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Protein

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

Gene

gpsA

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H.UniRule annotation

Pathwayi: glycerophospholipid metabolism

This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway glycerophospholipid metabolism and in Membrane lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei110NAD; via amide nitrogenUniRule annotation1
Binding sitei110SubstrateUniRule annotation1
Binding sitei141NAD; via amide nitrogenUniRule annotation1
Active sitei192Proton acceptorUniRule annotation1
Binding sitei256NADUniRule annotation1
Binding sitei282NADUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 17NADUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(P)+]UniRule annotation (EC:1.1.1.94UniRule annotation)
Alternative name(s):
NAD(P)H-dependent glycerol-3-phosphate dehydrogenaseUniRule annotation
Gene namesi
Name:gpsAUniRule annotation
Ordered Locus Names:CBU_1518
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
Proteomesi
  • UP000002671 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001379531 – 332Glycerol-3-phosphate dehydrogenase [NAD(P)+]Add BLAST332

Interactioni

Protein-protein interaction databases

STRINGi227377.CBU_1518.

Structurei

Secondary structure

1332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 11Combined sources4
Helixi15 – 25Combined sources11
Turni26 – 28Combined sources3
Beta strandi31 – 34Combined sources4
Helixi38 – 47Combined sources10
Beta strandi48 – 50Combined sources3
Turni51 – 53Combined sources3
Beta strandi63 – 67Combined sources5
Helixi69 – 73Combined sources5
Beta strandi78 – 81Combined sources4
Helixi85 – 95Combined sources11
Helixi96 – 98Combined sources3
Beta strandi104 – 107Combined sources4
Turni114 – 116Combined sources3
Helixi119 – 127Combined sources9
Beta strandi132 – 138Combined sources7
Helixi141 – 145Combined sources5
Beta strandi150 – 157Combined sources8
Helixi159 – 169Combined sources11
Beta strandi172 – 180Combined sources9
Helixi182 – 204Combined sources23
Helixi209 – 229Combined sources21
Helixi234 – 237Combined sources4
Turni240 – 242Combined sources3
Helixi243 – 251Combined sources9
Helixi256 – 266Combined sources11
Helixi270 – 277Combined sources8
Helixi283 – 296Combined sources14
Helixi302 – 312Combined sources11
Helixi317 – 325Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K96X-ray2.10A/B1-332[»]
ProteinModelPortaliQ83BJ0.
SMRiQ83BJ0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ83BJ0.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni256 – 257Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CSF. Bacteria.
COG0240. LUCA.
HOGENOMiHOG000246854.
KOiK00057.
OMAiSAQMEMS.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00394. NAD_Glyc3P_dehydrog. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
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.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q83BJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPFKHPIAI LGAGSWGTAL ALVLARKGQK VRLWSYESDH VDEMQAEGVN
60 70 80 90 100
NRYLPNYPFP ETLKAYCDLK ASLEGVTDIL IVVPSFAFHE VITRMKPLID
110 120 130 140 150
AKTRIAWGTK GLAKGSRLLH EVVATELGQV PMAVISGPSL ATEVAANLPT
160 170 180 190 200
AVSLASNNSQ FSKDLIERLH GQRFRVYKND DMIGVELCGS VKNILAIATG
210 220 230 240 250
ISDGLKLGSN ARAALITRGL TEMGRLVSVF GGKQETLTGL AGLGDLVLTC
260 270 280 290 300
TDNQSRNRRF GLALGEGVDK KEAQQAIGQA IEGLYNTDQV HALAQKHAIE
310 320 330
MPLTFQVHRI LHEDLDPQQA VQELLERSPK AE
Length:332
Mass (Da):36,067
Last modified:June 1, 2003 - v1
Checksum:i0790551553B52A94
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO91015.1.
RefSeqiNP_820501.1. NC_002971.3.
WP_010958277.1. NZ_CCYB01000022.1.

Genome annotation databases

EnsemblBacteriaiAAO91015; AAO91015; CBU_1518.
GeneIDi1209428.
KEGGicbu:CBU_1518.
PATRICi17931803. VBICoxBur82552_1521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO91015.1.
RefSeqiNP_820501.1. NC_002971.3.
WP_010958277.1. NZ_CCYB01000022.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K96X-ray2.10A/B1-332[»]
ProteinModelPortaliQ83BJ0.
SMRiQ83BJ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227377.CBU_1518.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO91015; AAO91015; CBU_1518.
GeneIDi1209428.
KEGGicbu:CBU_1518.
PATRICi17931803. VBICoxBur82552_1521.

Phylogenomic databases

eggNOGiENOG4105CSF. Bacteria.
COG0240. LUCA.
HOGENOMiHOG000246854.
KOiK00057.
OMAiSAQMEMS.

Enzyme and pathway databases

UniPathwayiUPA00940.

Miscellaneous databases

EvolutionaryTraceiQ83BJ0.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00394. NAD_Glyc3P_dehydrog. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
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.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGPDA_COXBU
AccessioniPrimary (citable) accession number: Q83BJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 95 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, Complete proteome, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.