FCL2_ARATH
ID FCL2_ARATH Reviewed; 328 AA.
AC Q9LMU0; Q3EDA2; Q3EDA3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Putative GDP-L-fucose synthase 2;
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 2;
DE Short=AtGER2;
GN Name=GER2; OrderedLocusNames=At1g17890; ORFNames=F2H15.12;
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [5]
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. {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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LMU0-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Fucose synthase subfamily. {ECO:0000305}.
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DR EMBL; AC034106; AAF97269.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29650.1; -; Genomic_DNA.
DR EMBL; AY063880; AAL36236.1; -; mRNA.
DR EMBL; AY096364; AAM20005.1; -; mRNA.
DR PIR; B86314; B86314.
DR RefSeq; NP_564040.1; NM_101652.3. [Q9LMU0-1]
DR AlphaFoldDB; Q9LMU0; -.
DR SMR; Q9LMU0; -.
DR BioGRID; 23607; 2.
DR STRING; 3702.AT1G17890.1; -.
DR iPTMnet; Q9LMU0; -.
DR PaxDb; Q9LMU0; -.
DR PRIDE; Q9LMU0; -.
DR ProteomicsDB; 222519; -. [Q9LMU0-1]
DR EnsemblPlants; AT1G17890.1; AT1G17890.1; AT1G17890. [Q9LMU0-1]
DR GeneID; 838368; -.
DR Gramene; AT1G17890.1; AT1G17890.1; AT1G17890. [Q9LMU0-1]
DR KEGG; ath:AT1G17890; -.
DR Araport; AT1G17890; -.
DR TAIR; locus:2030973; AT1G17890.
DR eggNOG; KOG1431; Eukaryota.
DR InParanoid; Q9LMU0; -.
DR OMA; LMACNEF; -.
DR OrthoDB; 922791at2759; -.
DR PhylomeDB; Q9LMU0; -.
DR BRENDA; 1.1.1.271; 399.
DR UniPathway; UPA00128; UER00191.
DR PRO; PR:Q9LMU0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMU0; baseline and differential.
DR Genevisible; Q9LMU0; AT.
DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IBA:GO_Central.
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 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; Alternative splicing; Isomerase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..328
FT /note="Putative GDP-L-fucose synthase 2"
FT /id="PRO_0000174355"
FT ACT_SITE 152
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 26..32
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 179..182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 123
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 125
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 156
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 328 AA; 36227 MW; 31C4449E9C5B1AC6 CRC64;
MADNTGSEMK SGSFMLEKSA KIFVAGHRGL VGSAIVRKLQ DQGFTNLVLR THSELDLTSQ
SDVESFFATE KPVYVILAAA KVGGIHANNT YPADFIGVNL QIQTNVIHSA YTHGVKKLLF
LGSSCIYPKF APQPIPESAL LTGPLEPTNE WYAIAKIAGI KMCQAYRLQH QWDAISGMPT
NLYGQNDNFH PENSHVLPAL MRRFHEAKAN NADEVVVWGS GSPLREFLHV DDLADACVFL
MDQYSGFEHV NVGSGVEVTI KELAELVKEV VGFKGKLVWD TTKPDGTPRK LMDSSKLASL
GWTPKISLKD GLSQTYEWYL ENVVQKKQ
