ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P31865


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name KPYK_TRIRE
Primary accession number P31865
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 55)
Name and origin of the protein
Protein name Pyruvate kinase
Synonyms PK
EC 2.7.1.40
Gene name
Name: pki1
From
Trichoderma reesei (Hypocrea jecorina) [TaxID: 51453] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(93)90430-B; PubMed=8359694 [NCBI, ExPASy, EBI, Israel, Japan]
Schindler M., Mach R.L., Vollenhofer S.K., Hodits R., Gruber F., Visser J., de Graaff L., Kubicek C.P.;
"Characterization of the pyruvate kinase-encoding gene (pki1) of Trichoderma reesei.";
Gene 130:271-275(1993).
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
L07060; AAA02922.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JN0780; JN0780.
3D structure databases
HSSP P00549; 1A3W. [HSSP ENTRY / PDB]
ModBase P31865.
Ontologies
GO
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from InterPro).
GO:0030955; Molecular function: potassium ion binding (inferred from electronic annotation from InterPro).
GO:0004743; Molecular function: pyruvate kinase activity (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001697; Pyr_Knase.
IPR015813; Pyrv/PenolPyrv_Kinase_cat.
IPR015794; Pyrv_Knase_a/b.
IPR015793; Pyrv_Knase_brl.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
G3DSA:3.40.1380.20; Pyrv_Knase_a/b; 1.
PANTHER PTHR11817; Pyruvate_kinase; 1.
Pfam PF00224; PK; 1.
PF02887; PK_C; 1.
Pfam graphical view of domain structure.
PRINTS PR01050; PYRUVTKNASE.
ProDom PD001009; Pyruvate_kinase; 2.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01064; pyruv_kin; 1.
PROSITE PS00110; PYRUVATE_KINASE; 1.
BLOCKS P31865.
ProtoNet P31865.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycolysis; Kinase; Magnesium; Metal-binding; Phosphoprotein; Pyruvate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   538  538     Pyruvate kinase. PRO_0000112119
ACT_SITE   263   263        By similarity. 
METAL   265   265        Magnesium (Potential). 
METAL   286   286        Magnesium (Potential). 
METAL   287   287        Magnesium (Potential). 
BINDING   360   360        ADP (Potential). 
MOD_RES   45    45        Phosphoserine (Potential). 
Sequence information
Length: 538 AA [This is the length of the unprocessed precursor] Molecular weight: 58888 Da [This is the MW of the unprocessed precursor] CRC64: E9C26AC0E8186FE7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSQISRTQSI MATTAQEHLE TGGRINWLAS LNTAFTPARN FRRTSIICTI GPKTNSVEAL 

        70         80         90        100        110        120 
NKLRDAGLNV ARMNFSHGSY EYHQSVIDNV RASVAAHPGR PVAIALDTKG PEIRTGNTAG 

       130        140        150        160        170        180 
DVDIPISAGT VMNFTTDEKY ATACDTQNMY VDYKNITKVI QPGRVIYVDD GVLAFDVLSI 

       190        200        210        220        230        240 
KDDQTVEVRA RNNGFISSRK GVNLPNTDVD LPALSEKDKA DLRFGVKNNV DMVFASFIRR 

       250        260        270        280        290        300 
AQDIKDIRDV LGPEGKQIQI IAKIENRQGL NNFAEILEET DGVMVARGDL GIEIPAAEVF 

       310        320        330        340        350        360 
AAQKKMIAMC NIAGKPVICA TQMLESMIKN PRPTRAEISD VGNAVTDGAD CVMLSGETAK 

       370        380        390        400        410        420 
GNYPAESIHE MHEASLKAEN TIPYVSHFEE MCTLVKRPVS TVESCAMAAV RASLDLGAGG 

       430        440        450        460        470        480 
IIVLSTSGDS ARLLSKYRPV CPIFMVTRNP TTSRFSHLYR GVYPFLYPEQ KPDFDTVNWQ 

       490        500        510        520        530 
EDVDKRIKWA VTRAIELKTL TAGDTVVVVQ GWKGGMGNTN TLRIVRADPD HLGIGQME 

P31865 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!