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Database: UniProt
Entry: A0A1M7DXF2_9FLAO
LinkDB: A0A1M7DXF2_9FLAO
Original site: A0A1M7DXF2_9FLAO 
ID   A0A1M7DXF2_9FLAO        Unreviewed;       235 AA.
AC   A0A1M7DXF2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=SAMN05444484_102770 {ECO:0000313|EMBL:SHL84182.1};
OS   Flavobacterium chilense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=946677 {ECO:0000313|EMBL:SHL84182.1, ECO:0000313|Proteomes:UP000184028};
RN   [1] {ECO:0000313|EMBL:SHL84182.1, ECO:0000313|Proteomes:UP000184028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24724 {ECO:0000313|EMBL:SHL84182.1,
RC   ECO:0000313|Proteomes:UP000184028};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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: Inhibited by UTP. {ECO:0000256|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: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; FRBT01000002; SHL84182.1; -; Genomic_DNA.
DR   RefSeq; WP_068842201.1; NZ_LSYT01000002.1.
DR   AlphaFoldDB; A0A1M7DXF2; -.
DR   STRING; 946677.SAMN05444484_102770; -.
DR   OrthoDB; 9807458at2; -.
DR   UniPathway; UPA00159; UER00275.
DR   Proteomes; UP000184028; 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:SF4; AMINO ACID KINASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR42833; URIDYLATE KINASE; 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   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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01220}.
FT   DOMAIN          4..213
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   BINDING         9..12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         51
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         56
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         132..139
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         159
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
SQ   SEQUENCE   235 AA;  25590 MW;  9DE203A9174C84F1 CRC64;
     MKYKRILLKL SGEALMGDLQ YGIDPKRLAE YAEEIKQIHS KGVEIAIVIG GGNIFRGVAG
     ASAGMDRVQG DYMGMLATVI NGMALQGALE DKGMKTRLQT ALKMESIAEP YIKRRADRHL
     EKGRIVIFGA GTGNPYFTTD TAAVLRGIEI NADVILKGTR VDGVYDSDPE KNASAIKFDM
     ISFDDVLKKG LNVMDTTAFT LSQENKLPIV VFDMNKIGNL LKICEGENIG TVVNI
//
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