PYRH_ENTFA
ID PYRH_ENTFA Reviewed; 240 AA.
AC Q831V1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Uridylate kinase;
DE Short=UK;
DE EC=2.7.4.22;
DE AltName: Full=Uridine monophosphate kinase;
DE Short=UMP kinase;
DE Short=UMPK;
GN Name=pyrH; OrderedLocusNames=EF_2396;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBUNIT.
RX PubMed=17210578; DOI=10.1074/jbc.m606963200;
RA Evrin C., Straut M., Slavova-Azmanova N., Bucurenci N., Onu A., Assairi L.,
RA Ionescu M., Palibroda N., Barzu O., Gilles A.-M.;
RT "Regulatory mechanisms differ in UMP kinases from Gram-negative and Gram-
RT positive bacteria.";
RL J. Biol. Chem. 282:7242-7253(2007).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC {ECO:0000269|PubMed:17210578}.
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 -!- ACTIVITY REGULATION: Allosterically activated by GTP. Probably
CC inhibited by UTP. {ECO:0000269|PubMed:17210578}.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC UDP from UMP (UMPK route): step 1/1.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:17210578}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000305}.
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DR EMBL; AE016830; AAO82117.1; -; Genomic_DNA.
DR RefSeq; NP_816047.1; NC_004668.1.
DR RefSeq; WP_002356761.1; NZ_KE136528.1.
DR AlphaFoldDB; Q831V1; -.
DR SMR; Q831V1; -.
DR STRING; 226185.EF_2396; -.
DR EnsemblBacteria; AAO82117; AAO82117; EF_2396.
DR GeneID; 60894449; -.
DR KEGG; efa:EF2396; -.
DR PATRIC; fig|226185.9.peg.2238; -.
DR eggNOG; COG0528; Bacteria.
DR HOGENOM; CLU_033861_0_0_9; -.
DR OMA; PIIVFDM; -.
DR UniPathway; UPA00159; UER00275.
DR Proteomes; UP000001415; 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; -; 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 Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF005650; Uridylate_kin; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR02075; pyrH_bact; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..240
FT /note="Uridylate kinase"
FT /id="PRO_1000053924"
FT REGION 20..25
FT /note="Involved in allosteric activation by GTP"
FT /evidence="ECO:0000255"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250"
FT BINDING 135..142
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 240 AA; 26111 MW; 56814E243275DDC8 CRC64;
MVKPKYQRVV LKLSGEALAG EDGFGIKPPV IKEIVQEIKE VHELGIEMAI VVGGGNIWRG
QIGAQMGMER AQADYMGMLA TVMNALALQD TLENLGVPTR VQTSIEMRQI AEPYIRRRAE
RHLEKGRVVI FAGGTGNPYF STDTTAALRA AEVDADVILM AKNNVDGVYS ADPRVDETAT
KFEELTHLDV ISKGLQVMDS TASSLSMDND IPLVVFNLNE AGNIRRAILG ENIGTTVRGK
