ID A0A0C3AGM8_9LACO Unreviewed; 240 AA.
AC A0A0C3AGM8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Uridylate kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE Short=UK {ECO:0000256|HAMAP-Rule:MF_01220};
DE EC=2.7.4.22 {ECO:0000256|HAMAP-Rule:MF_01220};
DE AltName: Full=Uridine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE Short=UMP kinase {ECO:0000256|HAMAP-Rule:MF_01220};
DE Short=UMPK {ECO:0000256|HAMAP-Rule:MF_01220};
GN Name=pyrH {ECO:0000256|HAMAP-Rule:MF_01220,
GN ECO:0000313|EMBL:KOY79159.1};
GN ORFNames=FF306_00106 {ECO:0000313|EMBL:GAT90015.1}, RZ71_07880
GN {ECO:0000313|EMBL:KOY76338.1}, RZ72_13170
GN {ECO:0000313|EMBL:KOY79159.1}, RZ78_13060
GN {ECO:0000313|EMBL:KPN82194.1};
OS Apilactobacillus kunkeei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Apilactobacillus.
OX NCBI_TaxID=148814 {ECO:0000313|EMBL:KOY79159.1, ECO:0000313|Proteomes:UP000037749};
RN [1] {ECO:0000313|Proteomes:UP000037749, ECO:0000313|Proteomes:UP000037778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAko {ECO:0000313|EMBL:KOY76338.1,
RC ECO:0000313|Proteomes:UP000037778}, LAla {ECO:0000313|EMBL:KOY79159.1,
RC ECO:0000313|Proteomes:UP000037749}, and LMbo
RC {ECO:0000313|EMBL:KPN82194.1, ECO:0000313|Proteomes:UP000050269};
RX PubMed=25953738; DOI=10.1093/gbe/evv079;
RA Tamarit D., Ellegaard K.M., Wikander J., Olofsson T., Vasquez A.,
RA Andersson S.G.;
RT "Functionally Structured Genomes in Lactobacillus kunkeei Colonizing the
RT Honey Crop and Food Products of Honeybees and Stingless Bees.";
RL Genome Biol. Evol. 7:1455-1473(2015).
RN [2] {ECO:0000313|EMBL:GAT90015.1, ECO:0000313|Proteomes:UP000186588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF30-6 {ECO:0000313|EMBL:GAT90015.1,
RC ECO:0000313|Proteomes:UP000186588};
RX PubMed=27776911; DOI=10.1016/j.syapm.2016.09.006;
RA Maeno S., Tanizawa Y., Kanesaki Y., Kubota E., Kumar H., Dicks L.,
RA Salminen S., Nakagawa J., Arita M., Endo A.;
RT "Genomic characterization of a fructophilic bee symbiont Lactobacillus
RT kunkeei reveals its niche-specific adaptation.";
RL Syst. Appl. Microbiol. 39:516-526(2016).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC {ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001018, ECO:0000256|HAMAP-
CC Rule:MF_01220};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. Inhibited by UTP.
CC {ECO:0000256|HAMAP-Rule:MF_01220}.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC UDP from UMP (UMPK route): step 1/1. {ECO:0000256|ARBA:ARBA00004791,
CC ECO:0000256|HAMAP-Rule:MF_01220}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01220}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220}.
CC -!- SIMILARITY: Belongs to the UMP kinase family.
CC {ECO:0000256|ARBA:ARBA00007614, ECO:0000256|HAMAP-Rule:MF_01220}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01220}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOY79159.1}.
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DR EMBL; BDDX01000001; GAT90015.1; -; Genomic_DNA.
DR EMBL; JXCY01000006; KOY76338.1; -; Genomic_DNA.
DR EMBL; JXCZ01000019; KOY79159.1; -; Genomic_DNA.
DR EMBL; JXDF01000017; KPN82194.1; -; Genomic_DNA.
DR RefSeq; WP_041152361.1; NZ_VBSE01000043.1.
DR PATRIC; fig|148814.13.peg.838; -.
DR OrthoDB; 9807458at2; -.
DR UniPathway; UPA00159; UER00275.
DR Proteomes; UP000037749; Unassembled WGS sequence.
DR Proteomes; UP000037778; Unassembled WGS sequence.
DR Proteomes; UP000050269; Unassembled WGS sequence.
DR Proteomes; UP000186588; Unassembled WGS sequence.
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; Acetylglutamate kinase-like; 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 NCBIfam; TIGR02075; pyrH_bact; 1.
DR PANTHER; PTHR42833; URIDYLATE KINASE; 1.
DR PANTHER; PTHR42833:SF4; URIDYLATE KINASE PUMPKIN, CHLOROPLASTIC; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF005650; Uridylate_kin; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW Rule:MF_01220};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01220};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01220};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01220};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01220};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_01220}; Reference proteome {ECO:0000313|Proteomes:UP000037778};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01220}.
FT DOMAIN 7..217
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT REGION 20..25
FT /note="Involved in allosteric activation by GTP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 54
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 74
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 135..142
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
SQ SEQUENCE 240 AA; 26001 MW; 14370A5B2F00AD87 CRC64;
MSDLKYKRIV LKLSGEALAG DEGHGINPPV IKKIAQEVKN VYELGIQIAI VVGGGNMWRG
VAGSKMGMER TQADYIGMLA TVMNGLALQE NLESLGVPTR VQTSIEMRQI AEPYIRRKAV
RHLEKNRVVI FSGGTGNPFF STDTTAALRA AEVHADAILM AKNGVDGIYS ADPNKDPNAV
KFDELTQMDI INKNLQVMDT TASSLSMDND IPLVVFNLNE SGNIEKVVKG EKIGTTVKGK
//
