ID   CATB_EMENI              Reviewed;         722 AA.
AC   P78619; C8VR41; Q5AQU1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Catalase B;
DE            EC=1.11.1.6;
DE   Flags: Precursor;
GN   Name=catB; ORFNames=AN9339;
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 A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=9150225; DOI=10.1128/jb.179.10.3284-3292.1997;
RA   Kawasaki L., Wysong D., Diamond R., Aguirre J.;
RT   "Two divergent catalase genes are differentially regulated during
RT   Aspergillus nidulans development and oxidative stress.";
RL   J. Bacteriol. 179:3284-3292(1997).
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).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25043916; DOI=10.1186/1471-2164-15-613;
RA   Martins I., Hartmann D.O., Alves P.C., Martins C., Garcia H.,
RA   Leclercq C.C., Ferreira R., He J., Renaut J., Becker J.D.,
RA   Silva Pereira C.;
RT   "Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant
RT   polyester suberin as carbon source.";
RL   BMC Genomics 15:613-613(2014).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25043916}.
CC   -!- DEVELOPMENTAL STAGE: Barely detectable in asexual spores (conidia),
CC       disappears after germination, and starts to accumulate 10 hours after
CC       spore inoculation, throughout growth and conidiation.
CC   -!- INDUCTION: By hydrogen peroxide, heat shock, paraquat, or uric acid
CC       catabolism but not by osmotic stress.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; U80672; AAC49713.1; -; Genomic_DNA.
DR   EMBL; AACD01000172; EAA66406.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF87433.1; -; Genomic_DNA.
DR   RefSeq; XP_682608.1; XM_677516.1.
DR   AlphaFoldDB; P78619; -.
DR   SMR; P78619; -.
DR   STRING; 162425.CADANIAP00001123; -.
DR   PRIDE; P78619; -.
DR   EnsemblFungi; CBF87433; CBF87433; ANIA_09339.
DR   EnsemblFungi; EAA66406; EAA66406; AN9339.2.
DR   GeneID; 2867831; -.
DR   KEGG; ani:AN9339.2; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_3_0_1; -.
DR   InParanoid; P78619; -.
DR   OMA; PRGDNEI; -.
DR   OrthoDB; 507937at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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; 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; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..722
FT                   /note="Catalase B"
FT                   /id="PRO_0000004686"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         388
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        382
FT                   /note="Missing (in Ref. 1; AAC49713)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   722 AA;  79320 MW;  08C0EC4E95043D3F CRC64;
     MRALGLVGLV GVANAVCPYM TGELGRRDTN PDATEATEEF LSEYYLDDTD SYLTTDVGGP
     IEDQQSLKAG ARGSTLLEDF IFRQKIQRFD HERVPERAVH ARGAGAHGVF TSYGDFSNIT
     AASFLSAEGK ETPVFVRFST VAGSRGSSDL ARDVHGFATR FYTDEGNFDI VGNNIPVFFI
     QDAIQFPDLI HAVKPKGDRE IPQAATAHDA AWDFFSQQPS TLHTLLWAMA GHGIPRSFRH
     VDGFGVHTFR LVTEDGSTKL VKFHWKTLQG LASMVWEEAQ QISGKNPDYM RQDLFESIEA
     GRYPEWELNV QIMDEEDQLR FGFDLFDPTK IVPEEYVPLT PLGKMTLNRN PRNYFAETEQ
     VMFQPGHVVR GVDFTEDPLL QQGRLFSYLD TQLNRNGGPN FEQLPINQPR VAIHNNNRDG
     AGQMFIPLNP DAYSPNTLKG STLKQANQTA GRGFFTAPDR TANGNLVRAK SSTFDDAWSQ
     PRLFWNSLLP AEKQFVVNAI RFENANVKSD VVKNNVIVQL NRISNDLATR VAKAIGVDAP
     EPDNTYYHDN TTSNIGAFGH RLQSLAGLKI AVLASVDAEE SFSAATALKA ELSNDNLDVI
     VVAERFSNGV NQTYSASDAI QFDAVVVAPG AEKLFGAKSA ANSSSTLYPA GRPLEILVDA
     FRFGKPVAAL GSGSTAFDNA GINTAVEGVY VADAVDESFA NNLEEGLTVF KFLDRFALDS
     DE