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Database: UniProt
Entry: A0A1D8RS93_9GAMM
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Original site: A0A1D8RS93_9GAMM 
ID   A0A1D8RS93_9GAMM        Unreviewed;       246 AA.
AC   A0A1D8RS93;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Uridylate kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE            Short=UK {ECO:0000256|HAMAP-Rule:MF_01220};
DE            EC=2.7.4.22 {ECO:0000256|HAMAP-Rule:MF_01220};
DE   AltName: Full=Uridine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE            Short=UMP kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE            Short=UMPK {ECO:0000256|HAMAP-Rule:MF_01220};
GN   Name=pyrH {ECO:0000256|HAMAP-Rule:MF_01220};
GN   ORFNames=A3Q34_03320 {ECO:0000313|EMBL:AOW75969.1};
OS   Colwellia sp. PAMC 20917.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=1816218 {ECO:0000313|EMBL:AOW75969.1, ECO:0000313|Proteomes:UP000177820};
RN   [1] {ECO:0000313|EMBL:AOW75969.1, ECO:0000313|Proteomes:UP000177820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 20917 {ECO:0000313|EMBL:AOW75969.1,
RC   ECO:0000313|Proteomes:UP000177820};
RA   Kim H.-W.;
RT   "Complete genome sequence of Colwellia sp. PAMC 20917.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC       {ECO:0000256|HAMAP-Rule:MF_01220}.
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=2.7.4.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00001018, ECO:0000256|HAMAP-
CC         Rule:MF_01220};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by UTP.
CC       {ECO:0000256|HAMAP-Rule:MF_01220}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       UDP from UMP (UMPK route): step 1/1. {ECO:0000256|ARBA:ARBA00004791,
CC       ECO:0000256|HAMAP-Rule:MF_01220}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01220}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220}.
CC   -!- SIMILARITY: Belongs to the UMP kinase family.
CC       {ECO:0000256|ARBA:ARBA00007614, ECO:0000256|HAMAP-Rule:MF_01220}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01220}.
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DR   EMBL; CP014944; AOW75969.1; -; Genomic_DNA.
DR   RefSeq; WP_070374055.1; NZ_CP014944.1.
DR   AlphaFoldDB; A0A1D8RS93; -.
DR   STRING; 1816218.A3Q34_03320; -.
DR   KEGG; coz:A3Q34_03320; -.
DR   OrthoDB; 9807458at2; -.
DR   UniPathway; UPA00159; UER00275.
DR   Proteomes; UP000177820; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04254; AAK_UMPK-PyrH-Ec; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   HAMAP; MF_01220_B; PyrH_B; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR011817; Uridylate_kinase.
DR   InterPro; IPR015963; Uridylate_kinase_bac.
DR   NCBIfam; TIGR02075; pyrH_bact; 1.
DR   PANTHER; PTHR42833:SF4; AMINO ACID KINASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR42833; URIDYLATE KINASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF005650; Uridylate_kin; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_01220};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01220};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01220};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01220};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01220};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01220}; Reference proteome {ECO:0000313|Proteomes:UP000177820};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01220}.
FT   DOMAIN          11..219
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   REGION          23..28
FT                   /note="Involved in allosteric activation by GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         15..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         57
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         77
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         138..145
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
SQ   SEQUENCE   246 AA;  26512 MW;  0B854BEACA0E5BF3 CRC64;
     MSISPKPIYR RILLKLSGEA LMGEEGFGID PKVLDRMAQE IKELIEMGIQ VGLVIGGGNL
     FRGAGLAEAG MNRVVGDQMG MLATVMNGLA MRDALHRAFV NAKLMSAIDL AGVCDRYNWA
     EGISLLKSGR VVIFSAGTGN PFFTTDSAAC LRGIEIEADV VLKATKVDGI YSDDPVKNPD
     ATLYSQLSYN EVLEKELKVM DLAAFTLARD HNMTIRVFNM NKPGALKAVV MGGNEGTTID
     HSENLV
//
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