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Database: UniProt
Entry: A0A1B3Z8T6_9SPHN
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ID   A0A1B3Z8T6_9SPHN        Unreviewed;       689 AA.
AC   A0A1B3Z8T6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=AWL63_07520 {ECO:0000313|EMBL:AOH83837.1};
OS   Sphingomonas panacis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1560345 {ECO:0000313|EMBL:AOH83837.1, ECO:0000313|Proteomes:UP000094256};
RN   [1] {ECO:0000313|EMBL:AOH83837.1, ECO:0000313|Proteomes:UP000094256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCY99 {ECO:0000313|EMBL:AOH83837.1,
RC   ECO:0000313|Proteomes:UP000094256};
RA   Kim Y.J., Yang D.C., Sing P.;
RT   "Complete genome and mega plasmid sequence of Sphingomonas panacis DCY99
RT   elicits systemic resistance in rice to Xanthomonas oryzae.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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. HPII subfamily.
CC       {ECO:0000256|ARBA:ARBA00010660}.
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DR   EMBL; CP014168; AOH83837.1; -; Genomic_DNA.
DR   RefSeq; WP_069204404.1; NZ_CP014168.1.
DR   AlphaFoldDB; A0A1B3Z8T6; -.
DR   STRING; 1560345.AWL63_07520; -.
DR   KEGG; span:AWL63_07520; -.
DR   OrthoDB; 9761719at2; -.
DR   Proteomes; UP000094256; 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   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}.
FT   DOMAIN          26..413
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   BINDING         70
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         109
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         158
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         355
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         359
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"
FT   BINDING         366
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ   SEQUENCE   689 AA;  75266 MW;  ACD8F30DE63BCCFB CRC64;
     MTDFKTSTGN GGETHQQASG DAAVLTTNHG VPVSDNQNSL RSGERGPTLL EDFVLREKIF
     HFDHERIPER IVHARGSGAH GVFEATDDIS DLSKAAVFTK GEKTEVFVRF STVAGGAGSV
     DTPRDVRGFA VKFYTREGNW DLVGNNIPVF FIQDAIKFPD LVHAVKMEAD RAYPQAGSAH
     DTFWDWASLM PESTHMLMWA MSDRTLPRSL RMMEGFGVHT FKLVNAEGKA SFVKFHWKPR
     LGIQSTIWDE ALKLQAADND YHRRDLWESI DTGAFPQWDL GIQVFDQAFA DAQPYDVLDA
     TKLIPEEVVP VRIIGTMTLN RNVDNFFAET EQVAFLPTNI VPGVDFSNDP LLQGRLFSYL
     DTQKSRLGTT NFHQIPVNAP RCPMHNFQRD GMMQTQVPKG RANYEPNSLA AHGEEGGPRE
     SQAGFATVNA ATGPNEQGDK LRIRAETFAD HFSQARLFYR SQDAHEQAHI ASSFVFELSK
     VGVLEQVPPR MVANLRNVDE DLAKRVADGL GIDLPEKAKA AREPVDMAPS DALSIHKNMK
     STLEGRSVGI LIADGTDAAE LDAVIKAVEA EKARAIIVAP KVGGAKLSDG TMRKADGQLA
     GSPSQIFDAV AIILSDAGCK MLLKEAAAVQ FAMDAFGHLK AIGASAAAKP LLDKAGAEPD
     AGVTDLGKAF IAAAKHRFYD REPNVRMLA
//
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