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KCY4_ORYSJ
ID   KCY4_ORYSJ              Reviewed;         214 AA.
AC   Q6K7H2; A0A0P0VQC2;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=UMP-CMP kinase 4 {ECO:0000255|HAMAP-Rule:MF_03172};
DE            EC=2.7.4.14 {ECO:0000255|HAMAP-Rule:MF_03172};
DE   AltName: Full=Deoxycytidylate kinase 4 {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=CK 4 {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=dCMP kinase 4 {ECO:0000255|HAMAP-Rule:MF_03172};
DE   AltName: Full=Uridine monophosphate/cytidine monophosphate kinase 4 {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=UMP/CMP kinase 4 {ECO:0000255|HAMAP-Rule:MF_03172};
DE            Short=UMP/CMPK 4 {ECO:0000255|HAMAP-Rule:MF_03172};
GN   OrderedLocusNames=Os02g0778400, LOC_Os02g53790; ORFNames=OJ1293_A01.3;
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 [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   [2]
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   [3]
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   [4]
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).
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 + 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   -!- 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   -!- 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=AK103372; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AP004846; BAD19510.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF10209.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS81190.1; -; Genomic_DNA.
DR   EMBL; AK103372; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; Q6K7H2; -.
DR   SMR; Q6K7H2; -.
DR   STRING; 4530.OS02T0778400-01; -.
DR   PaxDb; Q6K7H2; -.
DR   PRIDE; Q6K7H2; -.
DR   EnsemblPlants; Os02t0778400-01; Os02t0778400-01; Os02g0778400.
DR   Gramene; Os02t0778400-01; Os02t0778400-01; Os02g0778400.
DR   eggNOG; KOG3079; Eukaryota.
DR   HOGENOM; CLU_032354_0_1_1; -.
DR   InParanoid; Q6K7H2; -.
DR   OMA; LQGWNKQ; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6K7H2; OS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; 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:0004127; F:cytidylate kinase activity; IBA:GO_Central.
DR   GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR   GO; GO:0033862; F:UMP kinase activity; IBA:GO_Central.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0046705; P:CDP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006225; P:UDP biosynthetic process; IBA:GO_Central.
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..214
FT                   /note="UMP-CMP kinase 4"
FT                   /id="PRO_0000430124"
FT   REGION          57..86
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   REGION          149..157
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         37..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         63
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         84..86
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         111..114
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         118
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         154
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         165
FT                   /ligand="a ribonucleoside 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58043"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   BINDING         193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
SQ   SEQUENCE   214 AA;  23556 MW;  704C71D236B8F50E CRC64;
     MGSVVDAPTV VAGQEEVTDN MLGDKKVTVV FVLGGPGSGK GTQCANIVEH FGFIHLSAGD
     LLRAEIKSGS ENGTMIENMI KEGKIVPSEV TIKLLQEAMI KSGNDKFLID GFPRNEENRA
     AFENVTKITP AFVLFFDCSE EEMERRLLGR NQGRVDDNIE TIRKRFKVFV ESSLPVIEYY
     NAKDKVKKID AAKPIPEVFE DVKAIFAPYA PNAA
 
 
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