CATB_ASPOR
ID CATB_ASPOR Reviewed; 725 AA.
AC Q877A8; Q2U6W5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Catalase B;
DE EC=1.11.1.6 {ECO:0000269|PubMed:16233832};
DE Flags: Precursor;
GN Name=catB; ORFNames=AO090120000068;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RX PubMed=16233832; DOI=10.1263/jbb.99.562;
RA Hisada H., Hata Y., Kawato A., Abe Y., Akita O.;
RT "Cloning and expression analysis of two catalase genes from Aspergillus
RT oryzae.";
RL J. Biosci. Bioeng. 99:562-568(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide
CC through its degradation into water and oxygen.
CC {ECO:0000305|PubMed:16233832}.
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:0000269|PubMed:16233832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20310;
CC Evidence={ECO:0000305|PubMed:16233832};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: By hydrogen peroxide. {ECO:0000269|PubMed:16233832}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; AB078864; BAC55897.1; -; Genomic_DNA.
DR EMBL; AP007166; BAE62700.1; -; Genomic_DNA.
DR RefSeq; XP_001823833.1; XM_001823781.2.
DR AlphaFoldDB; Q877A8; -.
DR SMR; Q877A8; -.
DR STRING; 510516.Q877A8; -.
DR PRIDE; Q877A8; -.
DR EnsemblFungi; BAE62700; BAE62700; AO090120000068.
DR GeneID; 5996092; -.
DR KEGG; aor:AO090120000068; -.
DR VEuPathDB; FungiDB:AO090120000068; -.
DR HOGENOM; CLU_010645_3_0_1; -.
DR OMA; PRGDNEI; -.
DR Proteomes; UP000006564; Chromosome 5.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0004096; F:catalase activity; IMP:AspGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:AspGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; 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; 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; PS51402; CATALASE_3; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Glycoprotein; Heme; Hydrogen peroxide;
KW Iron; Metal-binding; Oxidoreductase; Peroxidase; Reference proteome;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..27
FT /evidence="ECO:0000250"
FT /id="PRO_0000043339"
FT CHAIN 28..725
FT /note="Catalase B"
FT /id="PRO_0000043340"
FT ACT_SITE 101
FT /evidence="ECO:0000250"
FT ACT_SITE 174
FT /evidence="ECO:0000250"
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 CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 725 AA; 79868 MW; 9A6A3761AAF1C29C CRC64;
MRALSLASLI GIASAACPYM TGELERRDTG TDDATAATEE FLSQYYMADN DTFLTSDVGG
PIEDQNSLQV GDRGPTLLED FIFRQKIQRF DHERVPERAV HARGVGAHGV FTSYGDYSNI
TAASFLGAEG KETPVFVRFS TVAGSRGSSD LARDVHGFAT RFYTDEGNFD IVGNNIPVFF
IQDAILFPDL IHAVKPRGDN EIPQAATAHD SAWDFFSQQP SSLHTLLWAM SGHGIPRSLR
HVDGFGIHTF RFVTDNGDSK LVKFHWKSLQ GKASMVWEEA QQVSGKNPDF MRQDLFEAIE
AGRYPEWELG VQIMDEEDQL KFGFDLFDPT KIVPEEYVPI TKLGKMTLNR NPRNYFAETE
QVMFQPGHIV RGVDFTEDPL LQGRLFSYLD TQLNRHGGPN FEQLPINQPR VPVHNNNRDG
AGQMFIPLNP NAYSPNTLNK GSPKQANQTV GKGFFTAPGR ESTGRFTRAV SPSFEDVWSQ
PRLFYNSLTP AEQQFVVDAI RFENSNVKSS VVRNNVIIQL NRVSNDLARR VARAIGVEEP
EADPTYYHNN KTTDVGTFGQ KLKKLDGLKV GFLASVETPA SIEAASELSK QLSEDGVDVV
VVAERLSDGV DQTYSGSDAI QFDAVIVAPG AEGLFSTFSF TAPSNATSSS TLFPAGRPLQ
IVIDGFRFGK PVGAVGSAAT ALKNAGIQTS RDGVYVDKSV TSGFVDGIKD GLRTFKFLDR
FKLDH
