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Database: UniProt/TrEMBL
Entry: Q0RKZ4_FRAAA
LinkDB: Q0RKZ4_FRAAA
Original site: Q0RKZ4_FRAAA 
ID   Q0RKZ4_FRAAA            Unreviewed;       513 AA.
AC   Q0RKZ4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   13-SEP-2023, entry version 99.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:CAJ61811.1};
DE            EC=1.11.1.6 {ECO:0000313|EMBL:CAJ61811.1};
GN   Name=katA {ECO:0000313|EMBL:CAJ61811.1};
GN   OrderedLocusNames=FRAAL3167 {ECO:0000313|EMBL:CAJ61811.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ61811.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ61811.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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}.
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DR   EMBL; CT573213; CAJ61811.1; -; Genomic_DNA.
DR   RefSeq; WP_011604316.1; NC_008278.1.
DR   AlphaFoldDB; Q0RKZ4; -.
DR   STRING; 326424.FRAAL3167; -.
DR   KEGG; fal:FRAAL3167; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   OMA; NPSWTCY; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000000657; 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; 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; 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   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:0000313|EMBL:CAJ61811.1};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:CAJ61811.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000657}.
FT   DOMAIN          16..397
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         345
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   513 AA;  58088 MW;  0E29BAA9E7FF30DD CRC64;
     MTTYETRPTT ETRPTTTDAG VPVASDEHSL TVGPDGPLLL QDHYLLEQMA NFNRERIPER
     QPHAKGGGAF GAFEVTNDVS AFTRAAVFQP GARTDVLIRF STVAGERGSP DTWRDPRGFA
     VKFYTSAGNL DIVGNNTPVF FIRDPLKFQH FIRSQKRRAD NNLRDHDMQW DFWTLSPESA
     HQVTWLMGDR GIPRTWRHMN GYSSHTYMWI NAAGEQFWVK YHFKTDQGIE FFTQDEADQM
     AAIDTDYHQR DLYEHIRDGE FPSWTLKMQI MPFEDAKTYR FNPFDLTKVW PHADYPLHEV
     GRLTLNRNVS DYHTEMEQAA FEPNNLVAGT GLSPDKMLLA RGFSYADAHR ARLGVNYKQI
     PVNSPKVPVH SYSKDGAMRV QNVSDPVYAP NSYGGPAARP ELTDDGGRWH ADGEMVRTAY
     TLRPDDDDWG QAGTMVREVL DDAARARLVD NIVGHLLNGV SEPVLERAFE YWRNVDKDLG
     GRIEAGVRAK QHLTDPKAAQ QANPARSDAQ AKA
//
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