ID A8GYR7_SHEPA Unreviewed; 504 AA.
AC A8GYR7;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN OrderedLocusNames=Spea_0125 {ECO:0000313|EMBL:ABV85454.1};
OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=398579 {ECO:0000313|EMBL:ABV85454.1, ECO:0000313|Proteomes:UP000002608};
RN [1] {ECO:0000313|EMBL:ABV85454.1, ECO:0000313|Proteomes:UP000002608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700345 / ANG-SQ1 {ECO:0000313|Proteomes:UP000002608};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT "Complete sequence of Shewanella pealeana ATCC 700345.";
RL Submitted (OCT-2007) 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; CP000851; ABV85454.1; -; Genomic_DNA.
DR RefSeq; WP_012153400.1; NC_009901.1.
DR AlphaFoldDB; A8GYR7; -.
DR STRING; 398579.Spea_0125; -.
DR KEGG; spl:Spea_0125; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_6; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000002608; 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:UP000002608};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..504
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002723162"
FT DOMAIN 26..407
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 73
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 354
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 504 AA; 56556 MW; 8B8C5219B328BE0D CRC64;
MEIVKKAGLA LSLSLVVVNV QAETLTRDNG APVGDNQNSI TAGSNGSVLL QDVQLIQKLQ
RFARERIPER VVHARGTGVH GEFIASSDLS ELTQAAPFAE KGKITPVFVR FSTVIHSKGS
PETLRDPRGF ATRFYSDQGN WDLVGNNLPV FFIRDAIKFP DMVHSLKPSP ITNLQDPNRF
FDFFSHEATA TNMLTWVYTN LGTPASYRKM DGWGVHAYKF INDEHQVKYV KFHWKSQQGV
EGLRPDEVVK TQGQNFNHLT DDLYSEINKG NFPKWDLMVK VLRPEDLNKF DYNPLDATKM
WLDVPETKVG TMTLNRVPDN FFQETEQAAF APSNLIPGIE PSEDKLLQGR IFSYADTQLY
RLGANLSQLP INQPKMAVAN HNQEGAANYG RTSSDVNYQP STKLALAEDH RYRAVQTPLS
GTVLQAVIAK QDNFTQAGVL YRSLSKQDKR DLITNLSADL GKVTDSHVKH QMLSYFYQAD
KDFGKRLTQA VAGDLNEVKK LANM
//
