GMK2_ORYSJ
ID GMK2_ORYSJ Reviewed; 285 AA.
AC Q10M74; A0A0N7KH63;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Guanylate kinase 2, chloroplastic/mitochondrial;
DE Short=OsGKpm;
DE EC=2.7.4.8;
DE AltName: Full=GMP kinase 2;
DE AltName: Full=Protein VIRESCENT 2;
DE Flags: Precursor;
GN Name=V2; OrderedLocusNames=Os03g0320900, LOC_Os03g20460;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF VAL-162.
RC STRAIN=cv. Taichung 65;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15356324; DOI=10.1093/pcp/pch111;
RA Sugimoto H., Kusumi K., Tozawa Y., Yazaki J., Kishimoto N., Kikuchi S.,
RA Iba K.;
RT "The virescent-2 mutation inhibits translation of plastid transcripts for
RT the plastid genetic system at an early stage of chloroplast
RT differentiation.";
RL Plant Cell Physiol. 45:985-996(2004).
CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP. Essential
CC for chloroplast differentiation at early stage of leaf development. May
CC not be involved in the synthesis and maintenance of the organellar DNA
CC during leaf development. {ECO:0000269|PubMed:15356324,
CC 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:17727616};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Mitochondrion.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions at the permissive temperature of 30 degrees Celsius, but
CC mutant seedlings develop chlorotic leaves with aberrant chloroplasts
CC under the restrictive temperature of 20 degrees Celsius.
CC {ECO:0000269|PubMed:15356324, ECO:0000269|PubMed:17727616}.
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR EMBL; AB267728; BAF46274.1; -; mRNA.
DR EMBL; DP000009; ABF95662.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11870.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83937.1; -; Genomic_DNA.
DR EMBL; AK106255; BAG97659.1; -; mRNA.
DR RefSeq; XP_015628708.1; XM_015773222.1.
DR AlphaFoldDB; Q10M74; -.
DR SMR; Q10M74; -.
DR STRING; 4530.OS03T0320900-01; -.
DR PaxDb; Q10M74; -.
DR PRIDE; Q10M74; -.
DR EnsemblPlants; Os03t0320900-01; Os03t0320900-01; Os03g0320900.
DR GeneID; 4332674; -.
DR Gramene; Os03t0320900-01; Os03t0320900-01; Os03g0320900.
DR KEGG; osa:4332674; -.
DR eggNOG; KOG0707; Eukaryota.
DR HOGENOM; CLU_072704_0_0_1; -.
DR InParanoid; Q10M74; -.
DR OMA; EWAVVHG; -.
DR OrthoDB; 1522834at2759; -.
DR BRENDA; 2.7.4.8; 8948.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10M74; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048638; P:regulation of developmental growth; IEA:EnsemblPlants.
DR Gene3D; 3.40.50.300; -; 1.
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; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03263; guanyl_kin; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Kinase; Mitochondrion; Nucleotide-binding;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..42
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..285
FT /note="Guanylate kinase 2, chloroplastic/mitochondrial"
FT /id="PRO_0000430129"
FT DOMAIN 91..272
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /evidence="ECO:0000250"
FT ACT_SITE 224
FT /evidence="ECO:0000250"
FT ACT_SITE 235
FT /evidence="ECO:0000250"
FT BINDING 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT BINDING 255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 162
FT /note="V->I: In v2; reduces specific activity for GMP 20-
FT fold. Development of chlorotic leaves at the restrictive
FT temperature of 20 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:17727616"
SQ SEQUENCE 285 AA; 31680 MW; 7C6C3C3CC2554A6E CRC64;
MLLTRRFSSA LARSPLLPRS LPPPRAVPAT PPAPRPPPRR LMSSSSSGWH HSSRPPPPPP
SGADKDQLFR GLEAALGTTF SSEPLAPPPQ PMILVISGPS GVGKDAVIQR LQEEREGMHF
VVTATSRAKR PGEVDGKDYY FVTKEEFLTM IERKELLEYA LVYGEYKGIP KQQIRDYMAK
GYDIVLRVDI QGAATLREIL GESAIFIFLV AESEEALVKR LIHRKTETSD MLLVRVATAR
EEVKRMNNFD YVVVNSEGNL EGAVKQVESI IDAEKAKVHK RTVNI
