ID A0A0S7XPH4_9BACT Unreviewed; 440 AA.
AC A0A0S7XPH4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=Catalase {ECO:0000313|EMBL:KPJ64401.1};
DE Flags: Fragment;
GN ORFNames=AMK68_01735 {ECO:0000313|EMBL:KPJ64401.1};
OS candidate division KD3-62 bacterium DG_56.
OC Bacteria; candidate division KD3-62.
OX NCBI_TaxID=1704032 {ECO:0000313|EMBL:KPJ64401.1, ECO:0000313|Proteomes:UP000052020};
RN [1] {ECO:0000313|EMBL:KPJ64401.1, ECO:0000313|Proteomes:UP000052020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_56 {ECO:0000313|EMBL:KPJ64401.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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 -!- 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}.
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:KPJ64401.1}.
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DR EMBL; LIZY01000028; KPJ64401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XPH4; -.
DR PATRIC; fig|1704032.3.peg.85; -.
DR Proteomes; UP000052020; 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; 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; 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 Peroxidase {ECO:0000256|ARBA:ARBA00022559}.
FT DOMAIN 1..331
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 325..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 276
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 1
FT /evidence="ECO:0000313|EMBL:KPJ64401.1"
SQ SEQUENCE 440 AA; 50045 MW; 9F17847B16FEFC37 CRC64;
GYFEVTADVA NYTKAKFLSK VGKRAEVFVR FSTVGGEKGS PDAARDPRGF AVKFYTEDGN
YDMVGNNTPV FFIRDPLKFP DFIHTQKRHP ATNLPDPDMF WDFLSLTPES IHQVTILFSD
RGTPRSYRHM NGYSSHTFKW HNDKGQYFWV QYHFKTEQGI QNFTREEAEI MAGKDPNHAT
RDLYEAIERA EYPSWRLEMQ IMTPEQAANY RFDPYDITKV WPHGDVPPIE VGRLVLNRNP
ENYFADVEQA AFSPGNLVPG IAASPDKMLQ ARLFSYHDTH RYRLGPNYQL LPVNAPKAAR
TSNYQRDGHM RFDGNAGGSP NYYPNTFGGA APDPDAGEPP FQVSGTAARQ PYTHPNDDFV
QAGDLYRKVM TDQDRDHLVS NIVAHLGNAQ KRIQLRQAAI FYKADDDYGR RVAEGLGLEA
NQVRRLSAVS QQELVEATKE
//