PYRH_BORA1
ID PYRH_BORA1 Reviewed; 238 AA.
AC Q2L160;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
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}; Synonyms=smbA;
GN OrderedLocusNames=BAV1736;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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: Inhibited by UTP. {ECO:0000255|HAMAP-
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ49344.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM167904; CAJ49344.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_039051757.1; NC_010645.1.
DR AlphaFoldDB; Q2L160; -.
DR SMR; Q2L160; -.
DR STRING; 360910.BAV1736; -.
DR EnsemblBacteria; CAJ49344; CAJ49344; BAV1736.
DR GeneID; 41393587; -.
DR KEGG; bav:BAV1736; -.
DR eggNOG; COG0528; Bacteria.
DR HOGENOM; CLU_033861_0_0_4; -.
DR OrthoDB; 1043239at2; -.
DR UniPathway; UPA00159; UER00275.
DR Proteomes; UP000001977; 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 ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..238
FT /note="Uridylate kinase"
FT /id="PRO_0000323797"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 54
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 74
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 135..142
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 168
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"
SQ SEQUENCE 238 AA; 25571 MW; F38A0CF6156439F2 CRC64;
MSSRSYKRVL LKLSGEALMG DDAFGINRST IVRMTDEIAE VAAMGVELAI VIGGGNIFRG
VAPGAQGMDR ATADYMGMMA TIMNALALQD ALKHKGLDTR VQSALNIDQV VEPYIRPKTL
RYLEEGKVVI FAAGTGNPFF TTDTAAALRG AEIGAEIVLK ATKVDGIYSA DPNKDPTATR
YARISFDEAI VRRLEVMDAT AFALCRDQKL PIKVFSINKS GALKRVVGGE DEGTLVHV
