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Q13630

- FCL_HUMAN

UniProt

Q13630 - FCL_HUMAN

Protein

GDP-L-fucose synthase

Gene

TSTA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.

    Pathwayi

    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

    1. coenzyme binding Source: InterPro
    2. electron carrier activity Source: UniProtKB
    3. GDP-4-dehydro-D-rhamnose reductase activity Source: UniProtKB
    4. GDP-L-fucose synthase activity Source: UniProtKB
    5. isomerase activity Source: UniProtKB-KW

    GO - Biological processi

    1. 'de novo' GDP-L-fucose biosynthetic process Source: UniProtKB
    2. cytolysis Source: Ensembl
    3. GDP-mannose metabolic process Source: UniProtKB
    4. leukocyte cell-cell adhesion Source: UniProtKB

    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: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:12390. TSTA3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37056.

    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

    ArrayExpressiQ13630.
    BgeeiQ13630.
    CleanExiHS_TSTA3.
    GenevestigatoriQ13630.

    Organism-specific databases

    HPAiHPA023361.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi113115. 14 interactions.
    IntActiQ13630. 2 interactions.
    STRINGi9606.ENSP00000353243.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000168011.
    HOVERGENiHBG000059.
    InParanoidiQ13630.
    KOiK02377.
    OMAiIRETCEW.
    PhylomeDBiQ13630.
    TreeFamiTF314936.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00956. GDP_fucose_synth.
    InterProiIPR001509. Epimerase_deHydtase.
    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

    MGEPQGSMRI LVTGGSGLVG KAIQKVVADG AGLPGEDWVF VSSKDADLTD    50
    TAQTRALFEK VQPTHVIHLA AMVGGLFRNI KYNLDFWRKN VHMNDNVLHS 100
    AFEVGARKVV SCLSTCIFPD KTTYPIDETM IHNGPPHNSN FGYSYAKRMI 150
    DVQNRAYFQQ YGCTFTAVIP TNVFGPHDNF NIEDGHVLPG LIHKVHLAKS 200
    SGSALTVWGT GNPRRQFIYS LDLAQLFIWV LREYNEVEPI ILSVGEEDEV 250
    SIKEAAEAVV EAMDFHGEVT FDTTKSDGQF KKTASNSKLR TYLPDFRFTP 300
    FKQAVKETCA WFTDNYEQAR K 321
    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:
    EMBL
    GenBank
    DDBJ
    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.
    UniGeneiHs.404119.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi13124123.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6408.1.
    RefSeqi NP_003304.1. NM_003313.3.
    UniGenei Hs.404119.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4B8W X-ray 2.75 A/B 7-320 [» ]
    4B8Z X-ray 2.75 A/B/C/D 8-320 [» ]
    4BKP X-ray 2.70 A/B/C/D 8-321 [» ]
    4BL5 X-ray 2.60 A/B/C/D/E/F/G/H/I/J/K/L 8-321 [» ]
    4E5Y X-ray 2.37 A/B/C/D 1-321 [» ]
    ProteinModelPortali Q13630.
    SMRi Q13630. Positions 4-321.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113115. 14 interactions.
    IntActi Q13630. 2 interactions.
    STRINGi 9606.ENSP00000353243.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei Q13630.

    Polymorphism databases

    DMDMi 13124123.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00014361.

    Proteomic databases

    MaxQBi Q13630.
    PaxDbi Q13630.
    PeptideAtlasi Q13630.
    PRIDEi Q13630.

    Protocols and materials databases

    DNASUi 7264.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000425753 ; ENSP00000398803 ; ENSG00000104522 .
    ENST00000529064 ; ENSP00000435386 ; ENSG00000104522 .
    GeneIDi 7264.
    KEGGi hsa:7264.
    UCSCi uc003yza.2. human.

    Organism-specific databases

    CTDi 7264.
    GeneCardsi GC08M144694.
    HGNCi HGNC:12390. TSTA3.
    HPAi HPA023361.
    MIMi 137020. gene.
    neXtProti NX_Q13630.
    PharmGKBi PA37056.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0451.
    HOGENOMi HOG000168011.
    HOVERGENi HBG000059.
    InParanoidi Q13630.
    KOi K02377.
    OMAi IRETCEW.
    PhylomeDBi Q13630.
    TreeFami TF314936.

    Enzyme and pathway databases

    UniPathwayi UPA00128 ; UER00191 .

    Miscellaneous databases

    GeneWikii TSTA3.
    GenomeRNAii 7264.
    NextBioi 28399.
    PROi Q13630.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13630.
    Bgeei Q13630.
    CleanExi HS_TSTA3.
    Genevestigatori Q13630.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00956. GDP_fucose_synth.
    InterProi IPR001509. Epimerase_deHydtase.
    IPR028614. GDP_fucose_synth.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF01370. Epimerase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.

    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: October 1, 2014
    This is version 128 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