PYRH_SULDN
ID PYRH_SULDN Reviewed; 237 AA.
AC Q30SN5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Uridylate kinase {ECO:0000255|HAMAP-Rule:MF_01220};
DE Short=UK {ECO:0000255|HAMAP-Rule:MF_01220};
DE EC=2.7.4.22 {ECO:0000255|HAMAP-Rule:MF_01220};
DE AltName: Full=Uridine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_01220};
DE Short=UMP kinase {ECO:0000255|HAMAP-Rule:MF_01220};
DE Short=UMPK {ECO:0000255|HAMAP-Rule:MF_01220};
GN Name=pyrH {ECO:0000255|HAMAP-Rule:MF_01220}; OrderedLocusNames=Suden_0717;
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Thiovulaceae; Sulfurimonas.
OX NCBI_TaxID=326298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251;
RX PubMed=18065616; DOI=10.1128/aem.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(2008).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01220};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by UTP.
CC {ECO:0000255|HAMAP-Rule:MF_01220}.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC UDP from UMP (UMPK route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01220}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01220}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01220}.
CC -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_01220}.
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DR EMBL; CP000153; ABB43996.1; -; Genomic_DNA.
DR RefSeq; WP_011372350.1; NC_007575.1.
DR AlphaFoldDB; Q30SN5; -.
DR SMR; Q30SN5; -.
DR STRING; 326298.Suden_0717; -.
DR EnsemblBacteria; ABB43996; ABB43996; Suden_0717.
DR KEGG; tdn:Suden_0717; -.
DR eggNOG; COG0528; Bacteria.
DR HOGENOM; CLU_033861_0_0_7; -.
DR OMA; PIIVFDM; -.
DR OrthoDB; 1043239at2; -.
DR UniPathway; UPA00159; UER00275.
DR Proteomes; UP000002714; 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 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..237
FT /note="Uridylate kinase"
FT /id="PRO_0000323961"
FT REGION 17..22
FT /note="Involved in allosteric activation by GTP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 9..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 51
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 72
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 133..140
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
SQ SEQUENCE 237 AA; 25636 MW; AF2275F66E1C4F23 CRC64;
MANKRVLVKF SGEALAGEAG YGIDTKILNF ISQEIKSLVE ANIEVGIVIG GGNIIRGVTA
AQDGIIKRTS GDYMGMLATV INGIAMQEAC EHAGLQVRMQ TAIKMEQIAE PYINRRAVRH
LEKGRVVIFA AGTGNPFFTT DTAATLRAVE IGAEVIIKAT KVDGVYDKDP NKFSDAIKLQ
ELSYEQALND NIKVMDDTSI ALAKDNSLPI LVCDMFKKGN LLDILQNGNM KNCSIVK
