GLAK1_ARATH
ID GLAK1_ARATH Reviewed; 362 AA.
AC Q93ZC9; Q9SS91;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glucuronokinase 1;
DE Short=AtGlcAK1;
DE EC=2.7.1.43;
GN Name=GLCAK1; OrderedLocusNames=At3g01640; ORFNames=F4P13.18;
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, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=19951951; DOI=10.1074/jbc.m109.069369;
RA Pieslinger A.M., Hoepflinger M.C., Tenhaken R.;
RT "Cloning of Glucuronokinase from Arabidopsis thaliana, the last missing
RT enzyme of the myo-inositol oxygenase pathway to nucleotide sugars.";
RL J. Biol. Chem. 285:2902-2910(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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).
RN [4]
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).
CC -!- FUNCTION: Sugar-1-kinase with a strict substrate specificity for D-
CC glucuronic acid and ATP. Involved in the biosynthesis of UDP-glucuronic
CC acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers.
CC May be also involved in a salvage pathway for glucuronic acid.
CC {ECO:0000269|PubMed:19951951}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucuronate = 1-phospho-alpha-D-glucuronate + ADP +
CC H(+); Xref=Rhea:RHEA:17005, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57897, ChEBI:CHEBI:58720, ChEBI:CHEBI:456216;
CC EC=2.7.1.43; Evidence={ECO:0000269|PubMed:19951951};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19951951};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19951951};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:19951951};
CC Note=Magnesium. Can also use other divalent cations like manganese or
CC cobalt. {ECO:0000269|PubMed:19951951};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=697 uM for D-glucuronic acid {ECO:0000269|PubMed:19951951};
CC KM=555 uM for ATP {ECO:0000269|PubMed:19951951};
CC Vmax=12.2 nmol/min/ug enzyme toward D-glucuronic acid
CC {ECO:0000269|PubMed:19951951};
CC Vmax=12.6 nmol/min/ug enzyme toward ATP
CC {ECO:0000269|PubMed:19951951};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:19951951};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:19951951};
CC -!- TISSUE SPECIFICITY: Highly expressed in pollen. Detected in seedlings,
CC inflorescences, seeds, leaves and roots. {ECO:0000269|PubMed:19951951}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01548.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GU599900; ADD92391.1; -; mRNA.
DR EMBL; AC009325; AAF01548.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73698.1; -; Genomic_DNA.
DR EMBL; AY057630; AAL15261.1; -; mRNA.
DR EMBL; AY141995; AAM98259.1; -; mRNA.
DR RefSeq; NP_566144.2; NM_111030.3.
DR AlphaFoldDB; Q93ZC9; -.
DR SMR; Q93ZC9; -.
DR STRING; 3702.AT3G01640.1; -.
DR PaxDb; Q93ZC9; -.
DR PRIDE; Q93ZC9; -.
DR ProteomicsDB; 220770; -.
DR DNASU; 819902; -.
DR EnsemblPlants; AT3G01640.1; AT3G01640.1; AT3G01640.
DR GeneID; 819902; -.
DR Gramene; AT3G01640.1; AT3G01640.1; AT3G01640.
DR KEGG; ath:AT3G01640; -.
DR Araport; AT3G01640; -.
DR TAIR; locus:2084208; AT3G01640.
DR eggNOG; ENOG502QPXH; Eukaryota.
DR HOGENOM; CLU_050132_0_0_1; -.
DR InParanoid; Q93ZC9; -.
DR PhylomeDB; Q93ZC9; -.
DR BioCyc; MetaCyc:AT3G01640-MON; -.
DR BRENDA; 2.7.1.43; 399.
DR SABIO-RK; Q93ZC9; -.
DR PRO; PR:Q93ZC9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93ZC9; baseline and differential.
DR Genevisible; Q93ZC9; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047940; F:glucuronokinase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004496; F:mevalonate kinase activity; IEA:InterPro.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:TAIR.
DR GO; GO:0042546; P:cell wall biogenesis; TAS:TAIR.
DR GO; GO:0006020; P:inositol metabolic process; TAS:TAIR.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048868; P:pollen tube development; TAS:TAIR.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006205; Mev_gal_kin.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR43290; PTHR43290; 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; Cobalt; Kinase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..362
FT /note="Glucuronokinase 1"
FT /id="PRO_0000407401"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 126..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 24
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 40076 MW; 15B43C18D48262E6 CRC64;
MDPNSTVSGD GQATAAIEHR SFARIGFLGN PSDVYFGRTI SLTIGNFWAS VKLEPSEHLV
IKPHPFHDLV QFTSLDHLLN RLQNEGYYGG VRLLMAICKV FRNYCKENDI QLHQANFSLS
YDTNIPRQTG LSGSSAIVSA ALNCLLDFYN VRHLIKVQVR PNIVLSAEKE LGIVAGLQDR
VAQVYGGLVH MDFSKEHMDK LGHGIYTPMD ISLLPPLHLI YAENPSDSGK VHSMVRQRWL
DGDEFIISSM KEVGSLAEEG RTALLNKDHS KLVELMNLNF DIRRRMFGDE CLGAMNIEMV
EVARRVGAAS KFTGSGGAVV VFCPEGPSQV KLLEEECRKA GFTLQPVKIA PSCLNDSDIQ
TL
