ID FCL_SINFN Reviewed; 314 AA. AC P55353; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=GDP-L-fucose synthase {ECO:0000255|HAMAP-Rule:MF_00956}; DE EC=1.1.1.271 {ECO:0000255|HAMAP-Rule:MF_00956}; DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase {ECO:0000255|HAMAP-Rule:MF_00956}; GN Name=fcl {ECO:0000255|HAMAP-Rule:MF_00956}; GN OrderedLocusNames=NGR_a00420; ORFNames=y4aF; OS Sinorhizobium fredii (strain NBRC 101917 / NGR234). OG Plasmid sym pNGR234a. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101917 / NGR234; RX PubMed=9163424; DOI=10.1038/387394a0; RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A., RA Perret X.; RT "Molecular basis of symbiosis between Rhizobium and legumes."; RL Nature 387:394-401(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101917 / NGR234; RX PubMed=19376903; DOI=10.1128/aem.00515-09; RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A., RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.; RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion RT systems."; RL Appl. Environ. Microbiol. 75:4035-4045(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:0000255|HAMAP-Rule:MF_00956}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00956}; 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:0000255|HAMAP-Rule:MF_00956}. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. Fucose synthase subfamily. {ECO:0000255|HAMAP-Rule:MF_00956}. 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; U00090; AAB91603.1; -; Genomic_DNA. DR RefSeq; NP_443765.1; NC_000914.2. DR AlphaFoldDB; P55353; -. DR SMR; P55353; -. DR KEGG; rhi:NGR_a00420; -. DR PATRIC; fig|394.7.peg.39; -. DR eggNOG; COG0451; Bacteria. DR HOGENOM; CLU_007383_18_0_5; -. DR OrthoDB; 9811425at2; -. DR UniPathway; UPA00128; UER00191. DR Proteomes; UP000001054; Plasmid sym pNGR234a. DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule. DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd05239; GDP_FS_SDR_e; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 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 PANTHER; PTHR43238; GDP-L-FUCOSE SYNTHASE; 1. DR PANTHER; PTHR43238:SF1; GDP-L-FUCOSE SYNTHASE; 1. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW Isomerase; Multifunctional enzyme; NADP; Nodulation; Oxidoreductase; KW Plasmid; Reference proteome. FT CHAIN 1..314 FT /note="GDP-L-fucose synthase" FT /id="PRO_0000174360" FT ACT_SITE 140 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT BINDING 15..21 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT BINDING 109..112 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT BINDING 144 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT BINDING 167..170 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT BINDING 183 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT BINDING 206 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT BINDING 213 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT BINDING 273 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT SITE 111 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" FT SITE 113 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00956" SQ SEQUENCE 314 AA; 34674 MW; 2E571D298AA98110 CRC64; MPMYLLDGKR IWVAGHKGMV GSAIIRSLAS EDCEVIVADR QKLDLTRQEE VEKFLLKEKP HAVIMAAAKV GGILANDTMP ADFIYQNLIM EANVIEGSFR SGVEKLLFLG SSCIYPKYAA QPIREEALLT GPLEPTNEWY AIAKIAGIKL CQAYRKQYGA NFISAMPTNL YGPRDKFDLN SSHVVPALIR KAHEAKIKDL GCLSIWGSGT PTRDFLYSED CSDALVFLLK HYSETEHINI GSGGEISIIE LAHIVCRVVG FKGDIVFDTS KPDGTPRKLL SSERLVSMGW RPKTSLELGL AKSYESFVSN VADN //