PYRH_STRPN
ID PYRH_STRPN Reviewed; 247 AA.
AC Q97R83;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=SP_0944;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBSTRATE SPECIFICITY,
RP CHARACTERIZATION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=R6 / R800;
RX PubMed=15324307; DOI=10.1042/bj20040440;
RA Fassy F., Krebs O., Lowinski M., Ferrari P., Winter J.,
RA Collard-Dutilleul V., Salahbey Hocini K.;
RT "UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP
RT binding and allosteric regulation.";
RL Biochem. J. 384:619-627(2004).
RN [3]
RP ACTIVITY REGULATION, KINETIC PARAMETERS, AND 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, with
CC ATP as the most efficient phosphate donor.
CC {ECO:0000269|PubMed:15324307}.
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. Inhibited by UTP,
CC 5-bromo-UTP and 5-iodo-UTP. {ECO:0000269|PubMed:15324307,
CC ECO:0000269|PubMed:17210578}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22 uM for UMP (in the absence of GTP)
CC {ECO:0000269|PubMed:15324307, ECO:0000269|PubMed:17210578};
CC KM=100 uM for UMP (in the presence of GTP)
CC {ECO:0000269|PubMed:15324307, ECO:0000269|PubMed:17210578};
CC Vmax=274 umol/min/mg enzyme (at pH 7.5 and in the presence of
CC manganese) {ECO:0000269|PubMed:15324307,
CC ECO:0000269|PubMed:17210578};
CC Vmax=399 umol/min/mg enzyme (at pH 7.5 and in the presence of
CC magnesium) {ECO:0000269|PubMed:15324307,
CC ECO:0000269|PubMed:17210578};
CC Vmax=182 umol/min/mg enzyme (at pH 6.5 and in the presence of
CC magnesium) {ECO:0000269|PubMed:15324307,
CC ECO:0000269|PubMed:17210578};
CC Note=Positive cooperativity is observed with ATP as variable
CC substrate, but it is strongly reduced in the presence of GTP. GTP
CC enhances the affinity for ATP whereas UTP decreases it.;
CC pH dependence:
CC Optimum pH is below 6.5 at low ATP concentrations and is 7.4-7.8 at
CC high ATP concentrations. {ECO:0000269|PubMed:15324307};
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:15324307,
CC 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; AE005672; AAK75067.1; -; Genomic_DNA.
DR PIR; B95109; B95109.
DR AlphaFoldDB; Q97R83; -.
DR SMR; Q97R83; -.
DR STRING; 170187.SP_0944; -.
DR EnsemblBacteria; AAK75067; AAK75067; SP_0944.
DR KEGG; spn:SP_0944; -.
DR eggNOG; COG0528; Bacteria.
DR OMA; PIIVFDM; -.
DR PhylomeDB; Q97R83; -.
DR BRENDA; 2.7.4.22; 1960.
DR SABIO-RK; Q97R83; -.
DR UniPathway; UPA00159; UER00275.
DR Proteomes; UP000000585; 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; Direct protein sequencing;
KW Kinase; Nucleotide-binding; Pyrimidine biosynthesis; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..247
FT /note="Uridylate kinase"
FT /id="PRO_0000143892"
FT REGION 22..27
FT /note="Involved in allosteric activation by GTP"
FT /evidence="ECO:0000255"
FT BINDING 14..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250"
FT BINDING 137..144
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 247 AA; 26703 MW; 6EDF503ED4EBFFD4 CRC64;
MKMANPKYKR ILIKLSGEAL AGERGVGIDI QTVQTIAKEI QEVHSLGIEI ALVIGGGNLW
RGEPAAEAGM DRVQADYTGM LGTVMNALVM ADSLQQVGVD TRVQTAIAMQ QVAEPYVRGR
ALRHLEKGRI VIFGAGIGSP YFSTDTTAAL RAAEIEADAI LMAKNGVDGV YNADPKKDKT
AVKFEELTHR DVINKGLRIM DSTASTLSMD NDIDLVVFNM NQPGNIKRVV FGENIGTTVS
NNIEEKE
