ID A0A0F0LDC7_9MICO Unreviewed; 487 AA.
AC A0A0F0LDC7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN Name=katA {ECO:0000313|EMBL:KJL30275.1};
GN ORFNames=RS83_01025 {ECO:0000313|EMBL:KJL30275.1};
OS Microbacterium oxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL30275.1, ECO:0000313|Proteomes:UP000033640};
RN [1] {ECO:0000313|EMBL:KJL30275.1, ECO:0000313|Proteomes:UP000033640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEL4b {ECO:0000313|EMBL:KJL30275.1,
RC ECO:0000313|Proteomes:UP000033640};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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|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:KJL30275.1}.
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DR EMBL; JYIW01000020; KJL30275.1; -; Genomic_DNA.
DR RefSeq; WP_045278438.1; NZ_JYIW01000020.1.
DR AlphaFoldDB; A0A0F0LDC7; -.
DR PATRIC; fig|82380.11.peg.1056; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000033640; 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 Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
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 7..391
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 COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 54
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 336
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 487 AA; 54659 MW; 88B6B35F497D1DD3 CRC64;
MTKPATTTQT GTPAPSDAHS LTVGADGPTV LHDRYLVEKL ASFNRERVPE RNPHAKGGGA
FGEFVVTEDV SAYTRAAVFQ PGATSETLIR FSSVAGEQGS PDTWRDVRGF SLRFYTSEGN
LDIVGNNTPT FFLRDAMKFP DFIHSQKRLG DSGLRDADMQ WDFWTLSPET AHQVTYLMGD
RGLPRSWRHM NGYGSHTYQW VNAAGERFWV QYHFLSQQGV EAMSAAEAEQ LAGSDADHYR
RDLFDAIARG DHPAWDVYVQ IMPYEEAKDY RFNPFDLTKT WSKKDYPRIK VGTFTLNRNP
QNFFAEIEQA AFSPGNQVPG TGISPDKMLM ARVFSYSDAQ RYRIGANYNQ LPVNQPHGAE
VRNYMHEGQM RYQSNPAEHR TYTPNSYGAA GGPEADPQAG IEASWESDGE LMRSAATLHL
DDDDFGQAGT LYRTVFDDEQ RARFLETLTG QGRGITVDVI RENFFQYWTN VDAALGEALR
RTVPAAV
//
