ID A0A0F7KEK1_9PROT Unreviewed; 688 AA.
AC A0A0F7KEK1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN ORFNames=AAW31_06685 {ECO:0000313|EMBL:AKH37573.1}, BCL69_106120
GN {ECO:0000313|EMBL:TYP80293.1};
OS Nitrosomonas communis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH37573.1, ECO:0000313|Proteomes:UP000034156};
RN [1] {ECO:0000313|Proteomes:UP000034156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156};
RA Kozlowski J.A., Kits K.D., Stein L.Y.;
RT "Draft genome of Nitrosomonas communis strain Nm2.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKH37573.1, ECO:0000313|Proteomes:UP000034156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm2 {ECO:0000313|EMBL:AKH37573.1,
RC ECO:0000313|Proteomes:UP000034156};
RX PubMed=26769932;
RA Kozlowski J.A., Kits K.D., Stein L.Y.;
RT "Genome Sequence of Nitrosomonas communis Strain Nm2, a Mesophilic Ammonia-
RT Oxidizing Bacterium Isolated from Mediterranean Soil.";
RL Genome Announc. 4:0-0(2016).
RN [3] {ECO:0000313|EMBL:TYP80293.1, ECO:0000313|Proteomes:UP000324176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm2 {ECO:0000313|EMBL:TYP80293.1,
RC ECO:0000313|Proteomes:UP000324176};
RA Wagner M.;
RT "Active sludge and wastewater microbial communities from Klosterneuburg,
RT Austria.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
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DR EMBL; CP011451; AKH37573.1; -; Genomic_DNA.
DR EMBL; VNHT01000061; TYP80293.1; -; Genomic_DNA.
DR RefSeq; WP_046849653.1; NZ_VNHT01000061.1.
DR AlphaFoldDB; A0A0F7KEK1; -.
DR KEGG; nco:AAW31_06685; -.
DR PATRIC; fig|44574.3.peg.1605; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000034156; Chromosome.
DR Proteomes; UP000324176; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000034156}.
FT DOMAIN 29..417
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 73
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 113
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 162
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 359
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 363
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:PIRSR038927-2"
FT BINDING 370
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 688 AA; 77264 MW; CC79E9A7D0F123AE CRC64;
MSDESDQKAA RGKGGEVHQQ AAGEIKVLTT QQGSPIADDQ NSLKAGARGP TLLEDHALRE
KLFHFDHERI PERVVHARGF GVHGYFETYD SLADITCADI FQRKGEITPA FVRFSTVVGS
KGSPDLARDV RGFAVKLYTE EGNWDIVGNN IPVFFIQDAI KFPDMVHSVK EEPDRGFPQA
QSAHDNFWDF ISLTPESMHM IMWVMSDRAI PRSFRFMEGF GVHSFRMVNK EGKAVFVKFH
WKPKLGLQSV LWDEAVKVNG ADPDFHRRDL WNAIIEGDFP EWELGLQIFD DEFAEQFEFD
VLDATKIIPE EQIPIRVVGR LVLNRVVDNF FAETEQVAFC TQNIVRGIDH SEDPLLQGRN
FSYLDTQLKR LGSPNFTHIP INAPKCPVHH FQQDGHMAIY NPKGRVNYEP NSWGDGGPRE
CPEKGFISYP QEVGGEKQRV RSESFADHYS QARQFYISQT PIEQQHIADA LAFELSKVKT
PRIRERIVSH LLNIDQELAS KVAEMLAIEG LPHPAEAALP TRYDLPPSDK LSILKNGPQS
FKGRKIGVLM SEDGNAAVLK YLEAALQEEG AIYEVIAPHA GELKGSDGAI IKIDEKIDGG
PSVLFDAIVI LPGAETVNML VSNYAAVRFV SDAFNHNKFI GYVDAAQPLL NKANIEDMLD
NGCHPLNDEA SVQAFIVKCR DLRYWKRG
//
