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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)DescriptionActionsGraphical viewLength
Binding sitei49Substrate1 Publication1
Binding sitei100FAD1 Publication1
Binding sitei124FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei162FAD1 Publication1
Binding sitei283FAD1 Publication1
Binding sitei338Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 14FAD1 Publication5
Nucleotide bindingi33 – 35FAD1 Publication3
Nucleotide bindingi44 – 47FAD1 Publication4
Nucleotide bindingi295 – 296FAD1 Publication2

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)DescriptionActionsGraphical viewLength
ChainiPRO_00003507231 – 396Digeranylgeranylglycerophospholipid reductaseAdd BLAST396

Proteomic databases

PRIDEiQ9HKS9.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi273075.Ta0516m.

Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 9Combined sources9
Helixi13 – 24Combined sources12
Beta strandi29 – 32Combined sources4
Beta strandi34 – 37Combined sources4
Beta strandi47 – 49Combined sources3
Helixi51 – 55Combined sources5
Turni62 – 64Combined sources3
Beta strandi65 – 75Combined sources11
Beta strandi83 – 86Combined sources4
Beta strandi88 – 91Combined sources4
Beta strandi95 – 98Combined sources4
Helixi100 – 114Combined sources15
Beta strandi117 – 121Combined sources5
Beta strandi124 – 130Combined sources7
Beta strandi133 – 141Combined sources9
Beta strandi144 – 155Combined sources12
Helixi162 – 167Combined sources6
Helixi170 – 172Combined sources3
Helixi176 – 178Combined sources3
Beta strandi179 – 189Combined sources11
Beta strandi196 – 200Combined sources5
Beta strandi208 – 216Combined sources9
Beta strandi219 – 227Combined sources9
Turni228 – 230Combined sources3
Helixi234 – 246Combined sources13
Helixi249 – 252Combined sources4
Beta strandi254 – 265Combined sources12
Beta strandi278 – 280Combined sources3
Helixi282 – 285Combined sources4
Turni290 – 292Combined sources3
Helixi296 – 316Combined sources21
Helixi321 – 350Combined sources30
Helixi354 – 364Combined sources11
Helixi374 – 384Combined sources11
Helixi386 – 395Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OZ2X-ray1.60A1-396[»]
ProteinModelPortaliQ9HKS9.
SMRiQ9HKS9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HKS9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni208 – 214Substrate binding1 Publication7
Regioni291 – 294Substrate binding1 Publication4
Regioni372 – 374Substrate binding1 Publication3

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG00570. Archaea.
COG0644. LUCA.
KOiK17830.
OMAiWIAFEEY.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_01287. DGGGPL_reductase. 1 hit.
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 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:Ta0516.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OZ2X-ray1.60A1-396[»]
ProteinModelPortaliQ9HKS9.
SMRiQ9HKS9.
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:Ta0516.

Phylogenomic databases

eggNOGiarCOG00570. Archaea.
COG0644. LUCA.
KOiK17830.
OMAiWIAFEEY.

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. 1 hit.
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...

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: November 2, 2016
This is version 97 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.