GMK1_ARATH
ID GMK1_ARATH Reviewed; 387 AA.
AC P93757; Q683H2; Q9M681; Q9M683;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Guanylate kinase 1;
DE Short=AtGK1;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase 1;
GN Name=GK-1; Synonyms=AGK1; OrderedLocusNames=At2g41880; ORFNames=T11A7.23;
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=10632732; DOI=10.1046/j.1432-1327.2000.01045.x;
RA Kumar V., Spangenberg O., Konrad M.;
RT "Cloning of the guanylate kinase homologues AGK-1 and AGK-2 from
RT Arabidopsis thaliana and characterization of AGK-1.";
RL Eur. J. Biochem. 267:606-615(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17727616; DOI=10.1111/j.1365-313x.2007.03251.x;
RA Sugimoto H., Kusumi K., Noguchi K., Yano M., Yoshimura A., Iba K.;
RT "The rice nuclear gene, VIRESCENT 2, is essential for chloroplast
RT development and encodes a novel type of guanylate kinase targeted to
RT plastids and mitochondria.";
RL Plant J. 52:512-527(2007).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP. Required
CC for normal development of the gametophyte and embryo, in association
CC with GK2. {ECO:0000269|PubMed:10632732, ECO:0000269|PubMed:17727616}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:456216; EC=2.7.4.8;
CC Evidence={ECO:0000269|PubMed:10632732};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50.6 uM for ATP {ECO:0000269|PubMed:10632732};
CC KM=6.4 uM for GMP {ECO:0000269|PubMed:10632732};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutant atgk1 and atgk2 is lethal.
CC {ECO:0000269|PubMed:17727616}.
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR EMBL; AF204675; AAF70408.1; -; mRNA.
DR EMBL; AF204677; AAF60252.1; -; Genomic_DNA.
DR EMBL; AC002339; AAM14825.1; -; Genomic_DNA.
DR EMBL; U90439; AAF18683.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10044.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61415.1; -; Genomic_DNA.
DR EMBL; AK175145; BAD42908.1; -; mRNA.
DR EMBL; BT028912; ABI49459.1; -; mRNA.
DR PIR; C84847; C84847.
DR PIR; T50675; T50675.
DR RefSeq; NP_001323632.1; NM_001336943.1.
DR RefSeq; NP_565961.1; NM_129752.5.
DR AlphaFoldDB; P93757; -.
DR SMR; P93757; -.
DR STRING; 3702.AT2G41880.1; -.
DR iPTMnet; P93757; -.
DR PaxDb; P93757; -.
DR PRIDE; P93757; -.
DR ProteomicsDB; 247008; -.
DR DNASU; 818788; -.
DR EnsemblPlants; AT2G41880.1; AT2G41880.1; AT2G41880.
DR EnsemblPlants; AT2G41880.7; AT2G41880.7; AT2G41880.
DR GeneID; 818788; -.
DR Gramene; AT2G41880.1; AT2G41880.1; AT2G41880.
DR Gramene; AT2G41880.7; AT2G41880.7; AT2G41880.
DR KEGG; ath:AT2G41880; -.
DR Araport; AT2G41880; -.
DR TAIR; locus:2054356; AT2G41880.
DR eggNOG; KOG0707; Eukaryota.
DR HOGENOM; CLU_037258_0_0_1; -.
DR InParanoid; P93757; -.
DR PhylomeDB; P93757; -.
DR BioCyc; ARA:AT2G41880-MON; -.
DR BioCyc; MetaCyc:AT2G41880-MON; -.
DR SABIO-RK; P93757; -.
DR PRO; PR:P93757; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93757; baseline and differential.
DR Genevisible; P93757; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004385; F:guanylate kinase activity; IDA:TAIR.
DR GO; GO:0048229; P:gametophyte development; IGI:UniProtKB.
DR GO; GO:0009117; P:nucleotide metabolic process; TAS:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR017665; Guanylate_kinase.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00625; Guanylate_kin; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03263; guanyl_kin; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..387
FT /note="Guanylate kinase 1"
FT /id="PRO_0000430125"
FT DOMAIN 137..319
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT ACT_SITE 177
FT /evidence="ECO:0000250"
FT ACT_SITE 270
FT /evidence="ECO:0000250"
FT ACT_SITE 281
FT /evidence="ECO:0000250"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 45
FT /note="T -> N (in Ref. 1; AAF70408/AAF60252)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="H -> Y (in Ref. 1; AAF70408/AAF60252)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="R -> I (in Ref. 1; AAF60252)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="A -> T (in Ref. 1; AAF70408/AAF60252)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="V -> L (in Ref. 1; AAF70408/AAF60252)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="P -> Q (in Ref. 4; BAD42908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 42668 MW; 9CC933E15577C36B CRC64;
MGEAPAVLVD HPENGHSNGV CVKSEPENTE ITVDVGDRIF LIGGTHERNN FSIGVQIYDK
ISNNWFSPIV LGTGPKPSKG YSAFVLEQGR ILVIKKGSPR NDSIWFLEVD SPYVREQKKL
LRKEVVAWSK GVRGNAEKPI VISGPSGVGK GTLISMLMKE FPSMFGFSVS HTTRSPRSME
MDGVHYHFAD KKVMEKEIKD GKFLEFASVH GNLYGTSIES VEAVTDSGKR CILDIDVQGA
RSVRASSLDA IFIFVCPPSM KELEDRLRAR GTETEEQIQK RLRNAEAEIK EGISSGIFGL
ILYNDNLEEC YKKLKNLLGL DGLAHVNGVE IEGINLPIEY AVSKMEDKII IQETGKETRN
KIVVDISSLN GGAPGRTRGI LVDAIKF
