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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+.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101NADP; via amide nitrogen
Active sitei140 – 1401Nucleophile By similarity
Binding sitei171 – 1711NADP
Binding sitei300 – 3001NADP; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 122NADPUniRule annotation
Nucleotide bindingi34 – 352NADPUniRule annotation

GO - Molecular functioni

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

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

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Glyceraldehyde-3-phosphate dehydrogenaseUniRule annotation
PRO_0000145722Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP10618.

Family & Domainsi

Region

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

MKAVAINGYG TVGKRVADAI AQQDDMKVIG VSKTRPDFEA RMALKKGYDL    50
YVAIPERVKL FEKAGIEVAG TVDDMLDEAD IVIDCTPEGI GAKNLKMYKE 100
KGIKAIFQGG EKHEDIGLSF NSLSNYEESY GKDYTRVVSC NTTGLCRTLK 150
PLHDSFGIKK VRAVIVRRGA DPAQVSKGPI NAIIPNPPKL PSHHGPDVKT 200
VLDINIDTMA VIVPTTLMHQ HNVMVEVEET PTVDDIIDVF EDTPRVILIS 250
AEDGLTSTAE IMEYAKELGR SRNDLFEIPV WRESITVVDN EIYYMQAVHQ 300
ESDIVPENVD AVRAILEMEE DKYKSINKTN KAMNILQ 337
Length:337
Mass (Da):37,408
Last modified:July 1, 1989 - v1
Checksum:iD83CBA88AAE5B0B8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M19980 Genomic DNA. Translation: AAA88227.1 .
PIRi JT0286.
RefSeqi YP_004003841.1. NC_014658.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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: June 11, 2014
This is version 107 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

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