FKGP_ARATH
ID FKGP_ARATH Reviewed; 1055 AA.
AC Q9LNJ9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Bifunctional fucokinase/fucose pyrophosphorylase;
DE Short=AtFKGP;
DE Includes:
DE RecName: Full=L-fucokinase;
DE EC=2.7.1.52;
DE Includes:
DE RecName: Full=Fucose-1-phosphate guanylyltransferase;
DE EC=2.7.7.30;
DE AltName: Full=GDP-fucose pyrophosphorylase;
GN Name=FKGP; OrderedLocusNames=At1g01220; ORFNames=F6F3.3;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF
RP GLY-133 AND GLY-830, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18199744; DOI=10.1074/jbc.m710078200;
RA Kotake T., Hojo S., Tajima N., Matsuoka K., Koyama T., Tsumuraya Y.;
RT "A bifunctional enzyme with L-fucokinase and GDP-L-fucose pyrophosphorylase
RT activities salvages free L-fucose in Arabidopsis.";
RL J. Biol. Chem. 283:8125-8135(2008).
RN [2]
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 [3]
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).
CC -!- FUNCTION: Bifunctional enzyme involved in the salvage pathway which
CC converts free L-fucose to GDP-L-fucose. The sugar-1-kinase activity has
CC a strict substrate specificity for L-fucose and ATP. The
CC pyrophosphorylase activity has a strict substrate specificity for L-
CC fucose 1-phosphate and GTP. {ECO:0000269|PubMed:18199744}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-fucose = ADP + beta-L-fucose 1-phosphate + H(+);
CC Xref=Rhea:RHEA:13241, ChEBI:CHEBI:2181, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57268, ChEBI:CHEBI:456216;
CC EC=2.7.1.52; Evidence={ECO:0000269|PubMed:18199744};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-L-fucose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC beta-L-fucose; Xref=Rhea:RHEA:13549, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57268,
CC ChEBI:CHEBI:57273; EC=2.7.7.30;
CC Evidence={ECO:0000269|PubMed:18199744};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18199744};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18199744};
CC Note=Divalent metal cations. Mn(2+) is better for the L-fucokinase
CC activity, while Mg(2+) is preferred for the GDP-fucose
CC pyrophosphorylase activity. {ECO:0000269|PubMed:18199744};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for L-fucose for the L-fucokinase activity
CC {ECO:0000269|PubMed:18199744};
CC KM=0.45 mM for ATPfor the L-fucokinase activity
CC {ECO:0000269|PubMed:18199744};
CC KM=0.052 mM for L-fucose 1-phosphate for the GDP-fucose
CC pyrophosphorylase activity in the forward reaction
CC {ECO:0000269|PubMed:18199744};
CC KM=0.17 mM for GTP for the GDP-fucose pyrophosphorylase activity in
CC the forward reaction {ECO:0000269|PubMed:18199744};
CC KM=0.40 mM for GDP-L-fucose for the GDP-fucose pyrophosphorylase
CC activity in the reverse reaction {ECO:0000269|PubMed:18199744};
CC KM=0.18 mM for diphosphate for the GDP-fucose pyrophosphorylase
CC activity in the reverse reaction {ECO:0000269|PubMed:18199744};
CC pH dependence:
CC Optimum pH is 10.5 for the L-fucokinase activity and 6.5-8 for the
CC GDP-fucose pyrophosphorylase activity. {ECO:0000269|PubMed:18199744};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius for the L-fucokinase
CC activity and 30-45 degrees Celsius for the GDP-fucose
CC pyrophosphorylase activity. {ECO:0000269|PubMed:18199744};
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in flower buds.
CC {ECO:0000269|PubMed:18199744}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and no alteration of the
CC sugar composition of cell wall polysaccharides, but accumulation of
CC free L-fucose. {ECO:0000269|PubMed:18199744}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97333.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC023628; AAF97333.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27255.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58557.1; -; Genomic_DNA.
DR PIR; D86142; D86142.
DR RefSeq; NP_001320982.1; NM_001331261.1.
DR RefSeq; NP_563620.1; NM_100004.4.
DR AlphaFoldDB; Q9LNJ9; -.
DR STRING; 3702.AT1G01220.1; -.
DR PaxDb; Q9LNJ9; -.
DR PRIDE; Q9LNJ9; -.
DR ProteomicsDB; 228929; -.
DR EnsemblPlants; AT1G01220.1; AT1G01220.1; AT1G01220.
DR EnsemblPlants; AT1G01220.7; AT1G01220.7; AT1G01220.
DR GeneID; 839420; -.
DR Gramene; AT1G01220.1; AT1G01220.1; AT1G01220.
DR Gramene; AT1G01220.7; AT1G01220.7; AT1G01220.
DR KEGG; ath:AT1G01220; -.
DR Araport; AT1G01220; -.
DR TAIR; locus:2035362; AT1G01220.
DR eggNOG; KOG4644; Eukaryota.
DR HOGENOM; CLU_006983_1_1_1; -.
DR InParanoid; Q9LNJ9; -.
DR OMA; QRWREAW; -.
DR OrthoDB; 135001at2759; -.
DR PRO; PR:Q9LNJ9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNJ9; baseline and differential.
DR Genevisible; Q9LNJ9; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050201; F:fucokinase activity; IDA:TAIR.
DR GO; GO:0047341; F:fucose-1-phosphate guanylyltransferase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042352; P:GDP-L-fucose salvage; IDA:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR012887; Fucokinase.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR Pfam; PF07959; Fucokinase; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Kinase; Magnesium; Manganese;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..1055
FT /note="Bifunctional fucokinase/fucose pyrophosphorylase"
FT /id="PRO_0000407405"
FT REGION 34..565
FT /note="GDP-fucose pyrophosphorylase"
FT REGION 693..1055
FT /note="L-fucokinase"
FT BINDING 826..836
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 133
FT /note="G->A: Loss of GDP-fucose pyrophosphorylase activity,
FT but no effect on L-fucokinase activity. Total loss of both
FT activities; when associated with A-830."
FT /evidence="ECO:0000269|PubMed:18199744"
FT MUTAGEN 830
FT /note="G->A: 90% reduction of the L-fucokinase activity,
FT but no effect on the GDP-fucose pyrophosphorylase activity.
FT Total loss of both activities; when associated with A-133."
FT /evidence="ECO:0000269|PubMed:18199744"
SQ SEQUENCE 1055 AA; 116351 MW; B37F9B75A881FD55 CRC64;
MSKQRKKADL ATVLRKSWYH LRLSVRHPTR VPTWDAIVLT AASPEQAELY DWQLRRAKRM
GRIASSTVTL AVPDPDGKRI GSGAATLNAI YALARHYEKL GFDLGPEMEV ANGACKWVRF
ISAKHVLMLH AGGDSKRVPW ANPMGKVFLP LPYLAADDPD GPVPLLFDHI LAIASCARQA
FQDQGGLFIM TGDVLPCFDA FKMTLPEDAA SIVTVPITLD IASNHGVIVT SKSESLAESY
TVSLVNDLLQ KPTVEDLVKK DAILHDGRTL LDTGIISARG RAWSDLVALG CSCQPMILEL
IGSKKEMSLY EDLVAAWVPS RHDWLRTRPL GELLVNSLGR QKMYSYCTYD LQFLHFGTSS
EVLDHLSGDA SGIVGRRHLC SIPATTVSDI AASSVILSSE IAPGVSIGED SLIYDSTVSG
AVQIGSQSIV VGIHIPSEDL GTPESFRFML PDRHCLWEVP LVGHKGRVIV YCGLHDNPKN
SIHKDGTFCG KPLEKVLFDL GIEESDLWSS YVAQDRCLWN AKLFPILTYS EMLKLASWLM
GLDDSRNKEK IKLWRSSQRV SLEELHGSIN FPEMCNGSSN HQADLAGGIA KACMNYGMLG
RNLSQLCHEI LQKESLGLEI CKNFLDQCPK FQEQNSKILP KSRAYQVEVD LLRACGDEAK
AIELEHKVWG AVAEETASAV RYGFREHLLE SSGKSHSENH ISHPDRVFQP RRTKVELPVR
VDFVGGWSDT PPWSLERAGY VLNMAITLEG SLPIGTIIET TNQMGISIQD DAGNELHIED
PISIKTPFEV NDPFRLVKSA LLVTGIVQEN FVDSTGLAIK TWANVPRGSG LGTSSILAAA
VVKGLLQISN GDESNENIAR LVLVLEQLMG TGGGWQDQIG GLYPGIKFTS SFPGIPMRLQ
VVPLLASPQL ISELEQRLLV VFTGQVRLAH QVLHKVVTRY LQRDNLLISS IKRLTELAKS
GREALMNCEV DEVGDIMSEA WRLHQELDPY CSNEFVDKLF EFSQPYSSGF KLVGAGGGGF
SLILAKDAEK AKELRQRLEE HAEFDVKVYN WSICI
