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UniProtKB/Swiss-Prot entry Q9C168


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CAT1_NEUCR
Primary accession number Q9C168
Secondary accession number Q7RUZ1
Integrated into Swiss-Prot on May 9, 2003
Sequence was last modified on January 4, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 67)
Name and origin of the protein
Protein name Catalase-1
Synonym EC 1.11.1.6
Gene name
Name: cat-1
ORFNames: NCU08791
From
Neurospora crassa [TaxID: 5141] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
Protein existence 1: Evidence at protein level;
References
[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;
DOI=10.1016/S0891-5849(02)00909-7; PubMed=12160934 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/S0891-5849(01)00637-2; PubMed=11728803 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/j.jmb.2004.07.027; PubMed=15342250 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY027545; AAK15808.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000017; EAA26998.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1SY7; X-ray; 1.75 A; A/B=22-736.[ExPASy / RCSB / EBI]
PDBsum 1SY7; -.
ModBase Q9C168.
Protein family/group databases
PeroxiBase 5207; NcKat01.
Enzyme and pathway databases
BioCyc NCRA-XX3-01:NCRA-XX3-01-003650-MON; -.
Ontologies
GO
GO:0005619; Cellular component: fungal-type spore wall (inferred from direct assay from UniProtKB).
GO:0004096; Molecular function: catalase activity (inferred from direct assay from UniProtKB).
GO:0020037; Molecular function: heme binding (inferred from direct assay from UniProtKB).
GO:0048315; Biological process: conidium formation (inferred from direct assay from UniProtKB).
GO:0006979; Biological process: response to oxidative stress (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002226; Catalase.
IPR010582; Catalase-rel.
IPR011614; Catalase_N.
Graphical view of domain structure.
Gene3D G3DSA:2.40.180.10; Catalase_N; 1.
PANTHER PTHR11465; Catalase; 1.
Pfam PF00199; Catalase; 1.
PF06628; Catalase-rel; 1.
Pfam graphical view of domain structure.
PRINTS PR00067; CATALASE.
ProDom PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00437; CATALASE_1; 1.
PS00438; CATALASE_2; 1.
BLOCKS Q9C168.
Genome annotation databases
NMPDR fig|5141.1.peg.8841; -.
Other
ProtoNet Q9C168.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell wall; Complete proteome; Direct protein sequencing; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Secreted; Thioether bond.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   736  736     Catalase-1. PRO_0000084923
ACT_SITE   92    92         
ACT_SITE   165   165         
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  3      
STRAND   64    68  5      
HELIX   72    82  11      
STRAND   90    92  3      
STRAND   94   106  13      
TURN   109   111  3      
HELIX   115   117  3      
STRAND   124   131  8      
STRAND   133   135  3      
STRAND   143   145  3      
STRAND   148   155  8      
STRAND   158   169  12      
HELIX   175   177  3      
HELIX   178   185  8      
TURN   189   192  4      
HELIX   201   209  9      
HELIX   211   213  3      
HELIX   214   220  7      
HELIX   223   225  3      
STRAND   226   228  3      
HELIX   230   232  3      
STRAND   241   244  4      
STRAND   250   259  10      
HELIX   268   277  10      
HELIX   281   291  11      
STRAND   297   306  10      
HELIX   307   309  3      
STRAND   313   315  3      
TURN   326   328  3      
STRAND   332   341  10      
HELIX   346   349  4      
TURN   350   352  3      
HELIX   372   381  10      
HELIX   383   386  4      
HELIX   391   393  3      
TURN   395   397  3      
STRAND   423   425  3      
TURN   436   439  4      
STRAND   447   454  8      
HELIX   458   461  4      
HELIX   465   473  9      
HELIX   476   491  16      
HELIX   496   506  11      
TURN   507   509  3      
HELIX   511   521  11      
HELIX   543   545  3      
STRAND   549   551  3      
STRAND   557   561  5      
HELIX   568   580  13      
STRAND   584   590  7      
STRAND   595   597  3      
STRAND   606   608  3      
TURN   609   611  3      
HELIX   614   616  3      
STRAND   617   622  6      
HELIX   626   633  8      
HELIX   636   647  12      
STRAND   651   655  5      
HELIX   658   666  9      
STRAND   676   678  3      
STRAND   680   682  3      
STRAND   685   690  6      
TURN   693   697  5      
HELIX   709   718  10      
HELIX   723   727  5      
HELIX   731   733  3      
Sequence information
Length: 736 AA [This is the length of the unprocessed precursor] Molecular weight: 82268 Da [This is the MW of the unprocessed precursor] CRC64: 76AC6E3A51336299 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSNIISQAGQ KAKEALTSAP SSKKVDDLKN EFKETDKSAR LTTDYGVKQT TADDWLRIVS 

        70         80         90        100        110        120 
DDKIGPSLLE DPFARERIMR FDHERIPERV VHARGSGAFG KFKVYESASD LTMAPVLTDT 

       130        140        150        160        170        180 
SRETPVFVRF STVLGSRGSA DTVRDVRGFA VKFYTEEGNW DLVGNNIPVF FIQDAIKFPD 

       190        200        210        220        230        240 
VIHAGKPEPH NEVPQAQSAH NNFWDFQFNH TEATHMFTWA MSDRAIPRSL RMMQGFGVNT 

       250        260        270        280        290        300 
YTLINAQGKR HFVKFHWTPE LGVHSLVWDE ALKLAGQDPD FHRKDLWEAI ENGAYPKWKF 

       310        320        330        340        350        360 
GIQAIAEEDE HKFDFDILDA TKIWPEDLVP VRYIGEMELN RNPDEFFPQT EQIAFCTSHV 

       370        380        390        400        410        420 
VNGIGFSDDP LLQGRNFSYF DTQISRLGVN FQELPINRPV CPVMNFNRDG AMRHTISRGT 

       430        440        450        460        470        480 
VNYYPNRFDA CPPASLKEGG YLEYAQKVAG IKARARSAKF KEHFSQAQLF YNSMSPIEKQ 

       490        500        510        520        530        540 
HMINAFGFEL DHCEDPVVYG RMVQRLADID LGLAQTIAEM VGGEAPTTTN HPNHGRKTIN 

       550        560        570        580        590        600 
LSQTEFPPAT PTIKSRRVAI IIADGYDNVA YDAAYAAISA NQAIPLVIGP RRSKVTAANG 

       610        620        630        640        650        660 
STVQPHHHLE GFRSTMVDAI FIPGGAKAAE TLSKNGRALH WIREAFGHLK AIGATGEAVD 

       670        680        690        700        710        720 
LVAKAIALPQ VTVSSEAEVH ESYGVVTLKK VKPESFTDAV KIAKGAAGFL GEFFYAIAQH 

       730 
RNWDRELDGL HSMIAY 

Q9C168 in FASTA format

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