ID   GLAK2_ARATH             Reviewed;         366 AA.
AC   Q9LY82; Q5PP60;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable glucuronokinase 2;
DE            EC=2.7.1.43;
GN   Name=GLCAK2; OrderedLocusNames=At5g14470; ORFNames=F18O22.260;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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] OF 8-366.
RA   Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION.
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).
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 (By
CC       similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Note=Magnesium. Can also use other divalent cations like manganese or
CC       cobalt. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV74231.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL163817; CAB87786.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92038.1; -; Genomic_DNA.
DR   EMBL; BT020237; AAV74231.1; ALT_INIT; mRNA.
DR   EMBL; BT020504; AAW39005.1; -; mRNA.
DR   PIR; T48620; T48620.
DR   RefSeq; NP_196951.3; NM_121451.5.
DR   AlphaFoldDB; Q9LY82; -.
DR   SMR; Q9LY82; -.
DR   STRING; 3702.AT5G14470.1; -.
DR   PaxDb; Q9LY82; -.
DR   PRIDE; Q9LY82; -.
DR   ProteomicsDB; 220771; -.
DR   DNASU; 831298; -.
DR   EnsemblPlants; AT5G14470.1; AT5G14470.1; AT5G14470.
DR   GeneID; 831298; -.
DR   Gramene; AT5G14470.1; AT5G14470.1; AT5G14470.
DR   KEGG; ath:AT5G14470; -.
DR   Araport; AT5G14470; -.
DR   TAIR; locus:2145723; AT5G14470.
DR   eggNOG; ENOG502QPXH; Eukaryota.
DR   HOGENOM; CLU_050132_0_0_1; -.
DR   InParanoid; Q9LY82; -.
DR   OMA; VFEHRSF; -.
DR   OrthoDB; 793044at2759; -.
DR   PhylomeDB; Q9LY82; -.
DR   BRENDA; 2.7.1.43; 399.
DR   PRO; PR:Q9LY82; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LY82; baseline and differential.
DR   Genevisible; Q9LY82; 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; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004496; F:mevalonate kinase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
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; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Carbohydrate metabolism; Cobalt; Kinase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..366
FT                   /note="Probable glucuronokinase 2"
FT                   /id="PRO_0000407402"
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   366 AA;  40861 MW;  8A1FE48F165B0D15 CRC64;
     MDPNPKPAIS GKDNGVFEHR SFARIGFLGN PSDVYFGRTI SFTIGNFWAW AKLEPSDHLL
     IKPHPFHDLV QFDSLDNLVY RLENDGYYGG VRLLMAICKV FRNYCKENGI QLHDKNFTLS
     YDTNIPRQTG LSGSSAIVSA ALSCLLDFYN VRQSIRIEVR PNLILNAEKE LGIVAGLQDR
     VAQVYGGGLV HMDFSKEHMD KVGYGIYTIM DINLLPPLHL IYAENPSDSG KVHSTVRRRW
     LDGDEFIISS MAEIAKLAEE GRTALLKKDY SNLKELMNRN FDLRRSMFGD ECLGAMNIEM
     VEVARKIGAA AKFTGSGGAV VVFCPEGPSQ VKLLEEECRK SGFIVEPVKL VPTRLSSSDI
     KTLSKT