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P56649

- G3P_PANVR

UniProt

P56649 - G3P_PANVR

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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene
N/A
Organism
Panulirus versicolor (Spiny blue lobster) (Palinurus versicolor)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311NAD
Binding sitei76 – 761NAD; via carbonyl oxygen By similarity
Active sitei148 – 1481Nucleophile
Sitei175 – 1751Activates thiol group during catalysis
Binding sitei178 – 1781Glyceraldehyde 3-phosphate By similarity
Binding sitei230 – 2301Glyceraldehyde 3-phosphate By similarity
Binding sitei312 – 3121NAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 112NAD

GO - Molecular functioni

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

GO - Biological processi

  1. glucose metabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKP56649.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.12)
Short name:
GAPDH
OrganismiPanulirus versicolor (Spiny blue lobster) (Palinurus versicolor)
Taxonomic identifieri150436 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAchelataPalinuroideaPalinuridaePanulirus

Subcellular locationi

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 – 333333Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylserine

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP56649.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64
Helixi10 – 2213
Beta strandi26 – 305
Beta strandi32 – 343
Helixi36 – 449
Turni47 – 493
Beta strandi56 – 594
Beta strandi62 – 654
Beta strandi68 – 736
Helixi78 – 803
Helixi83 – 864
Beta strandi90 – 934
Beta strandi95 – 973
Helixi101 – 1044
Helixi105 – 1084
Turni109 – 1113
Beta strandi113 – 1197
Beta strandi122 – 1243
Turni129 – 1313
Helixi133 – 1353
Beta strandi142 – 1443
Helixi148 – 16417
Beta strandi166 – 17510
Beta strandi181 – 1855
Helixi193 – 1953
Turni198 – 2003
Beta strandi203 – 2053
Helixi209 – 2168
Helixi218 – 2203
Turni221 – 2233
Beta strandi224 – 2307
Beta strandi237 – 24711
Helixi251 – 26313
Turni264 – 2696
Beta strandi270 – 2734
Helixi279 – 2824
Beta strandi288 – 2925
Turni293 – 2953
Beta strandi297 – 3004
Beta strandi303 – 3108
Helixi314 – 33118

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CRWX-ray2.00G/R1-333[»]
1DSSX-ray1.88G/R1-333[»]
1IHXX-ray2.80A/B/C/D1-333[»]
1IHYX-ray3.00A/B/C/D1-333[»]
1SZJX-ray2.00G/R1-333[»]
ProteinModelPortaliP56649.
SMRiP56649. Positions 1-333.

Miscellaneous databases

EvolutionaryTraceiP56649.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 1493Glyceraldehyde 3-phosphate binding By similarity
Regioni207 – 2082Glyceraldehyde 3-phosphate binding By similarity

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
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.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56649-1 [UniParc]FASTAAdd to Basket

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SKIGINGFGR IGRLVLRAAL EMGAQVVAVN DPFIALEYMV YMFKYDSTHG    50
MFKGEVKAED GALVVDGKKI TVFNEMKPEN IPWSKAGAEY IVESTGVFTT 100
IEKASAHFKG GAKKVIISAP SADAPMFVCG VNLEKYSKDM KVVSNASCTT 150
NCLAPVAKVL HENFEIVEGL MTTVHAVTAT QKTVDGPSAK DWRGGRGAAQ 200
NIIPSSTGAA KAVGKVIPEL DGKLTGMAFR VPTPNVSVVD LTVRLGKECS 250
YDDIKAAMKA ASEGPLQGVL GYTEDDVVSC DFTGDNRSSI FDAKAGIQLS 300
KTFVKVVSWY DNEFGYSQRV IDLIKHMQKV DSA 333
Length:333
Mass (Da):35,724
Last modified:July 15, 1999 - v1
Checksum:i818572106E294C19
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CRW X-ray 2.00 G/R 1-333 [» ]
1DSS X-ray 1.88 G/R 1-333 [» ]
1IHX X-ray 2.80 A/B/C/D 1-333 [» ]
1IHY X-ray 3.00 A/B/C/D 1-333 [» ]
1SZJ X-ray 2.00 G/R 1-333 [» ]
ProteinModelPortali P56649.
SMRi P56649. Positions 1-333.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P56649.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00184 .
SABIO-RK P56649.

Miscellaneous databases

EvolutionaryTracei P56649.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
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.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR10836. PTHR10836. 1 hit.
Pfami PF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000149. GAP_DH. 1 hit.
PRINTSi PR00078. G3PDHDRGNASE.
SMARTi SM00846. Gp_dh_N. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01534. GAPDH-I. 1 hit.
PROSITEi PS00071. GAPDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Structure of D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor carrying the fluorescent NAD derivatives at 2.7-A resolution."
    Lin Z.J., Li J., Zhang F.M., Song S.Y., Yang J., Liang S.J., Tsou C.L.
    Arch. Biochem. Biophys. 302:161-166(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  2. "Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor refined at 2-A resolution."
    Song S.Y., Li J., Lin Z.J.
    Acta Crystallogr. D 54:558-569(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH NAD.
    Tissue: Muscle.

Entry informationi

Entry nameiG3P_PANVR
AccessioniPrimary (citable) accession number: P56649
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: June 11, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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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