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Q13630 (FCL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TSTA3
Synonyms:SDR4E1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

GDP-beta-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-alpha-D-mannose + NADPH. HAMAP-Rule MF_00956

Pathway

Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2. HAMAP-Rule MF_00956

Subunit structure

Homodimer. Ref.1 Ref.7

Sequence similarities

Belongs to the NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 321321GDP-L-fucose synthase HAMAP-Rule MF_00956
PRO_0000174350

Regions

Nucleotide binding14 – 207NADP HAMAP-Rule MF_00956
Nucleotide binding170 – 1734NADP HAMAP-Rule MF_00956

Sites

Active site1431Proton donor/acceptor By similarity
Binding site1471NADP
Binding site1861NADP
Binding site1941Substrate
Binding site2081Substrate
Binding site2151Substrate
Binding site2771Substrate
Site1141Important for catalytic activity By similarity
Site1161Important for catalytic activity By similarity
Site1471Lowers pKa of active site Tyr By similarity

Experimental info

Sequence conflict51Q → E AA sequence Ref.5

Secondary structure

............................................................. 321
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13630 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 94BB1FF61658007C

FASTA32135,893
        10         20         30         40         50         60 
MGEPQGSMRI LVTGGSGLVG KAIQKVVADG AGLPGEDWVF VSSKDADLTD TAQTRALFEK 

        70         80         90        100        110        120 
VQPTHVIHLA AMVGGLFRNI KYNLDFWRKN VHMNDNVLHS AFEVGARKVV SCLSTCIFPD 

       130        140        150        160        170        180 
KTTYPIDETM IHNGPPHNSN FGYSYAKRMI DVQNRAYFQQ YGCTFTAVIP TNVFGPHDNF 

       190        200        210        220        230        240 
NIEDGHVLPG LIHKVHLAKS SGSALTVWGT GNPRRQFIYS LDLAQLFIWV LREYNEVEPI 

       250        260        270        280        290        300 
ILSVGEEDEV SIKEAAEAVV EAMDFHGEVT FDTTKSDGQF KKTASNSKLR TYLPDFRFTP 

       310        320 
FKQAVKETCA WFTDNYEQAR K 

« Hide

References

« Hide 'large scale' references
[1]"Synthesis of GDP-L-fucose by the human FX protein."
Tonetti M., Sturla L., Bisso A., Benatti U., De Flora A.
J. Biol. Chem. 271:27274-27279(1996) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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.
[8]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_003304.1. NM_003313.3.
UniGeneHs.404119.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4B8WX-ray2.75A/B7-320[»]
4B8ZX-ray2.75A/B/C/D7-320[»]
4BKPX-ray2.70A/B/C/D7-321[»]
4E5YX-ray2.37A/B/C/D1-321[»]
ProteinModelPortalQ13630.
SMRQ13630. Positions 4-321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113115. 14 interactions.
IntActQ13630. 2 interactions.
STRING9606.ENSP00000353243.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteQ13630.

Polymorphism databases

DMDM13124123.

2D gel databases

REPRODUCTION-2DPAGEIPI00014361.

Proteomic databases

PaxDbQ13630.
PeptideAtlasQ13630.
PRIDEQ13630.

Protocols and materials databases

DNASU7264.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000425753; ENSP00000398803; ENSG00000104522.
ENST00000529064; ENSP00000435386; ENSG00000104522.
GeneID7264.
KEGGhsa:7264.
UCSCuc003yza.2. human.

Organism-specific databases

CTD7264.
GeneCardsGC08M144694.
HGNCHGNC:12390. TSTA3.
HPAHPA023361.
MIM137020. gene.
neXtProtNX_Q13630.
PharmGKBPA37056.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0451.
HOGENOMHOG000168011.
HOVERGENHBG000059.
InParanoidQ13630.
KOK02377.
OMAIHCAGRV.
PhylomeDBQ13630.
TreeFamTF314936.

Enzyme and pathway databases

UniPathwayUPA00128; UER00191.

Gene expression databases

ArrayExpressQ13630.
BgeeQ13630.
CleanExHS_TSTA3.
GenevestigatorQ13630.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00956. GDP_fucose_synth.
InterProIPR001509. Epimerase_deHydtase.
IPR028614. GDP_fucose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTSTA3.
GenomeRNAi7264.
NextBio28399.
PROQ13630.
SOURCESearch...

Entry information

Entry nameFCL_HUMAN
AccessionPrimary (citable) accession number: Q13630
Secondary accession number(s): B2R8Y7 expand/collapse secondary AC list , D3DWK5, Q567Q9, Q9UDG7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM