ID   F8E885_FLESM            Unreviewed;       484 AA.
AC   F8E885;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:AEI15082.1};
DE            EC=1.11.1.6 {ECO:0000313|EMBL:AEI15082.1};
GN   OrderedLocusNames=Flexsi_1432 {ECO:0000313|EMBL:AEI15082.1};
OS   Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Flexistipitaceae; Flexistipes.
OX   NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI15082.1, ECO:0000313|Proteomes:UP000006621};
RN   [1] {ECO:0000313|EMBL:AEI15082.1, ECO:0000313|Proteomes:UP000006621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RX   PubMed=22180813; DOI=10.4056/sigs.2235024;
RA   Lapidus A., Chertkov O., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA   Abt B., Spring S., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Genome sequence of the moderately thermophilic halophile Flexistipes
RT   sinusarabici strain (MAS10).";
RL   Stand. Genomic Sci. 5:86-96(2011).
RN   [2] {ECO:0000313|Proteomes:UP000006621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Flexistipes sinusarabici DSM 4947.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002858; AEI15082.1; -; Genomic_DNA.
DR   RefSeq; WP_013886564.1; NC_015672.1.
DR   AlphaFoldDB; F8E885; -.
DR   STRING; 717231.Flexsi_1432; -.
DR   KEGG; fsi:Flexsi_1432; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_0; -.
DR   OrthoDB; 9760293at2; -.
DR   Proteomes; UP000006621; 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; 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; 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:AEI15082.1};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:AEI15082.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006621}.
FT   DOMAIN          10..391
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         339
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   484 AA;  55333 MW;  9E97DB0B2BC47294 CRC64;
     MKKNSKKFTT TDAGIPVSSD EFSLTVGSDG PILMQDHYLM EQMANFNREM IPDRQPHAKG
     SGAFGQFEVT KDISAYTKAA MFQPGTKTEV LARFSTVAGE SGSPDTWRDV RGFALKFYTS
     EGNYDMVGNN TPVFFIRDPM KFQHFIHSQK RRADSGLRDN DMQWDFWTQS PESAHQVTIL
     MSDRGIPKSY RHMNGYTSHT YMWINDSGER FWVKYHFKTD QGIECLTQEE GDRITGEDAD
     YHRRDLFNAI KERDYPSWTL KVQIMPFEEA QNYRFNPFDL TKVWPHEDYP LHEVGRLTLN
     RNPSDFHTEI EQAAFEPSNL VPGIGASPDK MLQARLISYS DAHRARLGVN YKQIPVNRPK
     SSVHSYSKGG AMRIENVSDP VYAPNSKGGP KADAEKYPEE TIWNASGDFI RSAYTLRRDD
     DDWGQAGTLV RKVMSEEERD RLVSNVIGHL SDGVSEPVLE RALEYWRNID KEIGDRIAKG
     IENG
//