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Database: UniProt
Entry: A0A175RNT1_9MICO
LinkDB: A0A175RNT1_9MICO
Original site: A0A175RNT1_9MICO 
ID   A0A175RNT1_9MICO        Unreviewed;       509 AA.
AC   A0A175RNT1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=NS184_10360 {ECO:0000313|EMBL:KTR05346.1};
OS   Curtobacterium luteum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=33881 {ECO:0000313|EMBL:KTR05346.1, ECO:0000313|Proteomes:UP000078252};
RN   [1] {ECO:0000313|EMBL:KTR05346.1, ECO:0000313|Proteomes:UP000078252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS184 {ECO:0000313|EMBL:KTR05346.1,
RC   ECO:0000313|Proteomes:UP000078252};
RX   PubMed=26793183;
RA   Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA   Patil P.B.;
RT   "Genomic Resource of Rice Seed Associated Bacteria.";
RL   Front. Microbiol. 6:1551-1551(2016).
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|ARBA:ARBA00000720,
CC         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:KTR05346.1}.
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DR   EMBL; LDQC01000056; KTR05346.1; -; Genomic_DNA.
DR   RefSeq; WP_058726032.1; NZ_LDQC01000056.1.
DR   AlphaFoldDB; A0A175RNT1; -.
DR   STRING; 33881.NS184_10360; -.
DR   PATRIC; fig|33881.3.peg.2419; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000078252; 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   CDD; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
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}.
FT   DOMAIN          18..401
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         347
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   509 AA;  56751 MW;  8971B408D0A7D5F4 CRC64;
     MSDQNTTTGQ PAGTPTTTTN SGAPVSSDQH SMGVGADGPL ALHDHYLVEK LAQFNRERVP
     ERVVHAKGGG AFGTFTVTHD VSQYTRAAFL QPGKQTETLV RFSSVAGEQG SPDTWRDPRG
     FALKFYTEEG NYDLVGNNTP VFFIRDGIKF PDFIRSQKRL PGSHLRDHDM QWDFWTLSPE
     SAHQVTWLMG DRGLPASWRE MDGFGSHTYQ WINAEGERFW VKYHFITQQG HKTLTQEDAD
     RIAGEDADFH IRDLHAAIER EDFPKWTLKV QVMPYADAES YRFNPFDLTK VWPHADYPLI
     EVGELELNRN PENYFAQIEQ ATFAPSNFVP GIAASPDKML LARIFSYADA HRYRVGTNHA
     QLPVNAPKNE VHSYSKDGAM RFDFQKSEVP VYAPNSLGGA HADPAATDEV PGWESDGALQ
     RSAATLHPED DDFGQAGTLY REVLDDAARE RLVGNIAGHV SKVTRDDLRE RVFAYWTNVD
     ADLGARVRAA VAPSAPGSNE DPEKVAVEA
//
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