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
//