GALK1_ARATH
ID GALK1_ARATH Reviewed; 496 AA.
AC Q9SEE5; O24021; O48936;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Galactokinase;
DE EC=2.7.1.6;
DE AltName: Full=Galactose kinase;
GN Name=GAL1; Synonyms=GALK; OrderedLocusNames=At3g06580; ORFNames=F5E6.9;
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], AND FUNCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9225860; DOI=10.1023/a:1005816104743;
RA Kaplan C.P., Tugal H.B., Baker A.;
RT "Isolation of a cDNA encoding an Arabidopsis galactokinase by functional
RT expression in yeast.";
RL Plant Mol. Biol. 34:497-506(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10344205; DOI=10.1023/a:1006181908753;
RA Sherson S., Gy I., Medd J., Schmidt R., Dean C., Kreis M., Lecharny A.,
RA Cobbett C.;
RT "The arabinose kinase, ARA1, gene of Arabidopsis is a novel member of the
RT galactose kinase gene family.";
RL Plant Mol. Biol. 39:1003-1012(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Gy I., Kreis M., Lecharny A.;
RT "Fine structure of an Arabidopsis thaliana galactose kinase Gal1 gene.";
RL (er) Plant Gene Register PGR99-171(1999).
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF GLU-62; SER-206; TYR-262 AND ALA-437, AND TISSUE
RP 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 [8]
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: Sugar-1-kinase with a very high substrate specificity for the
CC alpha-anomeric configuration of D-galacose (D-Gal). Converts also
CC efficiently 2-deoxy-D-Gal to 2-deoxy-D-al-1-phosphate.
CC {ECO:0000269|PubMed:19509290, ECO:0000269|PubMed:9225860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate
CC + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378, ChEBI:CHEBI:28061,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58336, ChEBI:CHEBI:456216; EC=2.7.1.6;
CC 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=701 uM for D-galactose {ECO:0000269|PubMed:19509290};
CC KM=701 uM for ATP {ECO:0000269|PubMed:19509290};
CC Vmax=3.5 umol/min/ug enzyme toward D-galactose
CC {ECO:0000269|PubMed:19509290};
CC Vmax=3.3 umol/min/ug enzyme toward ATP {ECO:0000269|PubMed:19509290};
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:19509290};
CC Temperature dependence:
CC Optimum temperature is 30-42 degrees Celsius.
CC {ECO:0000269|PubMed:19509290};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
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. GalK subfamily.
CC {ECO:0000305}.
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DR EMBL; X99851; CAA68163.1; -; mRNA.
DR EMBL; AF024623; AAB94084.1; -; mRNA.
DR EMBL; AF152851; AAF15552.1; -; Genomic_DNA.
DR EMBL; AC020580; AAG51339.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74417.1; -; Genomic_DNA.
DR EMBL; AY136356; AAM97022.1; -; mRNA.
DR EMBL; BT010374; AAQ56817.1; -; mRNA.
DR PIR; T51592; T51592.
DR RefSeq; NP_187310.1; NM_111534.4.
DR AlphaFoldDB; Q9SEE5; -.
DR SMR; Q9SEE5; -.
DR BioGRID; 5172; 2.
DR STRING; 3702.AT3G06580.1; -.
DR iPTMnet; Q9SEE5; -.
DR PaxDb; Q9SEE5; -.
DR PRIDE; Q9SEE5; -.
DR ProteomicsDB; 228755; -.
DR EnsemblPlants; AT3G06580.1; AT3G06580.1; AT3G06580.
DR GeneID; 819837; -.
DR Gramene; AT3G06580.1; AT3G06580.1; AT3G06580.
DR KEGG; ath:AT3G06580; -.
DR Araport; AT3G06580; -.
DR TAIR; locus:2084344; AT3G06580.
DR eggNOG; KOG0631; Eukaryota.
DR HOGENOM; CLU_017814_6_2_1; -.
DR InParanoid; Q9SEE5; -.
DR OMA; PVCYNLR; -.
DR OrthoDB; 860024at2759; -.
DR PhylomeDB; Q9SEE5; -.
DR BioCyc; ARA:AT1G64440-MON; -.
DR BioCyc; ARA:AT3G06580-MON; -.
DR BioCyc; MetaCyc:AT3G06580-MON; -.
DR UniPathway; UPA00214; -.
DR PRO; PR:Q9SEE5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SEE5; baseline and differential.
DR Genevisible; Q9SEE5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004335; F:galactokinase 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:0006012; P:galactose metabolic process; IDA:TAIR.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR000705; Galactokinase.
DR InterPro; IPR019741; Galactokinase_CS.
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; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR006206; Mevalonate/galactokinase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
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.
DR TIGRFAMs; TIGR00131; gal_kin; 1.
DR PROSITE; PS00106; GALACTOKINASE; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Calcium; Carbohydrate metabolism;
KW Galactose metabolism; Kinase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..496
FT /note="Galactokinase"
FT /id="PRO_0000184651"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 159..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 56
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 62
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19509290"
FT MUTAGEN 206
FT /note="S->G: Decreased specificity and phosphorylation of
FT GalNAc."
FT /evidence="ECO:0000269|PubMed:19509290"
FT MUTAGEN 262
FT /note="Y->F: No effect on specificity or activity."
FT /evidence="ECO:0000269|PubMed:19509290"
FT MUTAGEN 437
FT /note="A->S: Reduced phosphorylation activity."
FT /evidence="ECO:0000269|PubMed:19509290"
FT CONFLICT 274..304
FT /note="IILGVKLGMEPKEAISKVKTLSDVEGLCVSF -> DQYLVLSSEWNQKKQYQ
FT KLRLFLMWRDYVCHS (in Ref. 1; CAA68163)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="A -> T (in Ref. 2; AAB94084)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="S -> T (in Ref. 1; CAA68163)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="A -> P (in Ref. 3; AAF15552)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..465
FT /note="YK -> HN (in Ref. 1; CAA68163)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="A -> G (in Ref. 1; CAA68163)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="A -> S (in Ref. 1; CAA68163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 54341 MW; F520805A5B84CB61 CRC64;
MAKPEEVSVP IFTSLEPVYG EGSLLQEATQ RFDVLKANFN DVFGASPQLF ARSPGRVNLI
GEHIDYEGYS VLPMAIRQDT IIAIRKCEDQ KQLRIANVND KYTMCTYPAD PDQEIDLKNH
KWGHYFICAY KGFHEYAKSK GVNLGSPVGL DVLVDGIVPT GSGLSSSAAF VCSATIAIMA
VFGHNFEKKE LAQLTCECER HIGTQSGGMD QAISIMAKTG FAELIDFNPV RATDVKLPDG
GSFVIAHSLA ESQKAVTAAK NYNNRVVECR LASIILGVKL GMEPKEAISK VKTLSDVEGL
CVSFAGDRGS SDPLLAVKEY LKEEPYTAEE IEKILEEKLP SIVNNDPTSL AVLNAATHFK
LHQRAAHVYS EARRVHGFKD TVNSNLSDEE KLKKLGDLMN ESHYSCSVLY ECSCPELEEL
VQVCKENGAL GARLTGAGWG GCAVALVKEF DVTQFIPAVK EKYYKKRVEK GVVKKEDMEL
YLFASKPSSG AAIFNL
