GenomeNet

Database: UniProt
Entry: A0A1A5NYQ6_9ACTN
LinkDB: A0A1A5NYQ6_9ACTN
Original site: A0A1A5NYQ6_9ACTN 
ID   A0A1A5NYQ6_9ACTN        Unreviewed;       487 AA.
AC   A0A1A5NYQ6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=A4U61_23690 {ECO:0000313|EMBL:OBQ48196.1};
OS   Streptomyces sp. H-KF8.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1727216 {ECO:0000313|EMBL:OBQ48196.1, ECO:0000313|Proteomes:UP000093719};
RN   [1] {ECO:0000313|Proteomes:UP000093719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H-KF8 {ECO:0000313|Proteomes:UP000093719};
RA   Undabarrena A., Ugalde J.A., Seeger M., Camara B.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000720,
CC         ECO:0000256|RuleBase:RU000498};
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, ECO:0000256|RuleBase:RU000498}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBQ48196.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LWAB01000011; OBQ48196.1; -; Genomic_DNA.
DR   RefSeq; WP_055605573.1; NZ_LWAB01000011.1.
DR   AlphaFoldDB; A0A1A5NYQ6; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000093719; Unassembled WGS sequence.
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; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF61; 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; PS00437; CATALASE_1; 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   ECO:0000256|RuleBase:RU000498};
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:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093719}.
FT   DOMAIN          10..394
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         340
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   487 AA;  55070 MW;  A1AFC0E851456AF4 CRC64;
     MTENNQKPLT TAAGAPVADN QNALTAGPRG PMLLQDVWFL EKLAHFDREV IPERRMHAKG
     SGAFGTFTVT NDITRYTSAN IFSEVGKKTD LFVRFSTVAG ERGAADAERD IRGFALKFYT
     DEGNWDLVGN NTPVFFFRDP LRFPDLNRAV KRDPRTNLRD AENNWDFWTN LPEALHQITI
     VMSDRGIPAS YRHMHGFGSH TYSLINAEGE RFWVKFHHRT QQGIKNLTDA EAEALVGKDR
     ESHQRDLYEA IENGDFPKWK MFVQVMPEAD AENYRFHPFD LTKVWSKKDY PLIEVGEWEL
     NRNPANYFAD VEQAAFTPAN VVPGISYSPD KMLQGRLFSY GDAQRYRLGV NHHQIPVNAA
     KNPVNTYHRD GAMRIDGNQG STPGIEPNSY GRWPDQPAYR EPSQAVGAVA DRFNFREDDD
     NYFEQPGNLF RLMTAEQQQV LFENTARAIN GASEQTVARH IANCTKADPA YGEGVRKAIE
     ALAAGSL
//
DBGET integrated database retrieval system