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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 (Painted spiny 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.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311NAD1 Publication
Binding sitei76 – 761NAD; via carbonyl oxygenBy similarity
Active sitei148 – 1481Nucleophile
Sitei175 – 1751Activates thiol group during catalysis
Binding sitei178 – 1781Glyceraldehyde 3-phosphateBy similarity
Binding sitei230 – 2301Glyceraldehyde 3-phosphateBy similarity
Binding sitei312 – 3121NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 112NAD1 Publication

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 (Painted spiny lobster) (Palinurus versicolor)
Taxonomic identifieri150436 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAchelataPalinuroideaPalinuridaePanulirus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
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.1 Publication

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56649.

Family & Domainsi

Region

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

« Hide

        10         20         30         40         50
SKIGINGFGR IGRLVLRAAL EMGAQVVAVN DPFIALEYMV YMFKYDSTHG
60 70 80 90 100
MFKGEVKAED GALVVDGKKI TVFNEMKPEN IPWSKAGAEY IVESTGVFTT
110 120 130 140 150
IEKASAHFKG GAKKVIISAP SADAPMFVCG VNLEKYSKDM KVVSNASCTT
160 170 180 190 200
NCLAPVAKVL HENFEIVEGL MTTVHAVTAT QKTVDGPSAK DWRGGRGAAQ
210 220 230 240 250
NIIPSSTGAA KAVGKVIPEL DGKLTGMAFR VPTPNVSVVD LTVRLGKECS
260 270 280 290 300
YDDIKAAMKA ASEGPLQGVL GYTEDDVVSC DFTGDNRSSI FDAKAGIQLS
310 320 330
KTFVKVVSWY DNEFGYSQRV IDLIKHMQKV DSA
Length:333
Mass (Da):35,724
Last modified:July 15, 1999 - v1
Checksum:i818572106E294C19
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 86 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