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Database: UniProt
Entry: A0A419VWQ0_9BACT
LinkDB: A0A419VWQ0_9BACT
Original site: A0A419VWQ0_9BACT 
ID   A0A419VWQ0_9BACT        Unreviewed;       481 AA.
AC   A0A419VWQ0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   22-FEB-2023, entry version 11.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:RKD86538.1};
GN   ORFNames=BC643_4236 {ECO:0000313|EMBL:RKD86538.1};
OS   Mangrovibacterium diazotrophicum.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Mangrovibacterium.
OX   NCBI_TaxID=1261403 {ECO:0000313|EMBL:RKD86538.1, ECO:0000313|Proteomes:UP000283387};
RN   [1] {ECO:0000313|EMBL:RKD86538.1, ECO:0000313|Proteomes:UP000283387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27148 {ECO:0000313|EMBL:RKD86538.1,
RC   ECO:0000313|Proteomes:UP000283387};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (SEP-2018) 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   -!- 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:RKD86538.1}.
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DR   EMBL; RAPN01000004; RKD86538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A419VWQ0; -.
DR   OrthoDB; 9760293at2; -.
DR   Proteomes; UP000283387; 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:SF61; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283387}.
FT   DOMAIN          7..393
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         337
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   481 AA;  54785 MW;  65C0AAB1555F838B CRC64;
     MSNKRLTTTA GAPVSSNQNS LTAGQRGPVL MQDYQLIEKL AHQNRERIPE RVVHAKGWGA
     FGTFTVTNDI SQYSCAKVFS EVGKKTEMLA RFSTVAGEQG AADAERDVRG FALKFYTEEG
     NWDLVGNNTP VFFIRDPYKF PDFIHTQKRH PKTNMRSATA MWDFWSQVPE SLHQVTILMS
     DRGIPTAPMY MNGYGSHTYS FWNKDGERFW VKFHFKTQQG HRHFTNEEAE QVIGQNRESY
     QEALFGTIER GEFPKWNVFV QVMPEADAEK TPYNPFDLTK VWPHADYPLV EVGVMELNKN
     PENYFQMIEN AAFSPSNVVP GIGFSPDKML QGRIFSYADA HRYRLGTHYE MLPPNQPKCP
     FHHYHKDGAM RFFDNGNSNP DAYYEPNSFG GPVEDPSVAE PAMKISGDAD RYGYDTSYDD
     FKQPGDLFRM FDDEQRERLF KNIAGAMQGV PSEIIEKQLK HFDAADPAYG AGVRKALGIS
     K
//
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