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Database: UniProt
Entry: A0A0P7GSK0_9MICC
LinkDB: A0A0P7GSK0_9MICC
Original site: A0A0P7GSK0_9MICC 
ID   A0A0P7GSK0_9MICC        Unreviewed;       496 AA.
AC   A0A0P7GSK0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=AO716_02225 {ECO:0000313|EMBL:KPN21850.1};
OS   Arthrobacter sp. Edens01.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1732020 {ECO:0000313|EMBL:KPN21850.1, ECO:0000313|Proteomes:UP000054460};
RN   [1] {ECO:0000313|EMBL:KPN21850.1, ECO:0000313|Proteomes:UP000054460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edens01 {ECO:0000313|EMBL:KPN21850.1,
RC   ECO:0000313|Proteomes:UP000054460};
RA   Couger M.B.;
RT   "Draft Genome of Arthrobacter sp. strain Edens01.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPN21850.1}.
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DR   EMBL; LKIU01000002; KPN21850.1; -; Genomic_DNA.
DR   RefSeq; WP_055239264.1; NZ_LKIU01000002.1.
DR   AlphaFoldDB; A0A0P7GSK0; -.
DR   STRING; 1732020.AO716_02225; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000054460; Unassembled WGS sequence.
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   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:SF9; CATALASE; 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:UP000054460}.
FT   DOMAIN          6..389
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         335
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   496 AA;  54997 MW;  9936C6B899805E77 CRC64;
     MSNFTTTQTG TPVASDAHSL SHGADGAVVL HDRYLVEKLA QFNRERIPER IVHAKGGGAF
     GEFTVTEDVS MYTRAAVFQP GTTTETIQRF SSVAGEMGSP DTWRDVRGFA LRFYSSEGNY
     DIVGNNTPVF FIRDGIKFPD FIHSQKRLPG SGLRDADMQW DFWTNSPESA HQVTYLMGDR
     GIPRSWREMP GFGSHTYQWI NAAGERFWVK YHFTSNQGNH EITGAEAERI AGADADYYRR
     DLYENIAAGN FPSWDLHVQV MPYDDAKNYR FNPFDLTKVW PHADYPLIKV GTHTLNRNPE
     NFFAQIEQVA LSPANLVPGI AASPDKMLMA RIFSYPDAQR YRVGTNYNQL PVNAPKAPVN
     NYSQDGSGRF FFNSPETPVY APNTLGGPVA DPALAGEGTW ENDGALVRSA ATLHSEDSDF
     GQAGTLYREV FDDAAKARFL ETITGAVSGV QRPHIREAAI QYWTNVDADL GAKLRANLAT
     GETTANEQAE FVGVAD
//
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