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Database: UniProt/TrEMBL
Entry: A5CNX6_CLAM3
LinkDB: A5CNX6_CLAM3
Original site: A5CNX6_CLAM3 
ID   A5CNX6_CLAM3            Unreviewed;       509 AA.
AC   A5CNX6;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   Name=katA {ECO:0000313|EMBL:CAN00770.1};
GN   OrderedLocusNames=CMM_0737 {ECO:0000313|EMBL:CAN00770.1};
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN00770.1, ECO:0000313|Proteomes:UP000001564};
RN   [1] {ECO:0000313|EMBL:CAN00770.1, ECO:0000313|Proteomes:UP000001564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN00770.1,
RC   ECO:0000313|Proteomes:UP000001564};
RX   PubMed=18192381; DOI=10.1128/JB.01595-07;
RA   Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M.,
RA   Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C.,
RA   Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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         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}.
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DR   EMBL; AM711867; CAN00770.1; -; Genomic_DNA.
DR   RefSeq; WP_012037422.1; NC_009480.1.
DR   AlphaFoldDB; A5CNX6; -.
DR   KEGG; cmi:CMM_0737; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   OMA; HVWPQKQ; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000001564; Chromosome.
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; 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          8..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   REGION          375..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        55
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   509 AA;  56680 MW;  847FB7CEC7214435 CRC64;
     MTDQKFTTTD SGAPVASDEH SLSVGPDGAI PLHDHYLVEK LAQFNRERIP ERVVHAKGGG
     AFGTFRVTGD VSAYTRASLF QPGAEVEMLA RFSTVAGEQG SPDTWRDPRG FALKFYTDEG
     NYDLVGNNTP VFFIRDGIKF PDFIRSQKRL PGSHLRDHDM QWDFWTLSPE SAHQVTWLMG
     DRGLPSSWRH MDGFGSHTYQ WINAAGERFW VKYHFKTQQG IEILKQEQAD QIAGEDADFH
     IRDLTEAIDR GDYPEWKLEV QIMPYEEAKS YRFNPFDLTK VWSQKDYPRI EVGTMTLNRN
     PENYFAQIEQ AAFAPSNFVP GIQTSPDKML LARIFSYADA HRYRVGTNHA QLPVNAPKSP
     VHSYSKDGQG RYTFQDAGTP VYAPNSHGGA HADPARAAES AGWEQDGELV RAAATLHAED
     DDFVQARMLV NESMDDAQRE RLVGNIVGHV SKVTTAELRA RVIQYWTNVD GWLGAAVAAG
     LPPLAGDAPV AEATPGPTRD AEEVGVAAH
//
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