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Database: UniProt/TrEMBL
Entry: A0A1L6LX55_9DELT
LinkDB: A0A1L6LX55_9DELT
Original site: A0A1L6LX55_9DELT 
ID   A0A1L6LX55_9DELT        Unreviewed;       723 AA.
AC   A0A1L6LX55;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   20-JUN-2018, entry version 10.
DE   RecName: Full=Catalase {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
GN   ORFNames=A7982_11648 {ECO:0000313|EMBL:APR86299.1};
OS   Minicystis rosea.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Minicystis.
OX   NCBI_TaxID=888845 {ECO:0000313|EMBL:APR86299.1, ECO:0000313|Proteomes:UP000185464};
RN   [1] {ECO:0000313|EMBL:APR86299.1, ECO:0000313|Proteomes:UP000185464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24000 {ECO:0000313|EMBL:APR86299.1,
RC   ECO:0000313|Proteomes:UP000185464};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of
CC       hydrogen peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC         ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CP016211; APR86299.1; -; Genomic_DNA.
DR   KEGG; mrm:A7982_11648; -.
DR   KO; K03781; -.
DR   Proteomes; UP000185464; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 2.40.180.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR037060; Catalase_core_sf.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56634; SSF56634; 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   Complete proteome {ECO:0000313|Proteomes:UP000185464};
KW   Heme {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-3,
KW   ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|PIRSR:PIRSR038927-2, ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185464}.
FT   DOMAIN       34    422       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     81     81       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    154    154       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       368    368       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
FT   BINDING      78     78       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     118    118       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     167    167       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     364    364       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     375    375       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
SQ   SEQUENCE   723 AA;  79643 MW;  E18B1DDAB119DD1E CRC64;
     MSEKKAQPER DDEKSKDADL ERNRVDTEQK GYLTTEQGVR VEDTDNSLKV GDRGPTLLED
     FHLREKITHF DHERIPERVV HARGSGAHGY FQVYESLADL TRAKFLQDPS VKTPVFVRFS
     TVVGSRGSSD TPRDVRGFAT KFYTEEGNYD LVGNNIPVFF IQDGIKFPDI IHSVKPEPDR
     EIPQAASAHD TFWDFASLVP EITHMLMWVL SDRAIPRSYR MMEGFGVHTF RLVNAKGEAH
     FVKFHWKPLL GVHSLVWDEA QKIYGKDPDF NRRDLWDAIA SGNYPEYELG LQIIEEKDEH
     AFAFDLLDPT KIVPEELVPV RRVGKMVLNR NPDNFFAETE QVAFCTQNVV SGIDFTDDPL
     LQVRNFSYLD TQLLRLGGPN FTELPINRAV AQVQNNNRDG LMQHRIFKGR VAYTPNSLAG
     GCPMAAPEKL GGFVHYAEKV SGKTIRMRSP SFADHYTQAK LFWDSIAPWE KEHLIAAARF
     ELGKVETEAV RARMVEGFAK VDIDFARAVA EGIGVPPPAA PPPAVPAQAT PAPGKRSVAR
     SPAVSMANTV KNSIKTRKIA ILVADGVSGA ELQSVRAALL ADGAVPELVG PRVGSVKTAE
     GGLEKTPVSF QTTASVLYDA VYVPGGKASA DTLKALGLAL HFINEAYKHH KPIGASGEGV
     EVLKATSITG VKIADATAQG KPVSDKGVVT VESGKGIKPF ILDLVQAIAV VRHWDRDTSR
     IPA
//
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