ID   A0A0N4WYL0_HAEPC        Unreviewed;      1043 AA.
AC   A0A0N4WYL0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=HPLM_LOCUS16958 {ECO:0000313|EMBL:VDO62633.1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001696601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0001696601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO62633.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO62633.1,
RC   ECO:0000313|Proteomes:UP000268014};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000256|RuleBase:RU004142}.
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|ARBA:ARBA00001971};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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; UZAF01019683; VDO62633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4WYL0; -.
DR   STRING; 6290.A0A0N4WYL0; -.
DR   WBParaSite; HPLM_0001696601-mRNA-1; HPLM_0001696601-mRNA-1; HPLM_0001696601.
DR   OMA; FNRERIN; -.
DR   Proteomes; UP000038042; Unplaced.
DR   Proteomes; UP000268014; 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; 2.
DR   Gene3D; 2.40.180.10; Catalase core domain; 2.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
DR   InterPro; IPR024708; Catalase_AS.
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; 2.
DR   Pfam; PF06628; Catalase-rel; 2.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 2.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 2.
DR   PROSITE; PS00437; CATALASE_1; 2.
DR   PROSITE; PS00438; CATALASE_2; 2.
DR   PROSITE; PS51402; CATALASE_3; 2.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000498};
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:UP000268014}.
FT   DOMAIN          47..430
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   DOMAIN          558..954
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
SQ   SEQUENCE   1043 AA;  119516 MW;  DA6AA6DE1C842AC1 CRC64;
     MPKPADPCDV QLENYKKSQP VSVRIFIPLN NLDPLPMLPF QTPKIITTSN GAPIGSKTNV
     LTAGPRGPLL MQDVVYMDEM AHFDRERIPE RVVHAKGGGA HGVFEVTHDI TKYCKAEIFS
     KIGKQTPCFV RFSTVAGELG SADTARDPRG FAVKFYTEEG NWDLVGNNTP IFFIRDPLQF
     PNFIHTQKRN PQTHLKDPDM QWDFWGLRPE STHQVMFLMS DRGTPDGFRF MNGYGSHTFK
     MVNARGEPVY CKFHFKPPKI KNLSAADAAR LAGEDPDYAI RDLFNAIERG DFPSWKLYIQ
     VMTFEQAEKW PMNPFDVTKV WPHGEFPLIP VGTMTLNRNP KNYFAEVEQA AFCPAHVVPG
     IEFSPDKMLQ GRLFSYTDTH FHRLGPNYIQ LPINCPFRAR AHNAQRDGFA AYNNQENAPN
     YFPNSFNGGV ECPKALESKW KVTGDVARHE SIDDNNFEQP RVFWEKVLNN EERERLVENI
     FSAMKDCKPF IQDRAIQNFG KVHPDFGNKL RKKIDDYNAT KVRIFEIGHL ISKMPKYDPS
     DLQLQNYKSG QPKPKVMTTS NGAPIANKTN VLTVGPRGPM LMQDVVFMDE MAHFDRERIP
     ERVVHAKGGG AHGMFEVTHD ITKYCKADIF SKIGKQTPCF ARFSTVGGES GSADTARDPR
     GFAVKFYTEE GNWDLVGNNT PIFFIRDPMQ FPNFIHTQKR NPQTHLKDPD MMWDFWGLRP
     ESTHQVMFLM SDRGTPDGFR FMNGYGSHTF KLVNAKGEPV YCKFHFKMAR EYGMNLIALQ
     AQKIKNLSAE DAARLSGEDP DYSIRDLYNA IERGDFPQWK LHIQVMTFEQ AERWRLNPFD
     VTKVWPHSEF PLIPVGTMTL NRNPKNYFAE VEQAAFSPAH VVPGIEFSPD KMLQGRLFSY
     TDTHFHRLGP NYNQLPINCP FRARAHNTQR DGAACYDNQG NAPNYFPNSF NGGVECPRSV
     ESRWNTTGDV ARHESIDENN FEQPRLFWEK VLNNDERERL LENIFSTMKD CKQFIQDRAI
     QNFVKVSNSY SALKIENHEL QKS
//