GMK2_ARATH
ID GMK2_ARATH Reviewed; 389 AA.
AC Q9M682; Q9SCL8;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Guanylate kinase 2;
DE Short=AtGK2;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase 2;
GN Name=GK-2; Synonyms=AGK2; OrderedLocusNames=At3g57550; ORFNames=T8H10.150;
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].
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=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 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 GK1. {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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M682-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Growth retardation, narrow and dark-green leaves
CC with elongated petioles, root growth inhibition and reduced fertility.
CC The double mutant atgk1 and atgk2 is lethal.
CC {ECO:0000269|PubMed:17727616}.
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66112.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF204676; AAF70409.1; -; mRNA.
DR EMBL; AL133248; CAB66112.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79670.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63374.1; -; Genomic_DNA.
DR EMBL; BT002466; AAO00826.1; -; mRNA.
DR EMBL; BT009693; AAP88327.1; -; mRNA.
DR PIR; T46191; T46191.
DR RefSeq; NP_001325466.1; NM_001339877.1. [Q9M682-1]
DR RefSeq; NP_567051.1; NM_115615.3. [Q9M682-1]
DR AlphaFoldDB; Q9M682; -.
DR SMR; Q9M682; -.
DR BioGRID; 10238; 1.
DR STRING; 3702.AT3G57550.2; -.
DR PaxDb; Q9M682; -.
DR PRIDE; Q9M682; -.
DR ProteomicsDB; 247009; -. [Q9M682-1]
DR EnsemblPlants; AT3G57550.1; AT3G57550.1; AT3G57550. [Q9M682-1]
DR EnsemblPlants; AT3G57550.3; AT3G57550.3; AT3G57550. [Q9M682-1]
DR GeneID; 824922; -.
DR Gramene; AT3G57550.1; AT3G57550.1; AT3G57550. [Q9M682-1]
DR Gramene; AT3G57550.3; AT3G57550.3; AT3G57550. [Q9M682-1]
DR KEGG; ath:AT3G57550; -.
DR Araport; AT3G57550; -.
DR eggNOG; KOG0707; Eukaryota.
DR HOGENOM; CLU_037258_0_0_1; -.
DR OMA; NIWFLEV; -.
DR PhylomeDB; Q9M682; -.
DR PRO; PR:Q9M682; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M682; baseline and differential.
DR Genevisible; Q9M682; 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; IBA:GO_Central.
DR GO; GO:0048229; P:gametophyte development; IGI:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048638; P:regulation of developmental growth; IMP:UniProtKB.
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; IPR020590; Guanylate_kinase_CS.
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; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..389
FT /note="Guanylate kinase 2"
FT /id="PRO_0000430126"
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"
SQ SEQUENCE 389 AA; 42553 MW; F4848EE2DC23EBBD CRC64;
MGEAPAFFVD HLENGYTNGF GVKSEPKNRD TSVLIGDRSF VIGGNHEGNP LFLGVQIHDK
VTNKWSSPSV LGTGPKPCKG YSAIVLPKGR ILVIKKGSAS DDSIWFLEVD TPFIREQKKL
LGREVVAWSK GVRGNAEKPI VISGPSGVGK GTLISMLMKE FPSMFGFSVS HTTRAPRCME
KNGVHYHFTD KTVMEKEIKD GKFLEFASVH GNLYGTSIES VEVVTDSGKR CILDIDVQGA
RSVKASSLDA IFIFVCPPSM KELEDRLRAR GTETEEQIQK RLRNADAEIK AGKSSGIFEH
KLYNDNLEEC YKTLKNLLGI NDLAPVNGVE VEGINLPKEH TVTKMDDKIL IQETGEGTKN
KMIVLDLSSI NGGAPGRTRG IVLDTVKSS
