ID   CAT3_NEUCR              Reviewed;         719 AA.
AC   Q9C169; Q7RV04;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Catalase-3;
DE            EC=1.11.1.6;
DE   Flags: Precursor;
GN   Name=cat-3; ORFNames=NCU00355;
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=5141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-58 AND
RP   638-656, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=74-ORS23-1A; TISSUE=Mycelium;
RX   MEDLINE=22150829; 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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=22598136; 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.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   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.,
RA   Paulsen I., 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).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group.
CC   -!- DEVELOPMENTAL STAGE: Activity is predominant during late
CC       exponential growth and at the start of the conidiation process.
CC   -!- INDUCTION: Induced under stress conditions, such as H(2)O(2),
CC       paraquat, cadmium, heat shock, uric acid and nitrate treatment.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; AY027544; AAK15807.1; -; Genomic_DNA.
DR   EMBL; AABX02000001; EAA28590.1; -; Genomic_DNA.
DR   RefSeq; XP_957826.1; -.
DR   PDB; 3EJ6; X-ray; 2.30 A; A/B/C/D=32-719.
DR   PDBsum; 3EJ6; -.
DR   PeroxiBase; 5416; NcKat03.
DR   GeneID; 3873876; -.
DR   KEGG; ncr:NCU00355; -.
DR   NMPDR; fig|5141.1.peg.374; -.
DR   BioCyc; NCRA-XX3-01:NCRA-XX3-01-004065-MON; -.
DR   BRENDA; 1.11.1.6; 266.
DR   GO; GO:0004096; F:catalase activity; IEA:EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR010582; Catalase-rel_immune_responsive.
DR   InterPro; IPR011614; Catalase_N.
DR   InterPro; IPR018028; Catalase_rel_subgroup.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 1.
DR   PROSITE; PS00437; CATALASE_1; FALSE_NEG.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing; Heme;
KW   Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Signal.
FT   SIGNAL        1     18       Potential.
FT   PROPEP       19     30
FT                                /FTId=PRO_0000004687.
FT   CHAIN        31    719       Catalase-3.
FT                                /FTId=PRO_0000004688.
FT   ACT_SITE    102    102       By similarity.
FT   ACT_SITE    175    175       By similarity.
FT   METAL       389    389       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   719 AA;  79228 MW;  72790DE3310B64D0 CRC64;
     MRVNALLPLS GLIGTALAAC PFADPSALGR RAEGGEVDAR QRLKEVEVDD NGQFMTTDFG
     GNIEEQFSLK AGGRGSTLLE DFIFRQKLQH FDHERIPERV VHARGAGAHG IFTSYGDWSN
     ITAASFLGAK DKQTPVFVRF STVAGSRGSA DTARDVHGFA TRFYTDEGNF DIVGNNIPVF
     FIQDAIRFPD LIHSVKPSPD NEVPQAATAH DSAWDFFSSQ PSALHTLFWA MSGNGIPRSY
     RHMDGFGIHT FRLVTEDGKS KLVKWHWKTK QGKAALVWEE AQVLAGKNAD FHRQDLWDAI
     ESGNAPSWEL AVQLIDEDKA QAYGFDLLDP TKFLPEEFAP LQVLGEMTLN RNPMNYFAET
     EQISFQPGHI VRGVDFTEDP LLQGRLYSYL DTQLNRHRGP NFEQLPINRP VSGVHNNHRD
     GQGQAWIHKN IHHYSPSYLN KGYPAQANQT VGRGFFTTPG RTASGVLNRE LSATFDDHYT
     QPRLFFNSLT PVEQQFVINA IRFEASHVTN EQVKKNVLEQ LNKISNDVAK RVAVALGLEA
     PQPDPTYYHN NVTRGVSIFN ESLPTIATLR VGVLSTTKGG SLDKAKALKE QLEKDGLKVT
     VIAEYLASGV DQTYSAADAT AFDAVVVAEG AERVFSGKGA MSPLFPAGRP SQILTDGYRW
     GKPVAAVGSA KKALQSIGVE EKEAGVYAGA QDEVIKGVEE GLKVFKFLER FAVDGDDEE
//