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UniProtKB/Swiss-Prot entry O59494

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

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Entry information
Entry name G3P_PYRHO
Primary accession number O59494
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 62)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase
Synonyms GAPDH
EC 1.2.1.59
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Gene name
Name: gap
OrderedLocusNames: PH1830
From
Pyrococcus horikoshii [TaxID: 53953] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; Pyrococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OT3;
DOI=10.1093/dnares/5.2.55; PubMed=9679194 [NCBI, ExPASy, EBI, Israel, Japan]
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
DNA Res. 5:55-76(1998).
[2]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Pyrococcus horikoshii ot3.";
Submitted (JAN-2006) to the PDB data bank.
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
BA000001; BAA30950.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G71194; G71194.
RefSeq NP_143662.1; -.
3D structure databases
PDB
2CZC; X-ray; 2.00 A; A/B/C/D=1-334.[ExPASy / RCSB / EBI]
PDBsum 2CZC; -.
ModBase O59494.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from HAMAP).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00559; -; 1.
PBIL [Tree]
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006436; Glyceraldehyde-3-P_DHase_2_arc.
Graphical view of domain structure.
PANTHER PTHR10836; GAP_DH; 1.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
ProDom PD007761; GAPDH_like; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01546; GAPDH-II_archae; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS O59494.
Genome annotation databases
GeneID 1442672; -.
GenomeReviews BA000001_GR; PH1830.
KEGG pho:PH1830; -.
NMPDR fig|70601.1.peg.1786; -.
Phylogenomic databases
HOGENOM O59494; -.
Genome annotation databases
CMR O59494; PH1830.
Other
ProtoNet O59494.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   334  334     Glyceraldehyde-3-phosphate dehydrogenase. PRO_0000145731
NP_BIND   12    13  2     NAD. 
REGION   140   142  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   192   193  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   141   141        Nucleophile (By similarity). 
BINDING   111   111        NAD; via amide nitrogen. 
BINDING   167   167        NAD. 
BINDING   298   298        NAD; via carbonyl oxygen. 
STRAND   3     8  6      
HELIX   12    22  11      
STRAND   27    36  10      
HELIX   39    46  8      
STRAND   51    55  5      
HELIX   56    58  3      
HELIX   59    65  7      
HELIX   73    77  5      
STRAND   81    85  5      
HELIX   91   102  12      
STRAND   105   108  4      
HELIX   114   116  3      
STRAND   117   121  5      
HELIX   123   126  4      
HELIX   127   130  4      
STRAND   134   138  5      
HELIX   141   153  13      
HELIX   154   156  3      
STRAND   157   169  13      
STRAND   187   189  3      
HELIX   192   196  5      
TURN   197   199  3      
STRAND   204   212  9      
STRAND   217   227  11      
HELIX   231   239  9      
STRAND   244   247  4      
HELIX   249   251  3      
HELIX   256   265  10      
HELIX   269   271  3      
STRAND   275   279  5      
HELIX   280   282  3      
STRAND   284   286  3      
STRAND   289   296  8      
TURN   298   302  5      
HELIX   303   313  11      
HELIX   319   330  12      
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 37264 Da [This is the MW of the unprocessed precursor] CRC64: AEA615734718E39B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKVKVGVNGY GTIGKRVAYA VTKQDDMELI GITKTKPDFE AYRAKELGIP VYAASEEFIP 

        70         80         90        100        110        120 
RFEKEGFEVA GTLNDLLEKV DIIVDATPGG IGAKNKPLYE KAGVKAIFQG GEKADVAEVS 

       130        140        150        160        170        180 
FVAQANYEAA LGKNYVRVVS CNTTGLVRTL SAIREYADYV YAVMIRRAAD PNDTKRGPIN 

       190        200        210        220        230        240 
AIKPTVEVPS HHGPDVQTVI PINIETMAFV VPTTLMHVHS VMVELKKPLT KDDVIDIFEN 

       250        260        270        280        290        300 
TTRVLLFEKE KGFDSTAQII EFARDLHREW NNLYEIAVWK ESINIKGNRL FYIQAVHQES 

       310        320        330 
DVIPENIDAI RAMFELADKW DSIKKTNKSL GILK
O59494 in FASTA format

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