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Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic

Gene

GPD1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971NADBy similarity
Binding sitei120 – 1201NAD; via amide nitrogenBy similarity
Binding sitei120 – 1201SubstrateBy similarity
Binding sitei153 – 1531NAD; via amide nitrogenBy similarity
Active sitei204 – 2041Proton acceptorBy similarity
Binding sitei269 – 2691NADBy similarity
Binding sitei298 – 2981NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156NADBy similarity

GO - Molecular functioni

  1. glycerol-3-phosphate dehydrogenase [NAD+] activity Source: UniProtKB-EC
  2. NAD binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. glycerol-3-phosphate catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKP08507.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic (EC:1.1.1.8)
Short name:
GPD-C
Short name:
GPDH-C
Gene namesi
Name:GPD1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. glycerol-3-phosphate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmicPRO_0000138081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541PhosphoserineBy similarity
Modified residuei289 – 2891N6-succinyllysineBy similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP08507.
SMRiP08507. Positions 1-349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni269 – 2702Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG003669.
InParanoidiP08507.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08507-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGKKVCIVG SGDWGSAIAK IVGGNAAQLA QFDPRVTMWV FEEDIGGKKL
60 70 80 90 100
TEIINTHQEN VKYLPGHKLP PNVVAVPDVV KAAADADILI FVVPHQFIGK
110 120 130 140 150
ICDEIKGHLK ANAIGISLIK GVNEGPKGLK LISEVIGEHL GIPMSVLMGA
160 170 180 190 200
NIASEVADEK FCETTIGCKD QAQGQLLKQL MQTPNFRIVV TQEVNTVEIC
210 220 230 240 250
GALKDLVAVG AGFCDGIGFG DNTKAAVIRL GLMEMIAFAK LFCSGPVSPA
260 270 280 290 300
TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE MLNGQKLQGP
310 320 330 340
ETARELHSIL QHKGLVDWFP LFMAVYKVCY QGQPVGEFIR CLQNHPEHM
Length:349
Mass (Da):37,610
Last modified:January 23, 2007 - v2
Checksum:iA11FE0E1F4ADD807
GO

Sequence databases

PIRiA32512.

Cross-referencesi

Sequence databases

PIRiA32512.

3D structure databases

ProteinModelPortaliP08507.
SMRiP08507. Positions 1-349.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003669.
InParanoidiP08507.

Enzyme and pathway databases

SABIO-RKP08507.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of secondary structural elements in glycerol-3-phosphate dehydrogenase by comparison with other dehydrogenases."
    Otto J., Argos P., Rossmann M.G.
    Eur. J. Biochem. 109:325-330(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: SECONDARY STRUCTURE PREDICTION.

Entry informationi

Entry nameiGPDA_RABIT
AccessioniPrimary (citable) accession number: P08507
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.