ID A0A498N071_LABRO Unreviewed; 201 AA.
AC A0A498N071;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=UMP-CMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE EC=2.7.4.14 {ECO:0000256|HAMAP-Rule:MF_03172};
DE AltName: Full=Deoxycytidylate kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE Short=CK {ECO:0000256|HAMAP-Rule:MF_03172};
DE Short=dCMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE AltName: Full=Nucleoside-diphosphate kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE EC=2.7.4.6 {ECO:0000256|HAMAP-Rule:MF_03172};
DE AltName: Full=Uridine monophosphate/cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE Short=UMP/CMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
DE Short=UMP/CMPK {ECO:0000256|HAMAP-Rule:MF_03172};
GN Name=CMPK1 {ECO:0000256|HAMAP-Rule:MF_03172};
GN Synonyms=CMPK {ECO:0000256|HAMAP-Rule:MF_03172};
GN ORFNames=ROHU_019698 {ECO:0000313|EMBL:RXN27689.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN27689.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN27689.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN27689.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN27689.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) 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. Also displays broad nucleoside diphosphate
CC kinase activity. {ECO:0000256|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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001331, ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_03172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03172};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03172};
CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|HAMAP-Rule:MF_03172};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_03172}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_03172}. Nucleus {ECO:0000256|HAMAP-
CC Rule:MF_03172}. Note=Predominantly nuclear. {ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-Rule:MF_03172}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03172}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN27689.1}.
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DR EMBL; QBIY01011962; RXN27689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498N071; -.
DR STRING; 84645.A0A498N071; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
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: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; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01359; UMP_CMP_kin_fam; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03172};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03172};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03172};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03172};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03172};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498N071};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_03172}; Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03172}.
FT REGION 34..64
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT REGION 138..148
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 14..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 40
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 62..64
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 98..101
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 105
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 145
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 156
FT /ligand="a ribonucleoside 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:58043"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03172"
SQ SEQUENCE 201 AA; 22793 MW; 1079A7959B3CADFD CRC64;
MMKPQVVFVL GGPGAGKGTQ CAKIVENYSY THLSAGDLLR EERSRTGSEF GQLIDNYIKE
GKIVPVEITI NLLKKVVTLA MEQTMKADEK KFRFLIDGFP RNQDNLQGWN TVMDGKADVK
FVLFFDCSNE VCIDRCLERG KSSGRTDDNR ESLEKRIQTY LQSTRPIIEQ YEKQGKVRKI
DASRSVDEVF GDVKNLLDKE G
//
