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Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)] 2

Gene

GPD2

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
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 sitei157 – 1571NADBy similarity
Binding sitei180 – 1801NAD; via amide nitrogenBy similarity
Binding sitei180 – 1801SubstrateBy similarity
Binding sitei213 – 2131NAD; via amide nitrogenBy similarity
Active sitei273 – 2731Proton acceptorBy similarity
Binding sitei338 – 3381NADBy similarity
Binding sitei367 – 3671NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi69 – 746NADBy 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

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)] 2 (EC:1.1.1.8)
Gene namesi
Name:GPD2
Ordered Locus Names:CAGL0C05137g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
ProteomesiUP000002428 Componenti: Chromosome C

Organism-specific databases

EuPathDBiFungiDB:CAGL0C05137g.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Glycerol-3-phosphate dehydrogenase [NAD(+)] 2PRO_0000138087Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ6FWJ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni338 – 3392Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000246855.
InParanoidiQ6FWJ7.
KOiK00006.
OMAiEVANDNF.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
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]
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6FWJ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFVRLARIPR ITRHYRLGLF STQPKPKPNE YLYYRNKHKS KMEAPIKRSS
60 70 80 90 100
SAVSLVELER EPFKVTVIGS GNWGTTIAKV VAENTKANPQ VFQERVDMWV
110 120 130 140 150
FDENIDGTML TEIINTKHQN VKYLPNIDLP ENLVANPDLL KSVEGADILV
160 170 180 190 200
FNIPHQFLPK IVDQLRGHVE PHVRAISCLK GFEVGKKGVQ LLSTYITEEL
210 220 230 240 250
GIECGALSGA NLAPEVAKEH WSETTVAYHI PKDYQGDGMD VDHKVLKLLF
260 270 280 290 300
HRPYFHVSVI DDVAGISIAG ALKNVVALGC GFVEGLGWGN NAAAAIQRVG
310 320 330 340 350
LGEIIKFGQM FFPESRVETY YQESAGVADL ITTCSGGRNV RVATHMAKTG
360 370 380 390 400
KSAEDSEKEL LNGQSAQGVI TCKEVHEWLS TCEMIEEFPL FEAVYKIVYE
410 420
DVPMHKLPEM IEELDDIVVA GQ
Length:422
Mass (Da):47,005
Last modified:July 19, 2004 - v1
Checksum:i4BDF81C8757F3EB9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380949 Genomic DNA. Translation: CAG58303.1.
RefSeqiXP_445397.1. XM_445397.1.

Genome annotation databases

GeneIDi2886789.
KEGGicgr:CAGL0C05137g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380949 Genomic DNA. Translation: CAG58303.1.
RefSeqiXP_445397.1. XM_445397.1.

3D structure databases

ProteinModelPortaliQ6FWJ7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2886789.
KEGGicgr:CAGL0C05137g.

Organism-specific databases

EuPathDBiFungiDB:CAGL0C05137g.

Phylogenomic databases

HOGENOMiHOG000246855.
InParanoidiQ6FWJ7.
KOiK00006.
OMAiEVANDNF.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
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]
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGPD2_CANGA
AccessioniPrimary (citable) accession number: Q6FWJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 19, 2004
Last modified: April 29, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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.