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Database: UniProt
Entry: B1KPX9_SHEWM
LinkDB: B1KPX9_SHEWM
Original site: B1KPX9_SHEWM 
ID   B1KPX9_SHEWM            Unreviewed;       503 AA.
AC   B1KPX9;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
DE   Flags: Precursor;
GN   OrderedLocusNames=Swoo_3394 {ECO:0000313|EMBL:ACA87662.1};
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA87662.1, ECO:0000313|Proteomes:UP000002168};
RN   [1] {ECO:0000313|EMBL:ACA87662.1, ECO:0000313|Proteomes:UP000002168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000256|ARBA:ARBA00002974}.
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|RuleBase:RU000498};
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, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CP000961; ACA87662.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1KPX9; -.
DR   STRING; 392500.Swoo_3394; -.
DR   KEGG; swd:Swoo_3394; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_6; -.
DR   OMA; HVWPQKQ; -.
DR   Proteomes; UP000002168; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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   CDD; cd08154; catalase_clade_1; 1.
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; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF23; CATALASE-2; 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; 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|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
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   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002168};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..503
FT                   /note="Catalase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002767289"
FT   DOMAIN          25..406
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         353
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   503 AA;  56267 MW;  6B0933E62648407F CRC64;
     MDITKKSCLV LSMSLAFSVQ AETLTRDNGA PVGDNQNSIT AGSNGSVLLQ DVQLIQKLQR
     FARERIPERV VHARGTGVHG EFVASTDLSG LTQAAPFAEK GKVTPVFVRF STVIHSKGSP
     ETLRDPRGFA TRFYSDQGNW DLVGNNLPVF FIRDAIKFPD MVHSLKPSPV TNLQDPNRFF
     DFFSHEGTAT NMLTWVYTNL GTPSSYRKMD GFGVHAYKFI NDENQVKYVK FHWKSQQGVE
     GLRPNEVTKI QGQNFNHLTD DLYSEINKGN YPKWDLKVKV LSPSDLNKFD YNPLDATKMW
     QDVPETTVGT MTLNRVPGNF FQETEQAAFA PSNLIPGIEP SEDKLLQGRI FSYADTQLYR
     LGANLSHLPI NQAKVTVANH NQEGAGNYGH TSSDVNYQPS TKLALTDDSR YRAVNTKLSG
     TVQQAVIKKQ DNFTQAGVLY RSLSKQDKSD LITNLSGDLG KVEDSNVKHQ MLSYFYQADK
     EFGQRLTKAV NGDLKEVKRR AKS
//
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