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Catalase-1 (EC 1.11.1.6)

 CAT1_NEUCR              Reviewed;         736 AA.
Q9C168; Q7RUZ1;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 2.
28-FEB-2018, entry version 133.
RecName: Full=Catalase-1;
EC=1.11.1.6;
Name=cat-1; ORFNames=NCU08791;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-60; 152-167
AND 254-266, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND INDUCTION.
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
TISSUE=Conidium;
PubMed=12160934; DOI=10.1016/S0891-5849(02)00909-7;
Michan S., Lledias F., Baldwin J.D., Natvig D.O., Hansberg W.;
"Regulation and oxidation of two large monofunctional catalases.";
Free Radic. Biol. Med. 33:521-532(2002).
[2]
SEQUENCE REVISION TO N-TERMINUS.
Michan S., Ebbole D., Hansberg W.;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[4]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
SUBCELLULAR LOCATION, INDUCTION, AND GLYCOSYLATION.
PubMed=11728803; DOI=10.1016/S0891-5849(01)00637-2;
Diaz A., Rangel P., Montes de Oca Y., Lledias F., Hansberg W.;
"Molecular and kinetic study of catalase-1, a durable large catalase
of Neurospora crassa.";
Free Radic. Biol. Med. 31:1323-1333(2001).
[5]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 22-736 IN COMPLEX WITH
COFACTOR, ACTIVE SITE, AND CROSS-LINK.
PubMed=15342250; DOI=10.1016/j.jmb.2004.07.027;
Diaz A., Horjales E., Rudino-Pinera E., Arreola R., Hansberg W.;
"Unusual Cys-Tyr covalent bond in a large catalase.";
J. Mol. Biol. 342:971-985(2004).
-!- FUNCTION: Occurs in almost all aerobically respiring organisms and
serves to protect cells from the toxic effects of hydrogen
peroxide. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|PROSITE-ProRule:PRU10013,
ECO:0000269|PubMed:11728803, ECO:0000269|PubMed:12160934}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Active from pH 4 to 12. {ECO:0000269|PubMed:11728803};
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11728803,
ECO:0000269|PubMed:15342250}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:11728803}. Note=Principally associated with
the cell wall of conidia.
-!- DEVELOPMENTAL STAGE: Main catalase activity in conidia, during
germination of conidia, and initial growth.
{ECO:0000269|PubMed:12160934}.
-!- INDUCTION: During prestationary growth. By ethanol and in the
presence of air by heat shock. Inactivated by isopropanol and 20
mM 3-amino-1,2,4-triazole. {ECO:0000269|PubMed:11728803,
ECO:0000269|PubMed:12160934}.
-!- PTM: Glycosylated; with alpha-glucose and/or alpha-mannose.
{ECO:0000269|PubMed:11728803}.
-!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAA26998.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY027545; AAK15808.2; -; Genomic_DNA.
EMBL; CM002238; EAA26998.1; ALT_INIT; Genomic_DNA.
RefSeq; XP_956234.1; XM_951141.3.
PDB; 1SY7; X-ray; 1.75 A; A/B=22-736.
PDBsum; 1SY7; -.
ProteinModelPortal; Q9C168; -.
SMR; Q9C168; -.
IntAct; Q9C168; 1.
MINT; Q9C168; -.
PeroxiBase; 5207; NcKat01.
EnsemblFungi; EAA26998; EAA26998; NCU08791.
GeneID; 3872372; -.
KEGG; ncr:NCU08791; -.
EuPathDB; FungiDB:NCU08791; -.
HOGENOM; HOG000087851; -.
InParanoid; Q9C168; -.
KO; K03781; -.
OrthoDB; EOG092C0NOX; -.
BRENDA; 1.11.1.6; 3627.
SABIO-RK; Q9C168; -.
EvolutionaryTrace; Q9C168; -.
Proteomes; UP000001805; Chromosome 3, Linkage Group III.
GO; GO:0005619; C:ascospore wall; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0004096; F:catalase activity; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0048315; P:conidium formation; IDA:UniProtKB.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
GO; GO:0006979; P:response to oxidative stress; TAS:UniProtKB.
Gene3D; 2.40.180.10; -; 1.
Gene3D; 3.40.50.880; -; 1.
InterPro; IPR018028; Catalase.
InterPro; IPR024708; Catalase_AS.
InterPro; IPR024712; Catalase_clade2.
InterPro; IPR011614; Catalase_core.
InterPro; IPR037060; Catalase_core_sf.
InterPro; IPR002226; Catalase_haem_BS.
InterPro; IPR010582; Catalase_immune_responsive.
InterPro; IPR020835; Catalase_sf.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR002818; DJ-1/PfpI.
PANTHER; PTHR42821; PTHR42821; 1.
Pfam; PF00199; Catalase; 1.
Pfam; PF06628; Catalase-rel; 1.
Pfam; PF01965; DJ-1_PfpI; 1.
PIRSF; PIRSF038927; Catalase_clade2; 1.
PRINTS; PR00067; CATALASE.
SMART; SM01060; Catalase; 1.
SUPFAM; SSF52317; SSF52317; 1.
SUPFAM; SSF56634; SSF56634; 1.
PROSITE; PS00437; CATALASE_1; 1.
PROSITE; PS00438; CATALASE_2; 1.
PROSITE; PS51402; CATALASE_3; 1.
1: Evidence at protein level;
3D-structure; Cell wall; Complete proteome; Direct protein sequencing;
Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding;
Oxidoreductase; Peroxidase; Reference proteome; Secreted;
Thioether bond.
CHAIN 1 736 Catalase-1.
/FTId=PRO_0000084923.
ACT_SITE 92 92 {ECO:0000255|PROSITE-ProRule:PRU10013,
ECO:0000269|PubMed:15342250}.
ACT_SITE 165 165 {ECO:0000255|PROSITE-ProRule:PRU10013,
ECO:0000269|PubMed:15342250}.
METAL 379 379 Iron (heme axial ligand).
BINDING 89 89 Heme.
BINDING 129 129 Heme.
BINDING 178 178 Heme.
BINDING 375 375 Heme.
BINDING 386 386 Heme.
CROSSLNK 356 379 3-(S-cysteinyl)-tyrosine (Cys-Tyr).
STRAND 57 59 {ECO:0000244|PDB:1SY7}.
STRAND 64 67 {ECO:0000244|PDB:1SY7}.
HELIX 72 82 {ECO:0000244|PDB:1SY7}.
STRAND 90 92 {ECO:0000244|PDB:1SY7}.
STRAND 94 106 {ECO:0000244|PDB:1SY7}.
TURN 109 111 {ECO:0000244|PDB:1SY7}.
HELIX 115 117 {ECO:0000244|PDB:1SY7}.
STRAND 124 131 {ECO:0000244|PDB:1SY7}.
STRAND 133 135 {ECO:0000244|PDB:1SY7}.
STRAND 143 145 {ECO:0000244|PDB:1SY7}.
STRAND 148 155 {ECO:0000244|PDB:1SY7}.
STRAND 158 169 {ECO:0000244|PDB:1SY7}.
HELIX 175 177 {ECO:0000244|PDB:1SY7}.
HELIX 178 185 {ECO:0000244|PDB:1SY7}.
TURN 189 192 {ECO:0000244|PDB:1SY7}.
HELIX 201 209 {ECO:0000244|PDB:1SY7}.
HELIX 211 213 {ECO:0000244|PDB:1SY7}.
HELIX 214 220 {ECO:0000244|PDB:1SY7}.
HELIX 223 225 {ECO:0000244|PDB:1SY7}.
STRAND 226 228 {ECO:0000244|PDB:1SY7}.
HELIX 230 232 {ECO:0000244|PDB:1SY7}.
STRAND 241 244 {ECO:0000244|PDB:1SY7}.
STRAND 250 259 {ECO:0000244|PDB:1SY7}.
HELIX 268 277 {ECO:0000244|PDB:1SY7}.
HELIX 281 291 {ECO:0000244|PDB:1SY7}.
STRAND 297 306 {ECO:0000244|PDB:1SY7}.
HELIX 307 309 {ECO:0000244|PDB:1SY7}.
STRAND 313 315 {ECO:0000244|PDB:1SY7}.
TURN 326 328 {ECO:0000244|PDB:1SY7}.
STRAND 332 341 {ECO:0000244|PDB:1SY7}.
HELIX 346 349 {ECO:0000244|PDB:1SY7}.
TURN 350 352 {ECO:0000244|PDB:1SY7}.
HELIX 372 381 {ECO:0000244|PDB:1SY7}.
HELIX 383 386 {ECO:0000244|PDB:1SY7}.
HELIX 391 393 {ECO:0000244|PDB:1SY7}.
TURN 395 397 {ECO:0000244|PDB:1SY7}.
STRAND 423 425 {ECO:0000244|PDB:1SY7}.
TURN 436 439 {ECO:0000244|PDB:1SY7}.
HELIX 458 461 {ECO:0000244|PDB:1SY7}.
HELIX 465 473 {ECO:0000244|PDB:1SY7}.
HELIX 476 491 {ECO:0000244|PDB:1SY7}.
HELIX 496 506 {ECO:0000244|PDB:1SY7}.
TURN 507 509 {ECO:0000244|PDB:1SY7}.
HELIX 511 521 {ECO:0000244|PDB:1SY7}.
HELIX 543 545 {ECO:0000244|PDB:1SY7}.
STRAND 549 551 {ECO:0000244|PDB:1SY7}.
STRAND 557 561 {ECO:0000244|PDB:1SY7}.
HELIX 568 580 {ECO:0000244|PDB:1SY7}.
STRAND 584 590 {ECO:0000244|PDB:1SY7}.
STRAND 595 597 {ECO:0000244|PDB:1SY7}.
STRAND 606 608 {ECO:0000244|PDB:1SY7}.
TURN 609 611 {ECO:0000244|PDB:1SY7}.
HELIX 614 616 {ECO:0000244|PDB:1SY7}.
STRAND 617 622 {ECO:0000244|PDB:1SY7}.
HELIX 626 633 {ECO:0000244|PDB:1SY7}.
HELIX 636 647 {ECO:0000244|PDB:1SY7}.
STRAND 651 655 {ECO:0000244|PDB:1SY7}.
HELIX 658 666 {ECO:0000244|PDB:1SY7}.
STRAND 676 678 {ECO:0000244|PDB:1SY7}.
STRAND 680 682 {ECO:0000244|PDB:1SY7}.
STRAND 685 690 {ECO:0000244|PDB:1SY7}.
TURN 693 697 {ECO:0000244|PDB:1SY7}.
HELIX 709 718 {ECO:0000244|PDB:1SY7}.
HELIX 723 727 {ECO:0000244|PDB:1SY7}.
HELIX 731 733 {ECO:0000244|PDB:1SY7}.
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


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