRQVAVLA ADGVDAAGVR ALRSALTERG AIVEVIASHG GMVHADGGDG
     DTLPVDRTLM TVASVLYDGV VVAGGQTGVE TLTRNGEAVH FVLEAFKHAK PVAAFGAGVS
     LLRIAGILDA ARAHDADPAT GVITTEARGD GLDEEFVTDL ARALANHRTW QRATSAIPA
//
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