CAT3_NEUCR
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 03-AUG-2022, entry version 140.
DE RecName: Full=Catalase-3;
DE EC=1.11.1.6;
DE Flags: Precursor;
GN Name=cat-3; ORFNames=NCU00355;
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 31-58 AND 638-656,
RP CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=74-ORS23-1A; TISSUE=Mycelium;
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 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).
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:12160934};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- DEVELOPMENTAL STAGE: Activity is predominant during late exponential
CC growth and at the start of the conidiation process.
CC {ECO:0000269|PubMed:12160934}.
CC -!- INDUCTION: Induced under stress conditions, such as H(2)O(2), paraquat,
CC cadmium, heat shock, uric acid and nitrate treatment.
CC {ECO:0000269|PubMed:12160934}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; AY027544; AAK15807.1; -; Genomic_DNA.
DR EMBL; CM002238; EAA28590.1; -; Genomic_DNA.
DR RefSeq; XP_957826.1; XM_952733.3.
DR PDB; 3EJ6; X-ray; 2.30 A; A/B/C/D=32-719.
DR PDB; 3ZJ4; X-ray; 3.10 A; A/B/C/D=1-719.
DR PDB; 3ZJ5; X-ray; 1.95 A; A/B/C/D=1-719.
DR PDB; 4AJ9; X-ray; 1.85 A; A/B/C/D=38-719.
DR PDB; 4BIM; X-ray; 2.95 A; A/B/C/D=1-719.
DR PDB; 6NSW; X-ray; 2.10 A; A/B/C/D=1-719.
DR PDB; 6NSY; X-ray; 2.20 A; A/B/C/D=1-719.
DR PDB; 6NSZ; X-ray; 2.20 A; A/B/C/D=1-719.
DR PDB; 6NT0; X-ray; 2.20 A; A/B/C/D=1-719.
DR PDB; 6NT1; X-ray; 2.20 A; A/B/C/D=1-719.
DR PDBsum; 3EJ6; -.
DR PDBsum; 3ZJ4; -.
DR PDBsum; 3ZJ5; -.
DR PDBsum; 4AJ9; -.
DR PDBsum; 4BIM; -.
DR PDBsum; 6NSW; -.
DR PDBsum; 6NSY; -.
DR PDBsum; 6NSZ; -.
DR PDBsum; 6NT0; -.
DR PDBsum; 6NT1; -.
DR AlphaFoldDB; Q9C169; -.
DR SMR; Q9C169; -.
DR IntAct; Q9C169; 1.
DR MINT; Q9C169; -.
DR STRING; 5141.EFNCRP00000000465; -.
DR PeroxiBase; 5416; NcKat03.
DR PRIDE; Q9C169; -.
DR EnsemblFungi; EAA28590; EAA28590; NCU00355.
DR GeneID; 3873876; -.
DR KEGG; ncr:NCU00355; -.
DR VEuPathDB; FungiDB:NCU00355; -.
DR HOGENOM; CLU_010645_3_0_1; -.
DR InParanoid; Q9C169; -.
DR EvolutionaryTrace; Q9C169; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; SSF56634; SSF56634; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..30
FT /evidence="ECO:0000269|PubMed:12160934"
FT /id="PRO_0000004687"
FT CHAIN 31..719
FT /note="Catalase-3"
FT /id="PRO_0000004688"
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 HELIX 41..46
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3ZJ4"
FT STRAND 104..116
FT /evidence="ECO:0007829|PDB:4AJ9"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3ZJ5"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 168..179
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:4AJ9"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6NSW"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 260..271
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 307..315
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4AJ9"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:4AJ9"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 380..397
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:4AJ9"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:3ZJ4"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:4AJ9"
FT TURN 438..442
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 462..469
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 480..487
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 491..505
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 511..524
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 526..536
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 558..561
FT /evidence="ECO:0007829|PDB:3EJ6"
FT STRAND 570..574
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:3EJ6"
FT HELIX 581..593
FT /evidence="ECO:0007829|PDB:4AJ9"
FT TURN 594..596
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 598..605
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:4BIM"
FT TURN 614..616
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 623..627
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 631..635
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 637..640
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 649..659
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 668..670
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 671..676
FT /evidence="ECO:0007829|PDB:4AJ9"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:3EJ6"
FT STRAND 686..690
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 691..704
FT /evidence="ECO:0007829|PDB:4AJ9"
FT HELIX 708..710
FT /evidence="ECO:0007829|PDB:4AJ9"
FT TURN 714..717
FT /evidence="ECO:0007829|PDB:6NSW"
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
