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KCY2_ARATH
ID   KCY2_ARATH              Reviewed;         259 AA.
AC   Q6NMK6; A0A1P8B5G4; Q9SB35;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Probable UMP-CMP kinase 2;
DE            EC=2.7.4.14 {ECO:0000255|HAMAP-Rule:MF_03172};
DE   AltName: Full=Deoxycytidylate kinase {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=CK {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=dCMP kinase {ECO:0000255|HAMAP-Rule:MF_03172};
DE   AltName: Full=Uridine monophosphate/cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=UMP/CMP kinase {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=UMP/CMPK {ECO:0000255|HAMAP-Rule:MF_03172};
GN   Name=UMK2; OrderedLocusNames=At4g25280; ORFNames=F24A6.120;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-259.
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside
CC       monophosphates at the expense of ATP. Plays an important role in de
CC       novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP
CC       as phosphate acceptors. {ECO:0000255|HAMAP-Rule:MF_03172}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03172};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC         ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03172};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03172};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03172};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_03172};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03172}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}.
CC   -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC       small peripheral domains, NMPbind and LID, which undergo movements
CC       during catalysis. The LID domain closes over the site of phosphoryl
CC       transfer upon ATP binding. Assembling and dissambling the active center
CC       during each catalytic cycle provides an effective means to prevent ATP
CC       hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03172}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03172}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR24708.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA23069.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB81339.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL035396; CAA23069.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161563; CAB81339.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85034.2; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66837.1; -; Genomic_DNA.
DR   EMBL; BT010930; AAR24708.1; ALT_INIT; mRNA.
DR   EMBL; BT011652; AAS47658.1; -; mRNA.
DR   PIR; T05549; T05549.
DR   RefSeq; NP_001320061.1; NM_001341726.1.
DR   RefSeq; NP_194258.3; NM_118660.3.
DR   AlphaFoldDB; Q6NMK6; -.
DR   SMR; Q6NMK6; -.
DR   STRING; 3702.AT4G25280.1; -.
DR   PaxDb; Q6NMK6; -.
DR   PRIDE; Q6NMK6; -.
DR   ProteomicsDB; 247154; -.
DR   EnsemblPlants; AT4G25280.1; AT4G25280.1; AT4G25280.
DR   EnsemblPlants; AT4G25280.2; AT4G25280.2; AT4G25280.
DR   GeneID; 828631; -.
DR   Gramene; AT4G25280.1; AT4G25280.1; AT4G25280.
DR   Gramene; AT4G25280.2; AT4G25280.2; AT4G25280.
DR   KEGG; ath:AT4G25280; -.
DR   Araport; AT4G25280; -.
DR   TAIR; locus:2122644; AT4G25280.
DR   eggNOG; KOG3079; Eukaryota.
DR   HOGENOM; CLU_032354_0_1_1; -.
DR   InParanoid; Q6NMK6; -.
DR   OMA; TQCDRMI; -.
DR   OrthoDB; 1378291at2759; -.
DR   PhylomeDB; Q6NMK6; -.
DR   BioCyc; ARA:AT4G25280-MON; -.
DR   PRO; PR:Q6NMK6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q6NMK6; baseline and differential.
DR   Genevisible; Q6NMK6; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR   GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR   GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IBA:GO_Central.
DR   GO; GO:0033862; F:UMP kinase activity; IEA:RHEA.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR   GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR   HAMAP; MF_03172; Adenylate_kinase_UMP_CMP_kin; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006266; UMP_CMP_kinase.
DR   PANTHER; PTHR23359; PTHR23359; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01359; UMP_CMP_kin_fam; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..259
FT                   /note="Probable UMP-CMP kinase 2"
FT                   /id="PRO_0000425984"
FT   REGION          83..112
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   REGION          175..183
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         63..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         89
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         110..112
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         137..140
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         144
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         180
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         191
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
SQ   SEQUENCE   259 AA;  29045 MW;  D1766E98B3EB8540 CRC64;
     MWRRVALLSP MISSSSRSLK LSQAASGLKV GESFATDIIS QEERVSPPKE KAPFITFVLG
     GPGSGKGTQC EKIVETFGLQ HLSAGDLLRR EIAMHTENGA MILNLIKDGK IVPSEVTVKL
     IQKELESSDN RKFLIDGFPR TEENRVAFER IIRADPDVVL FFDCPEEEMV KRVLNRNQGR
     IDDNITTMKK RLKIFNALNR PVIDYYKNKG KLYTINAVGT VDDIFQHVLP IFNSFEQLKE
     SSHVNPQSHL GSSLVENSS
 
 
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