FCL_CAEEL
ID FCL_CAEEL Reviewed; 315 AA.
AC G5EER4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=GDP-L-fucose synthase {ECO:0000250|UniProtKB:Q13630};
DE EC=1.1.1.271 {ECO:0000269|PubMed:16650000};
DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase {ECO:0000312|EMBL:CAJ77755.1};
GN Name=ger-1 {ECO:0000312|WormBase:R01H2.5};
GN ORFNames=R01H2.5 {ECO:0000312|WormBase:R01H2.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:CAJ77755.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16650000; DOI=10.1111/j.1742-4658.2006.05239.x;
RA Rhomberg S., Fuchsluger C., Rendic D., Paschinger K., Jantsch V., Kosma P.,
RA Wilson I.B.H.;
RT "Reconstitution in vitro of the GDP-fucose biosynthetic pathways of
RT Caenorhabditis elegans and Drosophila melanogaster.";
RL FEBS J. 273:2244-2256(2006).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP-4-
CC dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a
CC reductase reaction. {ECO:0000269|PubMed:16650000}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose +
CC H(+) + NADPH; Xref=Rhea:RHEA:18885, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:57783, ChEBI:CHEBI:57964,
CC ChEBI:CHEBI:58349; EC=1.1.1.271;
CC Evidence={ECO:0000269|PubMed:16650000};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2.
CC {ECO:0000269|PubMed:16650000}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout larval development and in
CC adults. {ECO:0000269|PubMed:16650000}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Fucose synthase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM231686; CAJ77755.1; -; mRNA.
DR EMBL; BX284603; CCD69286.1; -; Genomic_DNA.
DR PIR; T16645; T16645.
DR RefSeq; NP_498540.1; NM_066139.4.
DR AlphaFoldDB; G5EER4; -.
DR SMR; G5EER4; -.
DR STRING; 6239.R01H2.5; -.
DR EPD; G5EER4; -.
DR PaxDb; G5EER4; -.
DR PeptideAtlas; G5EER4; -.
DR EnsemblMetazoa; R01H2.5.1; R01H2.5.1; WBGene00019813.
DR GeneID; 187512; -.
DR KEGG; cel:CELE_R01H2.5; -.
DR CTD; 187512; -.
DR WormBase; R01H2.5; CE00804; WBGene00019813; ger-1.
DR eggNOG; KOG1431; Eukaryota.
DR GeneTree; ENSGT00390000004681; -.
DR HOGENOM; CLU_007383_18_2_1; -.
DR InParanoid; G5EER4; -.
DR OMA; IHCAGRV; -.
DR OrthoDB; 922791at2759; -.
DR PhylomeDB; G5EER4; -.
DR BRENDA; 1.1.1.271; 1045.
DR Reactome; R-CEL-6787639; GDP-fucose biosynthesis.
DR UniPathway; UPA00128; UER00191.
DR PRO; PR:G5EER4; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019813; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IDA:WormBase.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042350; P:GDP-L-fucose biosynthetic process; IDA:WormBase.
DR CDD; cd05239; GDP_FS_SDR_e; 1.
DR HAMAP; MF_00956; GDP_fucose_synth; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR028614; GDP_fucose/colitose_synth.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Isomerase; Multifunctional enzyme; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..315
FT /note="GDP-L-fucose synthase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437079"
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32055"
FT BINDING 8..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 141
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 164..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13630"
FT SITE 108
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P32055"
FT SITE 110
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P32055"
FT SITE 141
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:P32055"
SQ SEQUENCE 315 AA; 35551 MW; 9AAB8E054C079079 CRC64;
MKTILVTGGT GLVGSAIKKV VETTEKRDDE KWVFIGSKDC DLENLEETRE LFESVKPTHV
IHLAAMVGGL FHNLAHNLQF FRKNMAINDN VLALCHEFDV IKCVSCLSTC IFPDKTSYPI
DETMVHLGPP HDSNFGYSYA KRMIDVLNKG YAQEHGRKYT SVVPCNVFGP HDNYNLQSGH
VLPALIHKAY VAQRDGTPLQ VYGSGTPLRQ FIYSIDLARL FIRVVREYED VEPIILSVNE
SDEVSIRDAV SAVVKAIDFT GDVEYDTSKA DGQFKKTASN EKLLKLFPDF QFTPFEQAIQ
ESVQWFVDNY ETARK
