FCL_DICDI
ID FCL_DICDI Reviewed; 320 AA.
AC Q55C77;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=GDP-L-fucose synthase {ECO:0000303|PubMed:19614564};
DE EC=1.1.1.271 {ECO:0000305|PubMed:19614564};
DE AltName: Full=FX protein {ECO:0000303|PubMed:19614564};
DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase {ECO:0000303|PubMed:19614564};
DE Short=GER {ECO:0000303|PubMed:19614564};
GN Name=ger; ORFNames=DDB_G0270184;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19614564; DOI=10.1042/bj20090786;
RA Schiller B., Hykollari A., Voglmeir J., Poltl G., Hummel K.,
RA Razzazi-Fazeli E., Geyer R., Wilson I.B.H.;
RT "Development of Dictyostelium discoideum is associated with alteration of
RT fucosylated N-glycan structures.";
RL Biochem. J. 423:41-52(2009).
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:0000305|PubMed:19614564}.
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:0000305|PubMed:19614564};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18887;
CC Evidence={ECO:0000305|PubMed:19614564};
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:0000305|PubMed:19614564}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Fucose synthase subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72442.1; -; Genomic_DNA.
DR RefSeq; XP_646604.1; XM_641512.1.
DR AlphaFoldDB; Q55C77; -.
DR SMR; Q55C77; -.
DR STRING; 44689.DDB0305155; -.
DR PaxDb; Q55C77; -.
DR EnsemblProtists; EAL72442; EAL72442; DDB_G0270184.
DR GeneID; 8617576; -.
DR KEGG; ddi:DDB_G0270184; -.
DR dictyBase; DDB_G0270184; ger.
DR eggNOG; KOG1431; Eukaryota.
DR HOGENOM; CLU_007383_18_2_1; -.
DR InParanoid; Q55C77; -.
DR OMA; IHCAGRV; -.
DR PhylomeDB; Q55C77; -.
DR Reactome; R-DDI-6787639; GDP-fucose biosynthesis.
DR UniPathway; UPA00128; UER00191.
DR PRO; PR:Q55C77; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IDA:dictyBase.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IDA:dictyBase.
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..320
FT /note="GDP-L-fucose synthase"
FT /id="PRO_0000383346"
FT ACT_SITE 142
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 14..20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 169..172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 113
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 115
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 146
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 320 AA; 36442 MW; DB9F7E616B915865 CRC64;
MTETTSKRTV LVTGGSGLVG KGIEKYVKET DKSNDVWVFM RSSDCDLKSR ESTRSYFEKI
KPTHVIHLAA RVGGLFSNMK YKVEFFRENI DINDNVLACC KEFNVVKCVS CLSTCIFPDK
TTYPIDETMI HNGPPHPSNE GYAYAKRMID VLNRAYNEEY GCKFTSVIPT NIYGPHDNYH
LTDGHVIPGL IHKTYLAMKN NQDLTIMGTG KPLRQFIYSY DLAKYFVWTL NNYEEMSPLI
LSVGEEDEIS IADVARLITE AMEFKGKLIF DTSKADGQYK KTASNLKLKS LVPDLTFTPI
QQAIKESCQW FIDNYETARK
