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P10618

- G3P_METFE

UniProt

P10618 - G3P_METFE

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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

gap

Organism
Methanothermus fervidus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Exhibits a dual-cofactor specificity, with a marked preference for NADP+ over NAD+.

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101NADP; via amide nitrogen1 Publication
Active sitei140 – 1401NucleophileBy similarity
Binding sitei171 – 1711NADP1 Publication
Binding sitei300 – 3001NADP; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 122NADP1 Publication
Nucleotide bindingi34 – 352NADP1 Publication

GO - Molecular functioni

  1. glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity Source: UniProtKB-EC
  2. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB-HAMAP
  3. glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity Source: CACAO
  4. NAD binding Source: InterPro
  5. NADP binding Source: InterPro

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

SABIO-RKP10618.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.59)
Short name:
GAPDH
Alternative name(s):
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Gene namesi
Name:gap
OrganismiMethanothermus fervidus
Taxonomic identifieri2180 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145722Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
337
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi13 – 219Combined sources
Beta strandi23 – 3513Combined sources
Helixi38 – 458Combined sources
Beta strandi50 – 545Combined sources
Helixi55 – 573Combined sources
Helixi58 – 636Combined sources
Helixi72 – 776Combined sources
Beta strandi80 – 845Combined sources
Helixi90 – 10112Combined sources
Beta strandi105 – 1073Combined sources
Helixi113 – 1164Combined sources
Helixi122 – 1254Combined sources
Helixi126 – 1294Combined sources
Beta strandi133 – 1375Combined sources
Helixi140 – 15617Combined sources
Beta strandi158 – 17013Combined sources
Beta strandi184 – 1918Combined sources
Helixi194 – 1996Combined sources
Beta strandi206 – 2149Combined sources
Beta strandi219 – 22911Combined sources
Helixi233 – 24210Combined sources
Beta strandi246 – 2494Combined sources
Turni251 – 2544Combined sources
Helixi258 – 26811Combined sources
Helixi271 – 2733Combined sources
Beta strandi277 – 2815Combined sources
Helixi282 – 2843Combined sources
Beta strandi286 – 2883Combined sources
Beta strandi291 – 2988Combined sources
Turni300 – 3034Combined sources
Helixi304 – 31512Combined sources
Helixi322 – 33312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CF2X-ray2.10O/P/Q/R1-337[»]
ProteinModelPortaliP10618.
SMRiP10618. Positions 1-336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10618.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 1413Glyceraldehyde 3-phosphate bindingBy similarity
Regioni194 – 1952Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

KOiK00150.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00559. G3P_dehdrog_arch.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006436. Glyceraldehyde-3-P_DH_2_arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01546. GAPDH-II_archae. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10618-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKAVAINGYG TVGKRVADAI AQQDDMKVIG VSKTRPDFEA RMALKKGYDL
60 70 80 90 100
YVAIPERVKL FEKAGIEVAG TVDDMLDEAD IVIDCTPEGI GAKNLKMYKE
110 120 130 140 150
KGIKAIFQGG EKHEDIGLSF NSLSNYEESY GKDYTRVVSC NTTGLCRTLK
160 170 180 190 200
PLHDSFGIKK VRAVIVRRGA DPAQVSKGPI NAIIPNPPKL PSHHGPDVKT
210 220 230 240 250
VLDINIDTMA VIVPTTLMHQ HNVMVEVEET PTVDDIIDVF EDTPRVILIS
260 270 280 290 300
AEDGLTSTAE IMEYAKELGR SRNDLFEIPV WRESITVVDN EIYYMQAVHQ
310 320 330
ESDIVPENVD AVRAILEMEE DKYKSINKTN KAMNILQ
Length:337
Mass (Da):37,408
Last modified:July 1, 1989 - v1
Checksum:iD83CBA88AAE5B0B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19980 Genomic DNA. Translation: AAA88227.1.
PIRiJT0286.
RefSeqiYP_004003841.1. NC_014658.1.

Genome annotation databases

GeneIDi9961991.
KEGGimfv:Mfer_0276.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19980 Genomic DNA. Translation: AAA88227.1 .
PIRi JT0286.
RefSeqi YP_004003841.1. NC_014658.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CF2 X-ray 2.10 O/P/Q/R 1-337 [» ]
ProteinModelPortali P10618.
SMRi P10618. Positions 1-336.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 9961991.
KEGGi mfv:Mfer_0276.

Phylogenomic databases

KOi K00150.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00184 .
SABIO-RK P10618.

Miscellaneous databases

EvolutionaryTracei P10618.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00559. G3P_dehdrog_arch.
InterProi IPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006436. Glyceraldehyde-3-P_DH_2_arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000149. GAP_DH. 1 hit.
SMARTi SM00846. Gp_dh_N. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01546. GAPDH-II_archae. 1 hit.
PROSITEi PS00071. GAPDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary structure of glyceraldehyde-3-phosphate dehydrogenase deduced from the nucleotide sequence of the thermophilic archaebacterium Methanothermus fervidus."
    Fabry S., Hensel R.
    Gene 64:189-197(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The crystal structure of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus in the presence of NADP(+) at 2.1 A resolution."
    Charron C., Talfournier F., Isupov M.N., Littlechild J.A., Branlant G., Vitoux B., Aubry A.
    J. Mol. Biol. 297:481-500(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

Entry informationi

Entry nameiG3P_METFE
AccessioniPrimary (citable) accession number: P10618
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3