ID J0L8T3_9BACT Unreviewed; 426 AA.
AC J0L8T3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
DE Flags: Fragment;
GN ORFNames=O71_23937 {ECO:0000313|EMBL:EJF07935.1};
OS Pontibacter sp. BAB1700.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1144253 {ECO:0000313|EMBL:EJF07935.1, ECO:0000313|Proteomes:UP000003746};
RN [1] {ECO:0000313|EMBL:EJF07935.1, ECO:0000313|Proteomes:UP000003746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB1700 {ECO:0000313|EMBL:EJF07935.1,
RC ECO:0000313|Proteomes:UP000003746};
RX PubMed=23105068; DOI=10.1128/JB.01550-12;
RA Joshi M.N., Sharma A.C., Pandya R.V., Patel R.P., Saiyed Z.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Pontibacter sp. nov. BAB1700, a Halotolerant,
RT Industrially Important Bacterium.";
RL J. Bacteriol. 194:6329-6330(2012).
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|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
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:EJF07935.1}.
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DR EMBL; AKIS01000247; EJF07935.1; -; Genomic_DNA.
DR RefSeq; WP_007661229.1; NZ_AKIS01000247.1.
DR AlphaFoldDB; J0L8T3; -.
DR Proteomes; UP000003746; 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; IPR024712; Catalase_clade2.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 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|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498};
KW Hydrogen peroxide {ECO:0000256|RuleBase:RU000498};
KW Iron {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR038928-2,
KW ECO:0000256|RuleBase:RU000498};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000498};
KW Peroxidase {ECO:0000256|RuleBase:RU000498}.
FT DOMAIN 36..425
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 157
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 371
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"
FT NON_TER 426
FT /evidence="ECO:0000313|EMBL:EJF07935.1"
SQ SEQUENCE 426 AA; 48781 MW; 5C4BDBCF4A1AC49D CRC64;
MEEKDNKQPK PTQVNEDSKN KQLEQYREDG QGEYMTTDQG VRINHTDDSL KAGQRGPTLM
EDFHFREKMT HFDHESIPER VVHARGSGVH GYFQPYDDSL KKYTKARFLT EPGTRTPVFV
RFSTVVGSRG SADTVRDVRG FATKFYTAEG NYDLVGNNMP VFFIQDGNKF PDLVHAIKPM
PDNEMPQASA AHDTFWDFAS LMPESTHMLM WVLSDRAIPR SFRMMEGFGV HTFRFINDEG
KATFVKFHWR STLGANSLVW DEAQKLAGKD PDWLRRDLWD AIEMGDYPEF ELSVQLVPEE
DEFKYDFDLL DATKIIPEEL VPRRPVGKMV LNRNPDNFFS ETEQVAFHPG NLVPGIDVTN
DPLLQGRLFS YIDTQLNRFN STNFTEVPIN RPVAPVHNHH GAGFMRMTIG KGKANYWPNS
IGNGCP
//
