(data stored in SCRATCH zone)

SWISSPROT: Q4ZZR9_PSEU2

ID   Q4ZZR9_PSEU2            Unreviewed;       716 AA.
AC   Q4ZZR9;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 94.
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   OrderedLocusNames=Psyr_0280 {ECO:0000313|EMBL:AAY35353.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35353.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35353.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35353.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of
CC       hydrogen peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240;
CC         EC=1.11.1.6; Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC         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; CP000075; AAY35353.1; -; Genomic_DNA.
DR   RefSeq; WP_011266295.1; NC_007005.1.
DR   RefSeq; YP_233391.1; NC_007005.1.
DR   STRING; 205918.Psyr_0280; -.
DR   EnsemblBacteria; AAY35353; AAY35353; Psyr_0280.
DR   GeneID; 3365756; -.
DR   KEGG; psb:Psyr_0280; -.
DR   PATRIC; fig|205918.7.peg.281; -.
DR   eggNOG; COG0753; LUCA.
DR   HOGENOM; HOG000087851; -.
DR   KO; K03781; -.
DR   OMA; VMWQMSD; -.
DR   BioCyc; PSYR205918:G1G4J-281-MONOMER; -.
DR   Proteomes; UP000000426; 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; IPR041399; Catalase_large_C.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   PANTHER; PTHR42821; PTHR42821; 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; 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;
DR   PRODOM; Q4ZZR9.
DR   SWISS-2DPAGE; Q4ZZR9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
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, ECO:0000313|EMBL:AAY35353.1};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:AAY35353.1}.
FT   DOMAIN       48    436       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     95     95       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    168    168       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       382    382       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
FT   BINDING      92     92       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     132    132       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     181    181       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     378    378       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     389    389       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
SQ   SEQUENCE   716 AA;  78966 MW;  A1257CE18F2EE4C6 CRC64;
     MASKNAPPVT ETPKSEMAGT DTLDRGNTNE KLESLEQFRS DATQQALRTN HGVKISDNQN
     TLKVGSRGPS LLEDFIMREK ITHFDHERIP ERIVHARGTA AHGYFQTYED HGALSKAGFL
     RDPGKKTPVF VRFSTVQGPR GSGDTVRDVR GFAVKLYTDE GNFDLVGNNM PVFFIQDAIK
     FPDFVHAVKP EPHNEIPTGG SAHDTFWDFV SLVPESAHMV LWTMSDRAIP KSLRTMQGFG
     IHTFRFINTE GKSSFVKFHW KPKFGVCSLV WDEAQKLAGK DTDFHRRDLW ESIEMGDYPE
     WELGVQIVAE EDEHKFDFDL LDPTKIIPEE LVPVTPLGKM VLNRNPDNYF AETEQVAFCP
     GHIVPGIDFS NDPLLQGRLF SYTDTQISRL GGPNFHEIPI NRPIAPNHNG QRDAQHRTTI
     DKGRASYEPN SIDGGWPKET PAGPVDGGFE TYPERVEAHK VRERSESFGD HFSQATLFFQ
     SMSHHEKEHI IAAYSFELGK VEREYIRARQ VNEILANIDM DLAKRVAANL GLPAPAAGTV
     PARQTSVKES PALSQVNLLS GDIVSRKVAI LVADGVDGKA VEAMKAALTA EGAHAKVLGP
     TSAPVKTADG KSLPVDASAE GLPSVAFDAV FVPGGKASIE ALKGDGVALH FILEAYKHLK
     AISFAGEAKE LLSLLRLEED AGLLEVSDST SFKPFFHAIA QHRVWDREAK AKAVPA
//

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