ID A0A0S7WGQ7_9CHLR Unreviewed; 503 AA.
AC A0A0S7WGQ7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, entry version 22.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=AMJ38_03515 {ECO:0000313|EMBL:KPJ49320.1};
OS Dehalococcoidia bacterium DG_22.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703393 {ECO:0000313|EMBL:KPJ49320.1, ECO:0000313|Proteomes:UP000054105};
RN [1] {ECO:0000313|EMBL:KPJ49320.1, ECO:0000313|Proteomes:UP000054105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_22 {ECO:0000313|EMBL:KPJ49320.1};
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 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:KPJ49320.1}.
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DR EMBL; LIZQ01000074; KPJ49320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7WGQ7; -.
DR PATRIC; fig|1703393.3.peg.640; -.
DR Proteomes; UP000054105; 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 9..394
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 339
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; 56910 MW; 62A35927936E4A63 CRC64;
MAEDKKVLTT SFGTPVDDDQ NTLTAGSPGP ALLQDIHLVE KLAHFDRERI PERVVHAKGA
GAYGYFEVTH DVTRYTRAKF LSQVGKRTEL FVRFSTVGGE KGSADAERDP RGFAVKFYTE
EGNYDFVGNN TPVFFIRDPL KFPDFIHTQK RIPATNLKDP DMFWDFLSLT PESIHQVTIL
FSDRGTPKTY RHMNGYSGHT FKWYNGKGEY FWVKIHFKTE QGIQNLTREE AERMKGVDPD
HATRDLHEAI ERGEYPAWKV YAQIMTPEQV EGYRFDSFDI TKVWPHGDAP LNPVGRMVLN
RNPENYFAEV EQAAFSPGNF VPGIAASPDK MLQGRLFSYH DTHRHRLGPN YHLLPVNSAK
AVPVNNYQRD GFMRFDSNGG GSPNYYPNSF GGPAPDPEAA EPAFEVSGKA ARQRYTHPND
DFVQPGVLYR KVMTDDDRAH LIGNIVAHLG GAQKRIQLRQ TAVFYKADPE YGRRVADGLG
LDVKEVERLA EMSPEERAKA TAK
//
