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Database: UniProt
Entry: K9XD87_9CHRO
LinkDB: K9XD87_9CHRO
Original site: K9XD87_9CHRO 
ID   K9XD87_9CHRO            Unreviewed;       496 AA.
AC   K9XD87;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:AFZ30041.1};
DE            EC=1.11.1.6 {ECO:0000313|EMBL:AFZ30041.1};
GN   ORFNames=Glo7428_1479 {ECO:0000313|EMBL:AFZ30041.1};
OS   Gloeocapsa sp. PCC 7428.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ30041.1, ECO:0000313|Proteomes:UP000010476};
RN   [1] {ECO:0000313|EMBL:AFZ30041.1, ECO:0000313|Proteomes:UP000010476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ30041.1,
RC   ECO:0000313|Proteomes:UP000010476};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
RL   Submitted (JUN-2012) 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; CP003646; AFZ30041.1; -; Genomic_DNA.
DR   RefSeq; WP_015187916.1; NC_019745.1.
DR   AlphaFoldDB; K9XD87; -.
DR   STRING; 1173026.Glo7428_1479; -.
DR   KEGG; glp:Glo7428_1479; -.
DR   PATRIC; fig|1173026.3.peg.1570; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_3; -.
DR   OrthoDB; 9760293at2; -.
DR   Proteomes; UP000010476; 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:AFZ30041.1};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:AFZ30041.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010476}.
FT   DOMAIN          8..392
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         338
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   496 AA;  56084 MW;  09813BEA84D3314A CRC64;
     MSDRNTLTTA NGTPVADNQN SLTAGDRGPV LMQDFHLMEK LAHFNRERIP ERVVHAKGAA
     AFGTFTVTHD ITCYSKAKVF SEIGKQTPVL LRFSTVGGEK GSADAERDPR GFAVKFYTGE
     GNWDLTGNNT PVFFIRDPLK FPDFIHTQKR NPQTNCKDAN AMWDFWSLSP EALHQITILF
     SDRGTPKTYR HMDGFGSHTF SLINDRGDRV WCKFHFKTLQ GIENFTTQEA VRVKGEDPDH
     ATRDLFDAID HGDYPRWRVC IQVMTEEQAM RHRDNPFDLT KVWKHSEYPL IDVGILELNR
     NPHNYFAEVE QAAFSPSNVV PGISFSPDKM LQARIMSYPD AQRYRLGANY QQLSVNQPKC
     PVMHYQRDGA MALGNNGGNA PNYEPNSYDN TPKQNCAYAE PALDLGNVKV DRYDRRQGND
     DYTQAGDLYR LMTPDAQARL VENIVDSLSS ARQDIQMRQL CHFFRADVKY GMQVAQGLGI
     HIDPAMVPAA HQPVGV
//
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