CAT1_NEUCR
ID CAT1_NEUCR Reviewed; 736 AA.
AC Q9C168; Q7RUZ1;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Catalase-1;
DE EC=1.11.1.6;
GN Name=cat-1; ORFNames=NCU08791;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-60; 152-167 AND
RP 254-266, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RC TISSUE=Conidium;
RX PubMed=12160934; DOI=10.1016/s0891-5849(02)00909-7;
RA Michan S., Lledias F., Baldwin J.D., Natvig D.O., Hansberg W.;
RT "Regulation and oxidation of two large monofunctional catalases.";
RL Free Radic. Biol. Med. 33:521-532(2002).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Michan S., Ebbole D., Hansberg W.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR
RP LOCATION, INDUCTION, AND GLYCOSYLATION.
RX PubMed=11728803; DOI=10.1016/s0891-5849(01)00637-2;
RA Diaz A., Rangel P., Montes de Oca Y., Lledias F., Hansberg W.;
RT "Molecular and kinetic study of catalase-1, a durable large catalase of
RT Neurospora crassa.";
RL Free Radic. Biol. Med. 31:1323-1333(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 22-736 IN COMPLEX WITH COFACTOR,
RP ACTIVE SITE, AND CROSS-LINK.
RX PubMed=15342250; DOI=10.1016/j.jmb.2004.07.027;
RA Diaz A., Horjales E., Rudino-Pinera E., Arreola R., Hansberg W.;
RT "Unusual Cys-Tyr covalent bond in a large catalase.";
RL J. Mol. Biol. 342:971-985(2004).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000250}.
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 ECO:0000269|PubMed:11728803, ECO:0000269|PubMed:12160934};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:15342250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active from pH 4 to 12. {ECO:0000269|PubMed:11728803};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11728803,
CC ECO:0000269|PubMed:15342250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:11728803}. Note=Principally associated with the
CC cell wall of conidia.
CC -!- DEVELOPMENTAL STAGE: Main catalase activity in conidia, during
CC germination of conidia, and initial growth.
CC {ECO:0000269|PubMed:12160934}.
CC -!- INDUCTION: During prestationary growth. By ethanol and in the presence
CC of air by heat shock. Inactivated by isopropanol and 20 mM 3-amino-
CC 1,2,4-triazole. {ECO:0000269|PubMed:11728803,
CC ECO:0000269|PubMed:12160934}.
CC -!- PTM: Glycosylated; with alpha-glucose and/or alpha-mannose.
CC {ECO:0000269|PubMed:11728803}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA26998.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY027545; AAK15808.2; -; Genomic_DNA.
DR EMBL; CM002238; EAA26998.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_956234.1; XM_951141.3.
DR PDB; 1SY7; X-ray; 1.75 A; A/B=22-736.
DR PDBsum; 1SY7; -.
DR AlphaFoldDB; Q9C168; -.
DR SMR; Q9C168; -.
DR IntAct; Q9C168; 1.
DR MINT; Q9C168; -.
DR STRING; 5141.EFNCRP00000004624; -.
DR PeroxiBase; 5207; NcKat01.
DR PRIDE; Q9C168; -.
DR EnsemblFungi; EAA26998; EAA26998; NCU08791.
DR GeneID; 3872372; -.
DR KEGG; ncr:NCU08791; -.
DR HOGENOM; CLU_010645_3_0_1; -.
DR InParanoid; Q9C168; -.
DR BRENDA; 1.11.1.6; 3627.
DR SABIO-RK; Q9C168; -.
DR EvolutionaryTrace; Q9C168; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005619; C:ascospore wall; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004096; F:catalase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048315; P:conidium formation; IDA:UniProtKB.
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 InterPro; IPR002818; DJ-1/PfpI.
DR PANTHER; PTHR42821; PTHR42821; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF01965; DJ-1_PfpI; 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 1: Evidence at protein level;
KW 3D-structure; Cell wall; Direct protein sequencing; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Secreted; Thioether bond.
FT CHAIN 1..736
FT /note="Catalase-1"
FT /id="PRO_0000084923"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013,
FT ECO:0000269|PubMed:15342250"
FT ACT_SITE 165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013,
FT ECO:0000269|PubMed:15342250"
FT BINDING 89
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:15342250"
FT BINDING 129
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:15342250"
FT BINDING 178
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:15342250"
FT BINDING 375
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:15342250"
FT BINDING 379
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:0000269|PubMed:15342250"
FT BINDING 386
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:15342250"
FT CROSSLNK 356..379
FT /note="3-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000269|PubMed:15342250"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 94..106
FT /evidence="ECO:0007829|PDB:1SY7"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:1SY7"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 297..306
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1SY7"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:1SY7"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 372..381
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:1SY7"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:1SY7"
FT TURN 436..439
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 465..473
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 476..491
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 496..506
FT /evidence="ECO:0007829|PDB:1SY7"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 511..521
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 568..580
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 584..590
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:1SY7"
FT TURN 609..611
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 626..633
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 636..647
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 658..666
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 680..682
FT /evidence="ECO:0007829|PDB:1SY7"
FT STRAND 685..690
FT /evidence="ECO:0007829|PDB:1SY7"
FT TURN 693..697
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 709..718
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 723..727
FT /evidence="ECO:0007829|PDB:1SY7"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:1SY7"
SQ SEQUENCE 736 AA; 82268 MW; 76AC6E3A51336299 CRC64;
MSNIISQAGQ KAKEALTSAP SSKKVDDLKN EFKETDKSAR LTTDYGVKQT TADDWLRIVS
DDKIGPSLLE DPFARERIMR FDHERIPERV VHARGSGAFG KFKVYESASD LTMAPVLTDT
SRETPVFVRF STVLGSRGSA DTVRDVRGFA VKFYTEEGNW DLVGNNIPVF FIQDAIKFPD
VIHAGKPEPH NEVPQAQSAH NNFWDFQFNH TEATHMFTWA MSDRAIPRSL RMMQGFGVNT
YTLINAQGKR HFVKFHWTPE LGVHSLVWDE ALKLAGQDPD FHRKDLWEAI ENGAYPKWKF
GIQAIAEEDE HKFDFDILDA TKIWPEDLVP VRYIGEMELN RNPDEFFPQT EQIAFCTSHV
VNGIGFSDDP LLQGRNFSYF DTQISRLGVN FQELPINRPV CPVMNFNRDG AMRHTISRGT
VNYYPNRFDA CPPASLKEGG YLEYAQKVAG IKARARSAKF KEHFSQAQLF YNSMSPIEKQ
HMINAFGFEL DHCEDPVVYG RMVQRLADID LGLAQTIAEM VGGEAPTTTN HPNHGRKTIN
LSQTEFPPAT PTIKSRRVAI IIADGYDNVA YDAAYAAISA NQAIPLVIGP RRSKVTAANG
STVQPHHHLE GFRSTMVDAI FIPGGAKAAE TLSKNGRALH WIREAFGHLK AIGATGEAVD
LVAKAIALPQ VTVSSEAEVH ESYGVVTLKK VKPESFTDAV KIAKGAAGFL GEFFYAIAQH
RNWDRELDGL HSMIAY
