ID A0A1G9G515_9RHOB Unreviewed; 255 AA.
AC A0A1G9G515;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ORFNames=SAMN05216257_106103 {ECO:0000313|EMBL:SDK95804.1};
OS Meinhardsimonia xiamenensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Meinhardsimonia.
OX NCBI_TaxID=990712 {ECO:0000313|EMBL:SDK95804.1, ECO:0000313|Proteomes:UP000199328};
RN [1] {ECO:0000313|Proteomes:UP000199328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10789 {ECO:0000313|Proteomes:UP000199328};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FNFV01000006; SDK95804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9G515; -.
DR STRING; 990712.SAMN05216257_106103; -.
DR OrthoDB; 9807458at2; -.
DR UniPathway; UPA00159; UER00275.
DR Proteomes; UP000199328; 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|HAMAP-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:UP000199328};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01220}.
FT DOMAIN 25..233
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT REGION 37..42
FT /note="Involved in allosteric activation by GTP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 71
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 91
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 152..159
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
SQ SEQUENCE 255 AA; 27620 MW; 06E6D21808A7EE2B CRC64;
MTDTGLAAAE ELAAAKRAPA TKYRRVMLKI SGEALMGDQG YGLHPPTVER IAREVKSVHE
LGVEICMVIG GGNIFRGLSG AAQGMERTTA DYMGMLATVM NALAMQSALE GLGVFTRVIS
AIRMDEICEP YIRRRAVRHL EKKRVCIFAA GTGNPYFTTD TAATLRASEM GCEAIFKGTK
VDGVYDKDPA KFPDAKRYDE VSYDEVLQKN LKVMDASAIA LARDNDKPII VFSLDEPGGF
RGILSGEGTY TLVHG
//
