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Protein

GDP-L-fucose synthase

Gene

TSTA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.1 Publication

Catalytic activityi

GDP-beta-L-fucose + NADP+ = GDP-4-dehydro-alpha-D-rhamnose + NADPH.

Pathwayi: GDP-L-fucose biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes GDP-L-fucose from GDP-alpha-D-mannose.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. GDP-mannose 4,6 dehydratase (GMDS)
  2. GDP-L-fucose synthase (TSTA3)
This subpathway is part of the pathway GDP-L-fucose biosynthesis via de novo pathway, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes GDP-L-fucose from GDP-alpha-D-mannose, the pathway GDP-L-fucose biosynthesis via de novo pathway and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei114Important for catalytic activityBy similarity1
Sitei116Important for catalytic activityBy similarity1
Active sitei143Proton donor/acceptorBy similarity1
Binding sitei147NADP2 Publications1
Sitei147Lowers pKa of active site TyrBy similarity1
Binding sitei186NADP1 Publication1
Binding sitei194Substrate1 Publication1
Binding sitei208Substrate1 Publication1
Binding sitei215Substrate1 Publication1
Binding sitei277Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 20NADP2 Publications7
Nucleotide bindingi170 – 173NADP2 Publications4

GO - Molecular functioni

  • coenzyme binding Source: InterPro
  • electron transfer activity Source: UniProtKB
  • GDP-4-dehydro-D-rhamnose reductase activity Source: UniProtKB
  • GDP-L-fucose synthase activity Source: UniProtKB
  • GDP-mannose 3,5-epimerase activity Source: FlyBase
  • identical protein binding Source: IntAct
  • isomerase activity Source: Reactome

GO - Biological processi

  • 'de novo' GDP-L-fucose biosynthetic process Source: UniProtKB
  • GDP-mannose metabolic process Source: UniProtKB
  • leukocyte cell-cell adhesion Source: UniProtKB

Keywordsi

Molecular functionIsomerase, Multifunctional enzyme, Oxidoreductase
LigandNADP

Enzyme and pathway databases

ReactomeiR-HSA-6787639 GDP-fucose biosynthesis
UniPathwayiUPA00128; UER00191

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-L-fucose synthase (EC:1.1.1.271)
Alternative name(s):
GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase
Protein FX
Red cell NADP(H)-binding protein
Short-chain dehydrogenase/reductase family 4E member 1
Gene namesi
Name:TSTA3
Synonyms:SDR4E1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000104522.15
HGNCiHGNC:12390 TSTA3
MIMi137020 gene
neXtProtiNX_Q13630

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Organism-specific databases

DisGeNETi7264
OpenTargetsiENSG00000104522
PharmGKBiPA37056

Chemistry databases

DrugBankiDB00157 NADH

Polymorphism and mutation databases

BioMutaiTSTA3
DMDMi13124123

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001743501 – 321GDP-L-fucose synthaseAdd BLAST321

Proteomic databases

EPDiQ13630
MaxQBiQ13630
PaxDbiQ13630
PeptideAtlasiQ13630
PRIDEiQ13630

2D gel databases

REPRODUCTION-2DPAGEiIPI00014361

PTM databases

iPTMnetiQ13630
PhosphoSitePlusiQ13630
SwissPalmiQ13630

Expressioni

Gene expression databases

BgeeiENSG00000104522
CleanExiHS_TSTA3
ExpressionAtlasiQ13630 baseline and differential
GenevisibleiQ13630 HS

Organism-specific databases

HPAiHPA023361

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-3910586,EBI-3910586

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi113115, 33 interactors
IntActiQ13630, 2 interactors
STRINGi9606.ENSP00000398803

Structurei

Secondary structure

1321
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 13Combined sources5
Turni14 – 16Combined sources3
Helixi18 – 23Combined sources6
Turni27 – 29Combined sources3
Beta strandi37 – 40Combined sources4
Beta strandi43 – 46Combined sources4
Helixi51 – 60Combined sources10
Beta strandi64 – 68Combined sources5
Turni74 – 77Combined sources4
Beta strandi78 – 80Combined sources3
Helixi83 – 103Combined sources21
Beta strandi107 – 112Combined sources6
Helixi115 – 117Combined sources3
Beta strandi118 – 121Combined sources4
Beta strandi124 – 126Combined sources3
Helixi128 – 130Combined sources3
Beta strandi138 – 140Combined sources3
Helixi141 – 161Combined sources21
Beta strandi164 – 170Combined sources7
Beta strandi172 – 175Combined sources4
Turni182 – 184Combined sources3
Helixi187 – 199Combined sources13
Beta strandi201 – 203Combined sources3
Beta strandi207 – 209Combined sources3
Beta strandi217 – 219Combined sources3
Helixi220 – 232Combined sources13
Beta strandi240 – 242Combined sources3
Helixi246 – 248Combined sources3
Helixi252 – 263Combined sources12
Beta strandi269 – 272Combined sources4
Helixi287 – 292Combined sources6
Helixi301 – 314Combined sources14
Turni315 – 318Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B8WX-ray2.75A/B7-320[»]
4B8ZX-ray2.75A/B/C/D8-320[»]
4BKPX-ray2.70A/B/C/D8-321[»]
4BL5X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L8-321[»]
4E5YX-ray2.37A/B/C/D1-321[»]
ProteinModelPortaliQ13630
SMRiQ13630
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1431 Eukaryota
COG0451 LUCA
GeneTreeiENSGT00390000004681
HOGENOMiHOG000168011
HOVERGENiHBG000059
InParanoidiQ13630
KOiK02377
OMAiIHCAGRV
OrthoDBiEOG091G0CG3
PhylomeDBiQ13630
TreeFamiTF314936

Family and domain databases

CDDicd05239 GDP_FS_SDR_e, 1 hit
HAMAPiMF_00956 GDP_fucose_synth, 1 hit
InterProiView protein in InterPro
IPR001509 Epimerase_deHydtase
IPR028614 GDP_fucose/colitose_synth
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF01370 Epimerase, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit

Sequencei

Sequence statusi: Complete.

Q13630-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEPQGSMRI LVTGGSGLVG KAIQKVVADG AGLPGEDWVF VSSKDADLTD
60 70 80 90 100
TAQTRALFEK VQPTHVIHLA AMVGGLFRNI KYNLDFWRKN VHMNDNVLHS
110 120 130 140 150
AFEVGARKVV SCLSTCIFPD KTTYPIDETM IHNGPPHNSN FGYSYAKRMI
160 170 180 190 200
DVQNRAYFQQ YGCTFTAVIP TNVFGPHDNF NIEDGHVLPG LIHKVHLAKS
210 220 230 240 250
SGSALTVWGT GNPRRQFIYS LDLAQLFIWV LREYNEVEPI ILSVGEEDEV
260 270 280 290 300
SIKEAAEAVV EAMDFHGEVT FDTTKSDGQF KKTASNSKLR TYLPDFRFTP
310 320
FKQAVKETCA WFTDNYEQAR K
Length:321
Mass (Da):35,893
Last modified:November 1, 1996 - v1
Checksum:i94BB1FF61658007C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5Q → E AA sequence (PubMed:7803801).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58766 mRNA Translation: AAC50786.1
AK313560 mRNA Translation: BAG36334.1
CH471162 Genomic DNA Translation: EAW82218.1
CH471162 Genomic DNA Translation: EAW82220.1
CH471162 Genomic DNA Translation: EAW82222.1
BC001941 mRNA Translation: AAH01941.1
BC093061 mRNA Translation: AAH93061.1
CCDSiCCDS6408.1
RefSeqiNP_001304712.1, NM_001317783.1
NP_003304.1, NM_003313.3
XP_005251108.2, XM_005251051.3
XP_011515571.1, XM_011517269.1
UniGeneiHs.404119

Genome annotation databases

EnsembliENST00000425753; ENSP00000398803; ENSG00000104522
ENST00000529064; ENSP00000435386; ENSG00000104522
ENST00000612580; ENSP00000478042; ENSG00000278243
ENST00000633782; ENSP00000487640; ENSG00000278243
GeneIDi7264
KEGGihsa:7264
UCSCiuc003yza.3 human

Similar proteinsi

Entry informationi

Entry nameiFCL_HUMAN
AccessioniPrimary (citable) accession number: Q13630
Secondary accession number(s): B2R8Y7
, D3DWK5, Q567Q9, Q9UDG7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 160 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

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