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Database: UniProt
Entry: A0A1A6H0V8_NEOLE
LinkDB: A0A1A6H0V8_NEOLE
Original site: A0A1A6H0V8_NEOLE 
ID   A0A1A6H0V8_NEOLE        Unreviewed;       420 AA.
AC   A0A1A6H0V8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132};
GN   ORFNames=A6R68_13538 {ECO:0000313|EMBL:OBS71884.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS71884.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS71884.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS71884.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS71884.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-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   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|ARBA:ARBA00001937};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329}.
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:OBS71884.1}.
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DR   EMBL; LZPO01055342; OBS71884.1; -; Genomic_DNA.
DR   STRING; 56216.A0A1A6H0V8; -.
DR   Proteomes; UP000092124; 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:0051781; P:positive regulation of cell division; 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; IPR002226; Catalase_haem_BS.
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; PS00437; CATALASE_1; 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}; Mitogen {ECO:0000256|ARBA:ARBA00023246};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092124}.
FT   DOMAIN          1..306
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   BINDING         251
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   420 AA;  48204 MW;  789F5FC319CBCF4F CRC64;
     MYQFSCAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAIL FPSFIHSQKR
     NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMXGYGSHTF KLVNANGEAV
     YCKFHYKVXV TDQGIKNLPV AEAARLTQDD PDYGIRDLFN AIATGNYPSW TFYIQVMTFK
     EAESFPFNPF DLTKIWPHKD YPLIPVGKLV LNRNPVNYFA EVEQMAFDPS NMPPGIEPSP
     DKMLQGRLFS YPDTHRHRLG PNYLQIPVNC PYRARVANYQ RDGPMCMHDN QGGAPNYYPN
     SFSAPEQQRS ALEHHFQCST DVQRFNSAIE DNVTQVRTFY TEVLNEEERR RLCENIAGHL
     KDAQLFIQKK AVKNFTDVHP EYGARIQALL DKYNAEKPKX AIHTYMQAGS HLAAKEKANL
//
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