ID   CATA_EMENI              Reviewed;         744 AA.
AC   P55305;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 47.
DE   RecName: Full=Catalase A;
DE            EC=1.11.1.6;
DE   AltName: Full=Spore-specific catalase;
GN   Name=catA;
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FGSC 26;
RX   MEDLINE=96171518; PubMed=8598056; DOI=10.1007/s002940050056;
RA   Navarro R.E., Stringer M.A., Hansberg W., Timberlake W.E., Aguirre J.;
RT   "catA, a new Aspergillus nidulans gene encoding a developmentally
RT   regulated catalase.";
RL   Curr. Genet. 29:352-359(1996).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group.
CC   -!- DEVELOPMENTAL STAGE: Sporulation-specific.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; U37803; AAC49254.1; -; Genomic_DNA.
DR   PIR; S68115; S68115.
DR   HSSP; P21179; 1CF9.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cel...; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR010582; Catalase-rel.
DR   InterPro; IPR011614; Catalase_N.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   2: Evidence at transcript level;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase; Sporulation.
FT   CHAIN         1    744       Catalase A.
FT                                /FTId=PRO_0000084921.
FT   ACT_SITE     93     93       By similarity.
FT   ACT_SITE    166    166       By similarity.
FT   METAL       380    380       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   744 AA;  84064 MW;  4B4D0B7C8EC8DFFA CRC64;
     MATSITAGLQ KAQQAVQDTA TKNKKIVDIS HDTVNVHTDQ EQRTDFGVAI TDPDHWLRVT
     NETHSGPSLL EDHIARERIH RFDHERIPER VVHARGTGAY GNFTLKESIE DLTYAGVLTD
     TSRNTPVFVR FSTVQGSRGS ADTVRDVRGF AVKFYTDEGN WDIVGNNIPV FFIQDAIKFP
     DFVHAVKPEP HNEVPQAQTA HNNFWDFVYL HPEATHMFMW AMSDRAIPRS YRMMQGFGVN
     TFSLVNKEGK RHFVKFHWIP HLGVHSLVWD EALKLAGQDP DFHRKDLMEA IDNKAYPKWD
     FAIQAIPEED QDKFEFDIFD ATKVWPEEQV PLRVVGELEL NRNIDEFFPE TEQVAFCTSH
     IVPGIDFSDD PLLQGRNFSY QDTQISRLGV NWEEIPINRP VCPFLNHNRD GAKRHRITKG
     TVNYWPNRFE ANPPASDKGF KSHPAPITGR KRRDLTPKFK EYHNQAQLFY NSLSEVEKVH
     VKKAFSFELD HCDDPIVYER LAGQRLAEID LPLAQAVAEM VGAPIPTKAL RDNHGKTSVR
     LSQFDFTPKA PGIISRRIAI IIGDGYDKIA FNGMKAAILA AASAPLRHWH QTSAIYAQGE
     DKNSSKGVIP DHMYDGMRST MFDATFIPGG SHIETLQKNG QIRYWIAETF GHLKALGAMG
     EAAQLVKEVL GNVMGVQIAG ADSAEPVEWY GVVTARGPES AESLSEGFKV LKDAGDFTSK
     FFYQISQHRN WQRELDGLAS TVAF
//