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
//