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Protein

GDP-L-fucose synthase

Gene

TSTA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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-6-deoxy-alpha-D-mannose + NADPH.

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei114 – 1141Important for catalytic activityBy similarity
Sitei116 – 1161Important for catalytic activityBy similarity
Active sitei143 – 1431Proton donor/acceptorBy similarity
Binding sitei147 – 1471NADP1 Publication
Sitei147 – 1471Lowers pKa of active site TyrBy similarity
Binding sitei186 – 1861NADP1 Publication
Binding sitei194 – 1941Substrate
Binding sitei208 – 2081Substrate
Binding sitei215 – 2151Substrate
Binding sitei277 – 2771Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 207NADP1 Publication
Nucleotide bindingi170 – 1734NADP1 Publication

GO - Molecular functioni

  • coenzyme binding Source: InterPro
  • electron carrier activity Source: UniProtKB
  • GDP-4-dehydro-D-rhamnose reductase activity Source: UniProtKB
  • GDP-L-fucose synthase activity Source: UniProtKB
  • isomerase activity Source: UniProtKB-KW

GO - Biological processi

  • 'de novo' GDP-L-fucose biosynthetic process Source: UniProtKB
  • cytolysis Source: Ensembl
  • GDP-mannose metabolic process Source: UniProtKB
  • leukocyte cell-cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

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
ProteomesiUP000005640 Componentsi: Chromosome 8, Unplaced

Organism-specific databases

HGNCiHGNC:12390. TSTA3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37056.

Polymorphism and mutation databases

BioMutaiTSTA3.
DMDMi13124123.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321GDP-L-fucose synthasePRO_0000174350Add
BLAST

Proteomic databases

MaxQBiQ13630.
PaxDbiQ13630.
PeptideAtlasiQ13630.
PRIDEiQ13630.

2D gel databases

REPRODUCTION-2DPAGEIPI00014361.

PTM databases

PhosphoSiteiQ13630.

Expressioni

Gene expression databases

BgeeiQ13630.
CleanExiHS_TSTA3.
ExpressionAtlasiQ13630. baseline and differential.
GenevisibleiQ13630. HS.

Organism-specific databases

HPAiHPA023361.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi113115. 15 interactions.
IntActiQ13630. 2 interactions.
STRINGi9606.ENSP00000398803.

Structurei

Secondary structure

1
321
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135Combined sources
Turni14 – 163Combined sources
Helixi18 – 236Combined sources
Turni27 – 293Combined sources
Beta strandi37 – 404Combined sources
Beta strandi43 – 464Combined sources
Helixi51 – 6010Combined sources
Beta strandi64 – 685Combined sources
Turni74 – 774Combined sources
Beta strandi78 – 803Combined sources
Helixi83 – 10321Combined sources
Beta strandi107 – 1126Combined sources
Helixi115 – 1173Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi124 – 1263Combined sources
Helixi128 – 1303Combined sources
Beta strandi138 – 1403Combined sources
Helixi141 – 16121Combined sources
Beta strandi164 – 1707Combined sources
Beta strandi172 – 1754Combined sources
Turni182 – 1843Combined sources
Helixi187 – 19913Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi207 – 2093Combined sources
Beta strandi217 – 2193Combined sources
Helixi220 – 23213Combined sources
Beta strandi240 – 2423Combined sources
Helixi246 – 2483Combined sources
Helixi252 – 26312Combined sources
Beta strandi269 – 2724Combined sources
Helixi287 – 2926Combined sources
Helixi301 – 31414Combined sources
Turni315 – 3184Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 4-321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0451.
GeneTreeiENSGT00390000004681.
HOGENOMiHOG000168011.
HOVERGENiHBG000059.
InParanoidiQ13630.
KOiK02377.
OMAiIHCAGRV.
PhylomeDBiQ13630.
TreeFamiTF314936.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00956. GDP_fucose_synth.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR028614. GDP_fucose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51Q → E AA sequence (PubMed:7803801).Curated

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_003304.1. NM_003313.3.
XP_005251108.2. XM_005251051.2.
XP_006725156.2. XM_006725093.2.
UniGeneiHs.404119.

Genome annotation databases

EnsembliENST00000425753; ENSP00000398803; ENSG00000104522.
ENST00000529064; ENSP00000435386; ENSG00000104522.
ENST00000612580; ENSP00000478042; ENSG00000278243.
GeneIDi7264.
KEGGihsa:7264.
UCSCiuc003yza.2. human.

Cross-referencesi

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_003304.1. NM_003313.3.
XP_005251108.2. XM_005251051.2.
XP_006725156.2. XM_006725093.2.
UniGeneiHs.404119.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 4-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113115. 15 interactions.
IntActiQ13630. 2 interactions.
STRINGi9606.ENSP00000398803.

PTM databases

PhosphoSiteiQ13630.

Polymorphism and mutation databases

BioMutaiTSTA3.
DMDMi13124123.

2D gel databases

REPRODUCTION-2DPAGEIPI00014361.

Proteomic databases

MaxQBiQ13630.
PaxDbiQ13630.
PeptideAtlasiQ13630.
PRIDEiQ13630.

Protocols and materials databases

DNASUi7264.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000425753; ENSP00000398803; ENSG00000104522.
ENST00000529064; ENSP00000435386; ENSG00000104522.
ENST00000612580; ENSP00000478042; ENSG00000278243.
GeneIDi7264.
KEGGihsa:7264.
UCSCiuc003yza.2. human.

Organism-specific databases

CTDi7264.
GeneCardsiGC08M144694.
HGNCiHGNC:12390. TSTA3.
HPAiHPA023361.
MIMi137020. gene.
neXtProtiNX_Q13630.
PharmGKBiPA37056.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0451.
GeneTreeiENSGT00390000004681.
HOGENOMiHOG000168011.
HOVERGENiHBG000059.
InParanoidiQ13630.
KOiK02377.
OMAiIHCAGRV.
PhylomeDBiQ13630.
TreeFamiTF314936.

Enzyme and pathway databases

UniPathwayiUPA00128; UER00191.

Miscellaneous databases

GeneWikiiTSTA3.
GenomeRNAii7264.
NextBioi28399.
PROiQ13630.
SOURCEiSearch...

Gene expression databases

BgeeiQ13630.
CleanExiHS_TSTA3.
ExpressionAtlasiQ13630. baseline and differential.
GenevisibleiQ13630. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00956. GDP_fucose_synth.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR028614. GDP_fucose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT.
    Tissue: Placenta.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Skin.
  5. "Primary structure of human erythrocyte nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein FX: identification with the mouse tum-transplantation antigen P35B."
    Camardella L., Carratore V., Ciardiello A., Damonte G., Benatti U., De Flora A.
    Blood 85:264-267(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Erythrocyte.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The crystal structure of human GDP-L-fucose synthase."
    Zhou H., Sun L., Li J., Xu C., Yu F., Liu Y., Ji C., He J.
    Acta Biochim. Biophys. Sin. 45:720-725(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.
  9. "Crystal structure of human GDP-L-fucose synthase with bound NADP."
    Structural genomics consortium (SGC)
    Submitted (APR-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 8-321 IN COMPLEXES WITH GDP AND NADP.

Entry informationi

Entry nameiFCL_HUMAN
AccessioniPrimary (citable) accession number: Q13630
Secondary accession number(s): B2R8Y7
, D3DWK5, Q567Q9, Q9UDG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 135 of the entry and version 1 of the sequence. [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, Multifunctional enzyme, 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

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.