ID CATB_ASPFU Reviewed; 728 AA.
AC Q92405; O14436; P79018; Q4WFG5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 24-JAN-2024, entry version 142.
DE RecName: Full=Catalase B;
DE EC=1.11.1.6;
DE AltName: Full=Antigenic catalase;
DE AltName: Full=Slow catalase;
DE Flags: Precursor;
GN Name=catB; Synonyms=cat1; ORFNames=AFUA_3G02270;
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90240 / AF-10;
RA Takasuka T., Anderson M., Denning D.W.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wysong D.R., Diamond R.D., Robbins P.W.;
RT "Cloning, sequencing and characterization of Aspergillus fumigatus catalase
RT genes.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-50,
RP GLYCOSYLATION, AND SUBUNIT.
RC STRAIN=CHUV 192-88;
RX PubMed=9353056; DOI=10.1128/iai.65.11.4718-4724.1997;
RA Calera J.A., Paris S., Monod M., Hamilton A.J., Debeaupuis J.-P.,
RA Diaquin M., Lopez-Medrano R., Leal F., Latge J.-P.;
RT "Cloning and disruption of the antigenic catalase gene of Aspergillus
RT fumigatus.";
RL Infect. Immun. 65:4718-4724(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9353056}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9353056}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; Y07763; CAA69069.1; -; Genomic_DNA.
DR EMBL; U87850; AAB48485.1; -; Genomic_DNA.
DR EMBL; U97574; AAB71223.1; -; Genomic_DNA.
DR EMBL; AAHF01000010; EAL86512.1; -; Genomic_DNA.
DR RefSeq; XP_748550.1; XM_743457.1.
DR AlphaFoldDB; Q92405; -.
DR SMR; Q92405; -.
DR STRING; 330879.Q92405; -.
DR Allergome; 8987; Asp f Catalase.
DR GlyCosmos; Q92405; 3 sites, No reported glycans.
DR EnsemblFungi; EAL86512; EAL86512; AFUA_3G02270.
DR GeneID; 3506033; -.
DR KEGG; afm:AFUA_3G02270; -.
DR VEuPathDB; FungiDB:Afu3g02270; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_3_0_1; -.
DR InParanoid; Q92405; -.
DR OMA; YGDWSNI; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0009986; C:cell surface; IDA:AspGD.
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; IDA: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: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 CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 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; CATALASE; 1.
DR PANTHER; PTHR42821:SF3; CATALASE B; 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; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..27
FT /evidence="ECO:0000269|PubMed:9353056"
FT /id="PRO_0000043337"
FT CHAIN 28..728
FT /note="Catalase B"
FT /id="PRO_0000043338"
FT ACT_SITE 102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 389
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 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 35
FT /note="A -> R (in Ref. 2; AAB48485)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="L -> F (in Ref. 3; AAB71223)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="L -> F (in Ref. 3; AAB71223)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="W -> R (in Ref. 2; AAB48485)"
FT /evidence="ECO:0000305"
FT CONFLICT 595..596
FT /note="DD -> EH (in Ref. 2; AAB48485)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="R -> A (in Ref. 2; AAB48485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 79910 MW; 65E21979A63D85E7 CRC64;
MRLTFIPSLI GVANAVCPYM TGELNRRDEI SDGDAAAATE EFLSQYYLND NDAFMTSDVG
GPIEDQNSLS AGERGPTLLE DFIFRQKIQR FDHERVPERA VHARGAGAHG VFTSYGDFSN
ITAASFLAKE GKQTPVFVRF STVAGSRGSS DLARDVHGFA TRFYTDEGNF DIVGNNIPVF
FIQDAILFPD LIHAVKPRGD NEIPQAATAH DSAWDFFSQQ PSTMHTLLWA MSGHGIPRSF
RHVDGFGVHT FRFVTDDGAS KLVKFHWKSL QGKASMVWEE AQQTSGKNPD FMRQDLHDAI
EAGRYPEWEL GVQIMDEEDQ LRFGFDLLDP TKIVPEEFVP ITKLGKMQLN RNPRNYFAET
EQVMFQPGHI VRGVDFTEDP LLQGRLFSYL DTQLNRHGGP NFEQLPINQP RVPVHNNNRD
GAGQMFIPLN PHAYSPKTSV NGSPKQANQT VGDGFFTAPG RTTSGKLVRA VSSSFEDVWS
QPRLFYNSLV PAEKQFVIDA IRFENANVKS PVVKNNVIIQ LNRIDNDLAR RVARAIGVAE
PEPDPTFYHN NKTADVGTFG TKLKKLDGLK VGVLGSVQHP GSVEGASTLR DRLKDDGVDV
VLVAERLADG VDQTYSTSDA IQFDAVVVAA GAESLFAASS FTGGSANSAS GASSLYPTGR
PLQILIDGFR FGKTVGALGS GTAALRNAGI ATSRDGVYVA QSVTDDFAND LKEGLRTFKF
LDRFPVDH
//
