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Database: UniProt
Entry: A0A1R4FSF2_9MICO
LinkDB: A0A1R4FSF2_9MICO
Original site: A0A1R4FSF2_9MICO 
ID   A0A1R4FSF2_9MICO        Unreviewed;       503 AA.
AC   A0A1R4FSF2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:SJM58819.1};
DE            EC=1.11.1.6 {ECO:0000313|EMBL:SJM58819.1};
GN   ORFNames=FM112_06170 {ECO:0000313|EMBL:SJM58819.1};
OS   Gulosibacter sp. 10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Gulosibacter.
OX   NCBI_TaxID=1255570 {ECO:0000313|EMBL:SJM58819.1, ECO:0000313|Proteomes:UP000195931};
RN   [1] {ECO:0000313|EMBL:SJM58819.1, ECO:0000313|Proteomes:UP000195931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10(10) {ECO:0000313|Proteomes:UP000195931};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FUIC01000014; SJM58819.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4FSF2; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000195931; 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; 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; 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   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:0000313|EMBL:SJM58819.1};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:SJM58819.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195931}.
FT   DOMAIN          15..397
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        62
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         344
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;  57127 MW;  45E0F2F3848E8AD8 CRC64;
     MTQFETNIDP TLPSTRQNGA PAESDRNSLT VGSNGPIVLH DVQLVETLSA FNRERVPERN
     PHAKGAGAFG ELEITEDVSQ WTRAKVFQKG SKTRSLLRFS TVAGEQGSPD TWRDVRGFAL
     KFYTEEGNLD IVGNNTPVFF LRDPMKFPHF IRSQKRLPDS GLRNNTMQYD FWTNNPESAH
     QVTYLMGDRG LPRSWREMNG YSSHTYSWIN EAGEIFWVKY HWISEQGVHT ISNEEAERLA
     GEDADFHRRD LFDAIERGEH PSWTLKVQVM PYEDAKQYRY NPFDLTKVWP HSDYPLHTVG
     RLTLNENPEN FFAQIEQAAF APSNYVPGTG ISPDKMLMGR MYGYADAHRY RIGTNFAQLP
     VNRPIVKTNS YTFDGNMRFD HSGSAPVYAP NSYERPHSDE TGKVENNWTS DGDLVRSAYA
     LHPEDDDFGQ PGKLVREVWN DEQRAQFVET VAGSLATVEE PVLSRAFQYW KNVDAECGDR
     IQKTVLEGRA EAGEIPGGDP ANP
//
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