ID A0A0M0GGQ6_SPOGL Unreviewed; 485 AA.
AC A0A0M0GGQ6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=AF332_18655 {ECO:0000313|EMBL:KON88626.1};
OS Sporosarcina globispora (Bacillus globisporus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1459 {ECO:0000313|EMBL:KON88626.1, ECO:0000313|Proteomes:UP000037109};
RN [1] {ECO:0000313|Proteomes:UP000037109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4 {ECO:0000313|Proteomes:UP000037109};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-10036 dsm4.";
RL Submitted (JUL-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|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:KON88626.1}.
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DR EMBL; LGUF01000007; KON88626.1; -; Genomic_DNA.
DR RefSeq; WP_053436003.1; NZ_LGUF01000007.1.
DR AlphaFoldDB; A0A0M0GGQ6; -.
DR STRING; 1459.AF332_18655; -.
DR PATRIC; fig|1459.3.peg.4108; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000037109; 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 8..392
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 55
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 338
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 485 AA; 54779 MW; BAF0BD3E954014A0 CRC64;
MTKNNNLTTS WGAPVGDNQN SMTAGSRGPA LIQDVHLLEK LAHFNRERVP ERVVHAKGAG
AHGYFEVTND LTKYTKAAFL SEVGKRTPLF VRFSTVAGEL GSADTVRDPR GFAVKFYTEE
GNYDLVGNNT PVFFIRDAIK FPDFIHTQKR DPKTHLKNPT AVWDFWSLSP ESLHQVTILM
SDRGIPATLR HMHGFGSHTF KWVNEQGEGV WIKYHFKTEQ GIKNLSVEAS AKMAGENPDY
HTEDLFNAIE NGDFPSWKLC VQIMPLEDAN TYRFDPFDVT KVWSQKDYPL IEVGRMVLNK
NPENYFAEVE QATFSPGTLV PGIDVSPDKM LQGRLFAYHD AHRYRVGANH QMLPINRPRN
EVQNYQRDGQ MRFDNNGGGS VYYEPNSFGG PTESPEHKQA AYPVSGLAES VAYDHNDHYT
QAGDLYRLMS EEERSRLVAN IVAAMKPVEK EEIKHRQIQH FFKADPDYGT RIAKGLGLAV
PQGVK
//
