ID A0A0J7ZLL4_STRVR Unreviewed; 709 AA.
AC A0A0J7ZLL4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-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 Name=katE {ECO:0000313|EMBL:KMS76814.1};
GN ORFNames=ACM01_02960 {ECO:0000313|EMBL:KMS76814.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS76814.1, ECO:0000313|Proteomes:UP000037432};
RN [1] {ECO:0000313|EMBL:KMS76814.1, ECO:0000313|Proteomes:UP000037432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS76814.1,
RC ECO:0000313|Proteomes:UP000037432};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUN-2015) 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}.
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:KMS76814.1}.
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DR EMBL; LFNT01000002; KMS76814.1; -; Genomic_DNA.
DR RefSeq; WP_048579413.1; NZ_LFNT01000002.1.
DR AlphaFoldDB; A0A0J7ZLL4; -.
DR PATRIC; fig|1938.3.peg.199; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000037432; 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}.
FT DOMAIN 23..410
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 70
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 67
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 107
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 156
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 353
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 357
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 364
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 709 AA; 78011 MW; D9C52FD8EF599A27 CRC64;
MGNRKEEQRE AFRADDPTAG PLTTDQGVEV DHTDDSLAAG ERGPTLMEDF HFREKLTHFD
HERIPERVVH ARGAGAYGYF EPYESCAEFT RAAFLQDPAV QTPVFVRFST VQGPKGSADT
VRDVRGFATK FYTSEGNYDL VGNNFPVFFI QDGIKFPDFV HAVKPEPHND IPTGSSAHDT
LWDFVSLQPE TLHAIMWLMS DRAIPRSYRM MQGFGVHTFR FVNADGKGTF VKFHWKPRLG
VRSLVWDEAQ ECQGRDPDFN RRDLWDAIEA GEYPEWELGV QLVAEEDEFA FDFDLLDATK
IIPEEQVPVR PIGRMVLNRN PENFFAETEQ VAFHTANVVP GIDFTNDPLL QARNFSYLDT
QLVRLGGPNF AQLPVNRPVA PVRTNQRDGY HQSALHSGTN YFPNSLGGGC PAHAGVDGSA
YTRPHARTDS RGGTPFAERV DGAKIRRRSP SFQDHYSQPA MFWNSMADWE KEHIVAAFRF
ELGKVGVREV RARTVEHLAK VNGDLASQVA RGIGVPEPSG TEAADKLSSP ALSLESQRGD
GSIRTRQIAV LVTDGVDTAQ VTSVREALTA EGAIVEALAP TDGAVAGAHG DRCEVDRALP
TVASVLYDAV LLPGGPHGTP PTAAVQDAMR FVRDAYRHGK PVGALGSGVG ILSSLEPEGI
RLSAEFHHTV VDQGVVTDTS PGPASEDFLE AFKAALSAHR HWGRPPVRR
//
