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Database: UniProt
Entry: K9AHS4_9MICO
LinkDB: K9AHS4_9MICO
Original site: K9AHS4_9MICO 
ID   K9AHS4_9MICO            Unreviewed;       493 AA.
AC   K9AHS4;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=C272_14013 {ECO:0000313|EMBL:EKU45666.1};
OS   Brevibacterium casei S18.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=1229781 {ECO:0000313|EMBL:EKU45666.1, ECO:0000313|Proteomes:UP000009879};
RN   [1] {ECO:0000313|EMBL:EKU45666.1, ECO:0000313|Proteomes:UP000009879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S18 {ECO:0000313|EMBL:EKU45666.1,
RC   ECO:0000313|Proteomes:UP000009879};
RA   Sharma R., Singh A., Jangir P.K.;
RT   "Genome Sequence of Brevibacterium casei S18.";
RL   Submitted (SEP-2012) 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:EKU45666.1}.
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DR   EMBL; AMSP01000014; EKU45666.1; -; Genomic_DNA.
DR   RefSeq; WP_009380325.1; NZ_AMSP01000014.1.
DR   AlphaFoldDB; K9AHS4; -.
DR   GeneID; 61004494; -.
DR   PATRIC; fig|1229781.4.peg.2809; -.
DR   eggNOG; COG0753; Bacteria.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000009879; 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:UP000009879}.
FT   DOMAIN          19..401
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        66
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         348
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   493 AA;  56018 MW;  6A4F7BC9840F4EB7 CRC64;
     MPTPEEQVDQ WFDPKKPSTT EVGTKRESDA HSLSVGPDGP LLLHDVALVE KIARFDRERV
     PERSPHAKGS GAFGEFVVTG DVSKYTKAKF LQPGTTTPML ARFSTVAGEL GSPDSWRDVR
     GFALKFYTED GNFDMVGNNT PVFFVRDPMK FPDFIHSQKR LPDSGLRSPN MQWDFWSLSP
     ESAHQVAYLM GPRGLPKTWR NMNGYSSHTY MWVNEDGEKF WVKYHFLTDQ GVENMSNEEA
     AKLAGEDADV HRRDLFDAIK DGNFPSWTLH VQIMPYEDAK TYRFNPFDLT KIWSKNDYPR
     IEVGRFTLNQ NPINHYAQIE QAAFSPSNTV PGTGVSPDKM LLSRVFSYPD AQRNRVGTNF
     NQLPVNAPVV KTNNYDKEGH MQYHHTGAAP VYAPNSYGRA YQDTQGVVDN GWEADGELVR
     MAYTLHRDDD DFGQAHTLVR EVYSEEERQE LVNTVVDMLK SDLEEPVLSN VFAYWKNIDA
     EVGQAIEDGY RQG
//
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