PYRH_SACD2
ID PYRH_SACD2 Reviewed; 247 AA.
AC Q21HH4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Sde_2595;
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(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; CP000282; ABD81855.1; -; Genomic_DNA.
DR RefSeq; WP_011469072.1; NC_007912.1.
DR AlphaFoldDB; Q21HH4; -.
DR SMR; Q21HH4; -.
DR STRING; 203122.Sde_2595; -.
DR EnsemblBacteria; ABD81855; ABD81855; Sde_2595.
DR KEGG; sde:Sde_2595; -.
DR eggNOG; COG0528; Bacteria.
DR HOGENOM; CLU_033861_0_0_6; -.
DR OMA; PIIVFDM; -.
DR OrthoDB; 1043239at2; -.
DR UniPathway; UPA00159; UER00275.
DR Proteomes; UP000001947; 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..247
FT /note="Uridylate kinase"
FT /id="PRO_0000323948"
FT REGION 23..28
FT /note="Involved in allosteric activation by GTP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 15..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 57
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 77
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 138..145
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
SQ SEQUENCE 247 AA; 26604 MW; 76C251FAABCF5C7F CRC64;
MPNTPDRKYK RILLKLSGEQ LMGDEGFGID PKVLDKMALE IGQLVGIGVQ VGLVIGGGNL
FRGAALSRAG LDRVTGDHMG MLATVMNALA MRDALERSNI SSTVMSAIPM HGVTDQYDRR
KALRLLDNGE VVIFSAGTGN PFFTTDSAAC LRGIEVNAEL VLKATKVDGV YSADPMKDPT
AVRYSKLTYE KVLTEQLGVM DLTAICLCQD HNMPVRVFQM DKQGALLNIV VGGDEGTLIQ
GKETEEA
