GALAK_ARATH
ID GALAK_ARATH Reviewed; 424 AA.
AC Q8VYG2; Q9CAF7; Q9SG76;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Galacturonokinase;
DE EC=2.7.1.44;
DE AltName: Full=D-galacturonic acid-1-P kinase;
GN Name=GALAK; OrderedLocusNames=At3g10700; ORFNames=F13M14.1 T7M13.22;
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 ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-41;
RP TYR-250 AND ALA-368, AND TISSUE SPECIFICITY.
RX PubMed=19509290; DOI=10.1074/jbc.m109.014761;
RA Yang T., Bar-Peled L., Gebhart L., Lee S.G., Bar-Peled M.;
RT "Identification of galacturonic acid-1-phosphate kinase, a new member of
RT the GHMP kinase superfamily in plants, and comparison with galactose-1-
RT phosphate kinase.";
RL J. Biol. Chem. 284:21526-21535(2009).
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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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: Sugar-1-kinase with a strict substrate specificity for the
CC alpha-anomeric configuration of D-galacturonic acid (D-GalA) and ATP.
CC Involved in the biosynthesis of UDP-galacturonic acid (UDP-GalA) from
CC the salvaged GalA that is released during growth-dependent cell wall
CC restructuring. {ECO:0000269|PubMed:19509290}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-galacturonate = 1-phospho-alpha-D-galacturonate + ADP
CC + H(+); Xref=Rhea:RHEA:12965, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58186, ChEBI:CHEBI:75525, ChEBI:CHEBI:456216;
CC EC=2.7.1.44; Evidence={ECO:0000269|PubMed:19509290};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19509290};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19509290};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:19509290};
CC Note=Magnesium. Can also use other divalent cations like manganese or
CC calcium. {ECO:0000269|PubMed:19509290};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and ADP.
CC {ECO:0000269|PubMed:19509290}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70.8 uM for D-galacturonate {ECO:0000269|PubMed:19509290};
CC KM=195 uM for ATP {ECO:0000269|PubMed:19509290};
CC Vmax=1.0 umol/min/ug enzyme toward D-galacturonate
CC {ECO:0000269|PubMed:19509290};
CC Vmax=0.5 umol/min/ug enzyme toward ATP {ECO:0000269|PubMed:19509290};
CC pH dependence:
CC Optimum pH is 7.5-7.8. {ECO:0000269|PubMed:19509290};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:19509290};
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC young siliques. Higher expression in the elongating middle stem region
CC than in the lower or upper stem region. {ECO:0000269|PubMed:19509290}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19579.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FJ439676; ACJ65066.1; -; mRNA.
DR EMBL; AC011560; AAG51369.1; -; Genomic_DNA.
DR EMBL; AC011708; AAF19579.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74944.1; -; Genomic_DNA.
DR EMBL; AY072103; AAL59925.1; -; mRNA.
DR EMBL; AY096732; AAM20366.1; -; mRNA.
DR RefSeq; NP_187681.2; NM_111906.4.
DR AlphaFoldDB; Q8VYG2; -.
DR SMR; Q8VYG2; -.
DR STRING; 3702.AT3G10700.1; -.
DR iPTMnet; Q8VYG2; -.
DR PaxDb; Q8VYG2; -.
DR PRIDE; Q8VYG2; -.
DR EnsemblPlants; AT3G10700.1; AT3G10700.1; AT3G10700.
DR GeneID; 820239; -.
DR Gramene; AT3G10700.1; AT3G10700.1; AT3G10700.
DR KEGG; ath:AT3G10700; -.
DR Araport; AT3G10700; -.
DR TAIR; locus:2075730; AT3G10700.
DR eggNOG; KOG0631; Eukaryota.
DR HOGENOM; CLU_017814_5_0_1; -.
DR InParanoid; Q8VYG2; -.
DR OMA; CKTKEYK; -.
DR OrthoDB; 860024at2759; -.
DR PhylomeDB; Q8VYG2; -.
DR BioCyc; ARA:AT3G10700-MON; -.
DR BRENDA; 2.7.1.44; 399.
DR PRO; PR:Q8VYG2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VYG2; baseline and differential.
DR Genevisible; Q8VYG2; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047912; F:galacturonokinase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:TAIR.
DR GO; GO:0046396; P:D-galacturonate metabolic process; IDA:TAIR.
DR GO; GO:0006012; P:galactose metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR000705; Galactokinase.
DR InterPro; IPR019539; GalKase_N.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006206; Mevalonate/galactokinase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10457:SF6; PTHR10457:SF6; 1.
DR Pfam; PF10509; GalKase_gal_bdg; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF000530; Galactokinase; 1.
DR PRINTS; PR00473; GALCTOKINASE.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Calcium; Carbohydrate metabolism; Kinase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..424
FT /note="Galacturonokinase"
FT /id="PRO_0000407403"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 146..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 35
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 41
FT /note="A->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19509290"
FT MUTAGEN 250
FT /note="Y->F: Loss of sugar specificity."
FT /evidence="ECO:0000269|PubMed:19509290"
FT MUTAGEN 368
FT /note="A->S: Reduced phosphorylation activity."
FT /evidence="ECO:0000269|PubMed:19509290"
SQ SEQUENCE 424 AA; 45729 MW; 8E9EED91CEDBA6F7 CRC64;
MSWPTDSELN SIKEAVAQMS GRDKGEVRVV VAPYRICPLG AHIDHQGGTV SAMTINKGIL
LGFVPSGDTQ VQLRSAQFEG EVCFRVDEIQ HPIGLANKNG ASTPSPSKEK SIWGTYARGA
VYALQSSKKN LKQGIIGYLS GSNGLDSSGL SSSAAVGVAY LLALENANEL TVSPTENIEY
DRLIENGYLG LRNGILDQSA ILLSNYGCLT YMDCKTLDHE LVQAPELEKP FRILLAFSGL
RQALTTNPGY NLRVSECQEA AKVLLTASGN SELEPTLCNV EHAVYEAHKH ELKPVLAKRA
EHYFSENMRV IKGREAWASG NLEEFGKLIS ASGLSSIENY ECGAEPLIQL YKILLKAPGV
YGARFSGAGF RGCCLAFVDA EKAEAAASYV KDEYEKAQPE FANNLNGGKP VLICEAGDAA
RVLL
