ID A0A075UYL1_9PSEU Unreviewed; 701 AA.
AC A0A075UYL1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
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:AIG77551.1};
GN ORFNames=AJAP_23500 {ECO:0000313|EMBL:AIG77551.1};
OS Amycolatopsis japonica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX NCBI_TaxID=208439 {ECO:0000313|EMBL:AIG77551.1, ECO:0000313|Proteomes:UP000028492};
RN [1] {ECO:0000313|EMBL:AIG77551.1, ECO:0000313|Proteomes:UP000028492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG417-CF17 (DSM 44213) {ECO:0000313|Proteomes:UP000028492};
RX PubMed=25193710; DOI=10.1016/j.jbiotec.2014.08.034;
RA Stegmann E., Albersmeier A., Spohn M., Gert H., Weber T., Wohlleben W.,
RA Kalinowski J., Ruckert C.;
RT "Complete genome sequence of the actinobacterium Amycolatopsis japonica
RT MG417-CF17(T) (=DSM 44213T) producing (S,S)-N,N'-ethylenediaminedisuccinic
RT acid.";
RL J. Biotechnol. 189:46-47(2014).
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; CP008953; AIG77551.1; -; Genomic_DNA.
DR RefSeq; WP_038515202.1; NZ_CP008953.1.
DR AlphaFoldDB; A0A075UYL1; -.
DR STRING; 208439.AJAP_23500; -.
DR KEGG; aja:AJAP_23500; -.
DR eggNOG; COG0693; Bacteria.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_3_0_11; -.
DR Proteomes; UP000028492; Chromosome.
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; cd08155; catalase_clade_2; 1.
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 26..414
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 70
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 110
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 159
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 356
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 360
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 367
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 701 AA; 77353 MW; 89011D3198E18BAC CRC64;
MAQHREDAKN EQLDGSRVDP EGSVLTTQQG VRVDHTDDSL TAGSRGPTLL EDFHAREKIT
HFDHERIPER VVHARGAGAY GFFEAYDDAL ADYTVAEFLT SGEKIPVFVR FSTVAGSRGS
ADTVRDVRGF ATKFYTRQGN YDLVGNNMPV FFIQDGIKFP DFVHAVKPEP HNEIPQAQSA
HDTFWDFVSL QPESLHMVLW LMSDRALPRS YRMMQGFGVH TFRLVNAEGK GTFVKFHWKP
ALGTHSLVWD ECQKIAGKDP DFNRRDLWDA IESGQYPEWE LGVQLVDEDS EHDFDFDLLD
ATKIIPEEQV PVRPVGRMVL DRNPDDFFAE TEQIAFHTAN IVPGIDFTND PLLQARNFSY
LDTQLIRLGG PNFSQLPVNR PIAPVHTNQR DGYGQQNVHK GRTSYFPNSR GGGCPAIADS
GVFRHYTEAV AGNKIRDRSE SFKDFYSQAT LFWNSMSPIE REHIVAAFRF ELGKVEDREV
RARTVAELNN VDHDLAAEVA EGIGVSVPAA PATPHHDRTS PALSQLNQPS VAPTSRKVAV
LAADGVDTIG VGRLVEALTA EGAIVEVLAP TEAELRPGGE GDPLRPDRQL NTMASVLYDA
VVVPCGPSAI NVLERDGYAV HFVAEAYKHG KPVAAFGSGL DLLRRAGVTS KLADDAETLI
DQGVVTTTAA EATLPDGFFA SFTAQLGEHR SWLRKTDAIP A
//
