ID   CATA_EMENI              Reviewed;         744 AA.
AC   P55305; C8VAD2; Q5ASU3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Catalase A;
DE            EC=1.11.1.6;
DE   AltName: Full=Spore-specific catalase;
GN   Name=catA; ORFNames=AN8637;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FGSC 26;
RX   PubMed=8598056; DOI=10.1007/bf02208616;
RA   Navarro R.E., Stringer M.A., Hansberg W., Timberlake W.E., Aguirre J.;
RT   "catA, a new Aspergillus nidulans gene encoding a developmentally regulated
RT   catalase.";
RL   Curr. Genet. 29:352-359(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen peroxide.
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:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- DEVELOPMENTAL STAGE: Sporulation-specific.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC49254.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U37803; AAC49254.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AACD01000158; EAA60671.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF78282.1; -; Genomic_DNA.
DR   PIR; S68115; S68115.
DR   RefSeq; XP_681906.1; XM_676814.1.
DR   AlphaFoldDB; P55305; -.
DR   SMR; P55305; -.
DR   STRING; 162425.CADANIAP00006410; -.
DR   PeroxiBase; 5213; AniKat01.
DR   EnsemblFungi; CBF78282; CBF78282; ANIA_08637.
DR   EnsemblFungi; EAA60671; EAA60671; AN8637.2.
DR   GeneID; 2868532; -.
DR   KEGG; ani:AN8637.2; -.
DR   VEuPathDB; FungiDB:AN8637; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_3_0_1; -.
DR   InParanoid; P55305; -.
DR   OMA; VMWQMSD; -.
DR   OrthoDB; 507937at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IMP:AspGD.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034605; P:cellular response to heat; IMP:AspGD.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:AspGD.
DR   GO; GO:0010106; P:cellular response to iron ion starvation; IEP:AspGD.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd03132; GATase1_catalase; 1.
DR   Gene3D; 1.20.1370.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR043156; Catalase_clade2_helical.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR041399; Catalase_large_C.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF18011; Catalase_C; 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   2: Evidence at transcript level;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Reference proteome; Sporulation.
FT   CHAIN           1..744
FT                   /note="Catalase A"
FT                   /id="PRO_0000084921"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         380
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:0000250"
FT   CONFLICT        582
FT                   /note="Q -> A (in Ref. 1; AAC49254)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   744 AA;  83990 MW;  3933E190CCBB0713 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 AQALPFVIGT KRSAIYAQGE
     DKNSSKGVIP DHMYDGMRST MFDATFIPGG SHIETLQKNG QIRYWIAETF GHLKALGAMG
     EAAQLVKEVL GNVMGVQIAG ADSAEPVEWY GVVTARGPES AESLSEGFKV LKDAGDFTSK
     FFYQISQHRN WQRELDGLAS TVAF