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UniProtKB/Swiss-Prot entry Q9YFS9

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

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Entry information
Entry name G3P_AERPE
Primary accession number Q9YFS9
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 27, 2002 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 63)
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: APE_0171.1
From
Aeropyrum pernix [TaxID: 56636] [HAMAP proteome]
Taxonomy Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Desulfurococcaceae; Aeropyrum.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K1;
DOI=10.1093/dnares/6.2.83; PubMed=10382966 [NCBI, ExPASy, EBI, Israel, Japan]
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.";
DNA Res. 6:83-101(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
BA000002; BAA79082.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H72772; H72772.
RefSeq NP_147019.2; -.
3D structure databases
HSSP P39460; 1B7G. [HSSP ENTRY / PDB]
ModBase Q9YFS9.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0043891; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity (inferred from electronic annotation from EC).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from HAMAP).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
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.
ProtoNet Q9YFS9.
Genome annotation databases
GeneID 1445701; -.
GenomeReviews BA000002_GR; APE_0171.1.
KEGG ape:APE_0171.1; -.
NMPDR fig|272557.1.peg.126; -.
Phylogenomic databases
HOGENOM Q9YFS9; -.
Genome annotation databases
CMR Q9YFS9; APE_0171.1.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
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   343  343     Glyceraldehyde-3-phosphate dehydrogenase. PRO_0000145715
NP_BIND   13    14  2     NAD (By similarity). 
REGION   141   143  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   196   197  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   142   142        Nucleophile (By similarity). 
BINDING   112   112        NAD; via amide nitrogen (By similarity). 
BINDING   170   170        NAD (By similarity). 
BINDING   303   303        NAD; via carbonyl oxygen (By similarity). 
Sequence information
Length: 343 AA [This is the length of the unprocessed precursor] Molecular weight: 37173 Da [This is the MW of the unprocessed precursor] CRC64: DA75B0577A5A64CB [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSVVKVGVNG FGTIGRRVAL AITLQKDMKL VGVVKRTPDY AALYAASRGI PIYTPTAKEA 

        70         80         90        100        110        120 
EEFEKRGIKV GGTLRELLAR VDVVVDATPE GQGAKNKPLY REAGVKQVYQ GGEKPEVAEA 

       130        140        150        160        170        180 
SFSTLCNYEE SKGRGSLRVV SCNTTGLLRL ICTLNREFGV ESVRAVLVRR GADPKEVKKG 

       190        200        210        220        230        240 
PIDSIVLNPP TLPSHHAVDV RTVLPWLDIK TAAVAVPTTF MHMHHVTLKL AKPVEKREVL 

       250        260        270        280        290        300 
ETLASAPRIM LVSSGDTGIK STSQLVDAAR LSRMGYDIPE LVVFEESVAV DGREVMLFQA 

       310        320        330        340 
VHQESIVVPE NIDAIRAVAS SPLTLDETLK ATDGSLGLRK TLW
Q9YFS9 in FASTA format

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