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UniProtKB/Swiss-Prot entry P39460


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

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Entry information
Entry name G3P_SULSO
Primary accession number P39460
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 80)
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
Synonyms: agaPD
OrderedLocusNames: SSO0528
ORFNames: C22_023
From
Sulfolobus solfataricus [TaxID: 2287] [HAMAP proteome]
Taxonomy Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Sulfolobus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=DSM 5833 / MT-4;
DOI=10.1007/BF00557333; PubMed=8259927 [NCBI, ExPASy, EBI, Israel, Japan]
Arcari P., Russo A.D., Ianniciello G., Gallo M., Bocchini V.;
"Nucleotide sequence and molecular evolution of the gene coding for glyceraldehyde-3-phosphate dehydrogenase in the thermoacidophilic archaebacterium Sulfolobus solfataricus.";
Biochem. Genet. 31:241-251(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8521845 [NCBI, ExPASy, EBI, Israel, Japan]
Jones C.E., Fleming T.M., Cowan D.A., Littlechild J.A., Piper P.W.;
"The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeon Sulfolobus solfataricus overlap by 8-bp. Isolation, sequencing of the genes and expression in Escherichia coli.";
Eur. J. Biochem. 233:800-808(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
DOI=10.1139/gen-43-1-116; PubMed=10701121 [NCBI, ExPASy, EBI, Israel, Japan]
Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C., Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T., Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E., Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J., Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
"Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
Genome 43:116-136(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
DOI=10.1073/pnas.141222098; PubMed=11427726 [NCBI, ExPASy, EBI, Israel, Japan]
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
"The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
[5]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
DOI=10.1006/jmbi.1999.3003; PubMed=10448043 [NCBI, ExPASy, EBI, Israel, Japan]
Isupov M.N., Fleming T.M., Dalby A.R., Crowhurst G.S., Bourne P.C., Littlechild J.A.;
"Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.";
J. Mol. Biol. 291:651-660(1999).
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
X66409; CAA47040.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X80178; CAA56460.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y18930; CAB57771.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE006683; AAK40848.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S51230; S51230.
S63529; S63529.
RefSeq NP_342058.1; -.
3D structure databases
PDB
1B7G; X-ray; 2.05 A; O/Q=1-340.[ExPASy / RCSB / EBI]
PDBsum 1B7G; -.
ModBase P39460.
Enzyme and pathway databases
BioCyc SSOL273057:SSO0528-MON; -.
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.
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 P39460.
Genome annotation databases
GeneID 1454815; -.
GenomeReviews AE006641_GR; SSO0528.
KEGG sso:SSO0528; -.
NMPDR fig|273057.1.peg.481; -.
Phylogenomic databases
HOGENOM P39460; -.
Genome annotation databases
CMR P39460; SSO0528.
Other
ProtoNet P39460.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; NAD; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   340  340     Glyceraldehyde-3-phosphate dehydrogenase. PRO_0000145735
NP_BIND   11    12  2     NAD (By similarity). 
REGION   138   140  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   193   194  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   139   139        Nucleophile (By similarity). 
BINDING   109   109        NAD; via amide nitrogen (By similarity). 
BINDING   167   167        NAD (By similarity). 
BINDING   300   300        NAD; via carbonyl oxygen (By similarity). 
DISULFID   123   149         
CONFLICT   48    48        I -> Y (in Ref. 1; CAA47040). 
CONFLICT   52    52        V -> AL (in Ref. 1; CAA47040). 
CONFLICT   72    73        ED -> DY (in Ref. 1; CAA47040). 
CONFLICT   159   159        K -> N (in Ref. 1; CAA47040). 
STRAND   2     7  6      
HELIX   11    21  11      
STRAND   26    32  7      
HELIX   38    45  8      
HELIX   54    56  3      
HELIX   57    61  5      
TURN   62    64  3      
HELIX   71    77  7      
STRAND   79    83  5      
HELIX   89    99  11      
STRAND   103   106  4      
HELIX   112   114  3      
HELIX   121   128  8      
STRAND   132   136  5      
HELIX   139   152  14      
STRAND   157   169  13      
STRAND   183   190  8      
HELIX   193   198  6      
STRAND   205   214  10      
STRAND   219   229  11      
HELIX   233   241  9      
STRAND   246   249  4      
STRAND   251   254  4      
HELIX   258   267  10      
HELIX   271   273  3      
STRAND   277   281  5      
HELIX   282   284  3      
STRAND   286   288  3      
STRAND   291   298  8      
TURN   300   303  4      
HELIX   304   315  12      
HELIX   321   331  11      
Sequence information
Length: 340 AA [This is the length of the unprocessed precursor] Molecular weight: 37596 Da [This is the MW of the unprocessed precursor] CRC64: 609C9260C3062B6D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MINVAVNGYG TIGKRVADAI IKQPDMKLVG VAKTSPNYEA FIAHRRGIRI YVPQQSIKKF 

        70         80         90        100        110        120 
EESGIPVAGT VEDLIKTSDI VVDTTPNGVG AQYKPIYLQL QRNAIFQGGE KAEVADISFS 

       130        140        150        160        170        180 
ALCNYNEALG KKYIRVVSCN TTALLRTICT VNKVSKVEKV RATIVRRAAD QKEVKKGPIN 

       190        200        210        220        230        240 
SLVPDPATVP SHHAKDVNSV IRNLDIATMA VIAPTTLMHM HFINITLKDK VEKKDILSVL 

       250        260        270        280        290        300 
ENTPRIVLIS SKYDAEATAE LVEVARDLKR DRNDIPEVMI FSDSIYVKDD EVMLMYAVHQ 

       310        320        330        340 
ESIVVPENID AIRASMKLMS AEDSMRITNE SLGILKGYLI 

P39460 in FASTA format

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