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
//