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Protein

Digeranylgeranylglycerophospholipid reductase

Gene

Ta0516

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di-O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains. Can use both NADH and NADPH as electron donors. Also catalyzes the reduction of the naturally occurring 2,3-di-O-geranylgeranylglyceryl phosphate derivatives such as 2,3-di-O-phytyl-sn-glyceryl phosphate (DPHGP), 3-O-(2,3-di-O-phytyl-sn-glycero-phospho)-sn-glycerol (DPHGPG) and 2,3-di-O-phytyl-sn-glycero-phosphoethanolamine (DPHGPE). Is not active toward 2,3-di-O-geranylgeranylglycerol.2 Publications

Catalytic activityi

2,3-bis-(O-phytanyl)-sn-glycerol 1-phosphate + 8 NAD(P)+ = 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate + 8 NAD(P)H.1 Publication

Cofactori

FAD3 PublicationsNote: Binds 1 FAD per subunit.3 Publications

Pathwayi: glycerophospholipid metabolism

This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491Substrate1 Publication
Binding sitei100 – 1001FAD1 Publication
Binding sitei124 – 1241FAD; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei162 – 1621FAD1 Publication
Binding sitei283 – 2831FAD1 Publication
Binding sitei338 – 3381Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 145FAD1 Publication
Nucleotide bindingi33 – 353FAD1 Publication
Nucleotide bindingi44 – 474FAD1 Publication
Nucleotide bindingi295 – 2962FAD1 Publication

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

FAD, Flavoprotein, NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17979.
BRENDAi1.3.1.101. 6324.
1.3.1.83. 6324.
UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended name:
Digeranylgeranylglycerophospholipid reductase (EC:1.3.1.101)
Short name:
DGGGPL reductase
Alternative name(s):
2,3-bis-O-geranylgeranylglyceryl phosphate reductase
Geranylgeranyl reductase
Short name:
GGR
Gene namesi
Ordered Locus Names:Ta0516
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

Subcellular locationi

  • Cell membrane 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Digeranylgeranylglycerophospholipid reductasePRO_0000350723Add
BLAST

Proteomic databases

PRIDEiQ9HKS9.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi273075.Ta0516m.

Structurei

Secondary structure

396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 99Combined sources
Helixi13 – 2412Combined sources
Beta strandi29 – 324Combined sources
Beta strandi34 – 374Combined sources
Beta strandi47 – 493Combined sources
Helixi51 – 555Combined sources
Turni62 – 643Combined sources
Beta strandi65 – 7511Combined sources
Beta strandi83 – 864Combined sources
Beta strandi88 – 914Combined sources
Beta strandi95 – 984Combined sources
Helixi100 – 11415Combined sources
Beta strandi117 – 1215Combined sources
Beta strandi124 – 1307Combined sources
Beta strandi133 – 1419Combined sources
Beta strandi144 – 15512Combined sources
Helixi162 – 1676Combined sources
Helixi170 – 1723Combined sources
Helixi176 – 1783Combined sources
Beta strandi179 – 18911Combined sources
Beta strandi196 – 2005Combined sources
Beta strandi208 – 2169Combined sources
Beta strandi219 – 2279Combined sources
Turni228 – 2303Combined sources
Helixi234 – 24613Combined sources
Helixi249 – 2524Combined sources
Beta strandi254 – 26512Combined sources
Beta strandi278 – 2803Combined sources
Helixi282 – 2854Combined sources
Turni290 – 2923Combined sources
Helixi296 – 31621Combined sources
Helixi321 – 35030Combined sources
Helixi354 – 36411Combined sources
Helixi374 – 38411Combined sources
Helixi386 – 39510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OZ2X-ray1.60A1-396[»]
ProteinModelPortaliQ9HKS9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HKS9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni208 – 2147Substrate binding1 Publication
Regioni291 – 2944Substrate binding1 Publication
Regioni372 – 3743Substrate binding1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG00570. Archaea.
COG0644. LUCA.
KOiK17830.
OMAiNVIVEFL.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_01287. DGGGPL_reductase.
InterProiIPR023590. DGGGPL_reductase.
IPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR011777. Geranylgeranyl_Rdtase_fam.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR02032. GG-red-SF. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HKS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METYDVLVVG GGPGGSTAAR YAAKYGLKTL MIEKRPEIGS PVRCGEGLSK
60 70 80 90 100
GILNEADIKA DRSFIANEVK GARIYGPSEK RPIILQSEKA GNEVGYVLER
110 120 130 140 150
DKFDKHLAAL AAKAGADVWV KSPALGVIKE NGKVAGAKIR HNNEIVDVRA
160 170 180 190 200
KMVIAADGFE SEFGRWAGLK SVILARNDII SALQYRMINV DVDPDYTDFY
210 220 230 240 250
LGSIAPAGYI WVFPKGEGMA NVGIGSSINW IHNRFELKNY LDRFIENHPG
260 270 280 290 300
LKKGQDIQLV TGGVSVSKVK MPITMPGLML VGDAARLIDP ITGGGIANAI
310 320 330 340 350
VSGMYAAQVT KEAIESNDYS PQMMQKYEKL IKERFERKHL RNWVAKEKLA
360 370 380 390
MLSDDTLDKL VDIVSEQVLT TISVEAILKA IAEKYPEVVK ELEDLI
Length:396
Mass (Da):43,353
Last modified:September 23, 2008 - v2
Checksum:iC607688CD4144EF8
GO

Sequence cautioni

The sequence CAC11656.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445064 Genomic DNA. Translation: CAC11656.1. Different initiation.
RefSeqiWP_010900941.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC11656; CAC11656; CAC11656.
GeneIDi1457015.
KEGGitac:Ta0516m.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445064 Genomic DNA. Translation: CAC11656.1. Different initiation.
RefSeqiWP_010900941.1. NC_002578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OZ2X-ray1.60A1-396[»]
ProteinModelPortaliQ9HKS9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta0516m.

Proteomic databases

PRIDEiQ9HKS9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC11656; CAC11656; CAC11656.
GeneIDi1457015.
KEGGitac:Ta0516m.

Phylogenomic databases

eggNOGiarCOG00570. Archaea.
COG0644. LUCA.
KOiK17830.
OMAiNVIVEFL.

Enzyme and pathway databases

UniPathwayiUPA00940.
BioCyciMetaCyc:MONOMER-17979.
BRENDAi1.3.1.101. 6324.
1.3.1.83. 6324.

Miscellaneous databases

EvolutionaryTraceiQ9HKS9.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_01287. DGGGPL_reductase.
InterProiIPR023590. DGGGPL_reductase.
IPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR011777. Geranylgeranyl_Rdtase_fam.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR02032. GG-red-SF. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
    Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
    Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  2. "Biosynthesis of archaeal membrane lipids: digeranylgeranylglycerophospholipid reductase of the thermoacidophilic archaeon Thermoplasma acidophilum."
    Nishimura Y., Eguchi T.
    J. Biochem. 139:1073-1081(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  3. "Stereochemistry of reduction in digeranylgeranylglycerophospholipid reductase involved in the biosynthesis of archaeal membrane lipids from Thermoplasma acidophilum."
    Nishimura Y., Eguchi T.
    Bioorg. Chem. 35:276-283(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, REACTION STEREOCHEMISTRY.
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  4. "Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids."
    Xu Q., Eguchi T., Mathews I.I., Rife C.L., Chiu H.J., Farr C.L., Feuerhelm J., Jaroszewski L., Klock H.E., Knuth M.W., Miller M.D., Weekes D., Elsliger M.A., Deacon A.M., Godzik A., Lesley S.A., Wilson I.A.
    J. Mol. Biol. 404:403-417(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FAD AND LIPID, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiGGR_THEAC
AccessioniPrimary (citable) accession number: Q9HKS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: September 23, 2008
Last modified: April 13, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Reduction reaction proceeds via syn addition of hydrogen for double bonds.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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

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.