FCL1_ARATH
ID FCL1_ARATH Reviewed; 323 AA.
AC O49213; Q0WQ67;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=GDP-L-fucose synthase 1;
DE EC=1.1.1.271 {ECO:0000269|PubMed:10758496};
DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase 1;
DE Short=AtFX;
DE Short=AtGER1;
GN Name=GER1; Synonyms=FX; OrderedLocusNames=At1g73250; ORFNames=T18K17.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-323, TISSUE SPECIFICITY, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=10758496; DOI=10.1046/j.1365-313x.2000.00698.x;
RA Bonin C.P., Reiter W.-D.;
RT "A bifunctional epimerase-reductase acts downstream of the MUR1 gene
RT product and completes the de novo synthesis of GDP-L-fucose in
RT Arabidopsis.";
RL Plant J. 21:445-454(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-323, AND INTERACTION WITH MUR1.
RX PubMed=12881408; DOI=10.1093/glycob/cwg099;
RA Nakayama K., Maeda Y., Jigami Y.;
RT "Interaction of GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase with
RT GDP-mannose-4,6-dehydratase stabilizes the enzyme activity for formation of
RT GDP-fucose from GDP-mannose.";
RL Glycobiology 13:673-680(2003).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. Not involved in the synthesis of GDP-L-galactose
CC from GDP-D-manose. {ECO:0000269|PubMed:10758496}.
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:10758496};
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 -!- SUBUNIT: Binds and stabilizes MUR1. Homodimer (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and flowers, less
CC abundant in leaves, stems and siliques. {ECO:0000269|PubMed:10758496}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Fucose synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52124.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC010556; AAG52124.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35434.1; -; Genomic_DNA.
DR EMBL; AK228837; BAF00732.1; -; mRNA.
DR EMBL; BT029480; ABL66737.1; -; mRNA.
DR EMBL; AF045286; AAC02703.2; -; Genomic_DNA.
DR EMBL; AB034806; BAA95670.1; -; mRNA.
DR PIR; F96758; F96758.
DR RefSeq; NP_177468.2; NM_105984.4.
DR AlphaFoldDB; O49213; -.
DR SMR; O49213; -.
DR BioGRID; 28878; 1.
DR STRING; 3702.AT1G73250.1; -.
DR iPTMnet; O49213; -.
DR PaxDb; O49213; -.
DR PRIDE; O49213; -.
DR ProteomicsDB; 230834; -.
DR EnsemblPlants; AT1G73250.1; AT1G73250.1; AT1G73250.
DR GeneID; 843659; -.
DR Gramene; AT1G73250.1; AT1G73250.1; AT1G73250.
DR KEGG; ath:AT1G73250; -.
DR Araport; AT1G73250; -.
DR TAIR; locus:2197264; AT1G73250.
DR eggNOG; KOG1431; Eukaryota.
DR HOGENOM; CLU_007383_18_0_1; -.
DR InParanoid; O49213; -.
DR OMA; EQWIFIS; -.
DR OrthoDB; 922791at2759; -.
DR BioCyc; ARA:AT1G73250-MON; -.
DR BioCyc; MetaCyc:AT1G73250-MON; -.
DR BRENDA; 1.1.1.271; 399.
DR UniPathway; UPA00128; UER00191.
DR PRO; PR:O49213; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O49213; baseline and differential.
DR Genevisible; O49213; AT.
DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IDA:TAIR.
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:0006005; P:L-fucose biosynthetic process; IDA:TAIR.
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 Acetylation; Isomerase; Multifunctional enzyme; NADP; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..323
FT /note="GDP-L-fucose synthase 1"
FT /id="PRO_0000174354"
FT ACT_SITE 149
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 23..29
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 176..179
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 120
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 122
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 153
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 323 AA; 35570 MW; AE0A882CF19B5FEE CRC64;
MAETIGSEVS SMSDKSAKIF VAGHRGLVGS AIVRKLQEQG FTNLVLKTHA ELDLTRQADV
ESFFSQEKPV YVILAAAKVG GIHANNTYPA DFIGVNLQIQ TNVIHSAYEH GVKKLLFLGS
SCIYPKFAPQ PIPESALLTA SLEPTNEWYA IAKIAGIKTC QAYRIQHGWD AISGMPTNLY
GPNDNFHPEN SHVLPALMRR FHEAKVNGAE EVVVWGTGSP LREFLHVDDL ADACVFLLDR
YSGLEHVNIG SGQEVTIREL AELVKEVVGF EGKLGWDCTK PDGTPRKLMD SSKLASLGWT
PKVSLRDGLS QTYDWYLKNV CNR
