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Database: UniProt
Entry: A0A1T1AMV1_RHOFE
LinkDB: A0A1T1AMV1_RHOFE
Original site: A0A1T1AMV1_RHOFE 
ID   A0A1T1AMV1_RHOFE        Unreviewed;       240 AA.
AC   A0A1T1AMV1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=RF819_01030 {ECO:0000313|EMBL:OOV05476.1};
OS   Rhodoferax fermentans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=28066 {ECO:0000313|EMBL:OOV05476.1, ECO:0000313|Proteomes:UP000190750};
RN   [1] {ECO:0000313|EMBL:OOV05476.1, ECO:0000313|Proteomes:UP000190750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7819 {ECO:0000313|EMBL:OOV05476.1,
RC   ECO:0000313|Proteomes:UP000190750};
RA   Kim Y.J., Farh M.E.-A., Yang D.-C.;
RT   "Genome sequencing of Rhodoferax fermentans JCM 7819.";
RL   Submitted (JAN-2017) 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}.
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:OOV05476.1}.
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DR   EMBL; MTJN01000002; OOV05476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1AMV1; -.
DR   STRING; 28066.RF819_01030; -.
DR   OrthoDB; 9807458at2; -.
DR   UniPathway; UPA00159; UER00275.
DR   Proteomes; UP000190750; 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}; Reference proteome {ECO:0000313|Proteomes:UP000190750};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01220}.
FT   DOMAIN          9..218
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   BINDING         14..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         56
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         76
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         137..144
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
FT   BINDING         173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01220"
SQ   SEQUENCE   240 AA;  25549 MW;  7B4DD5E3FA3F13AC CRC64;
     MTTAKPAYKR ILLKLSGEAL MGDDQFGINR NTIVRMVDEI VEVTRLGVEV AVVIGGGNIF
     RGVAGGSVGM DRATADYMGM LATVMNSLAL GDTMNKAGLT ARVMSAIAIE QVVEPYVRPK
     ALQYLEEGKV VIFAAGTGNP FFTTDTAAAL RGAEIGAQIV LKATKVDGVY SADPKKDPTA
     TRYSKISFDD AISQNLGIMD ATAFALCRDQ KLPIKVFSIF KNGALKRVVL GEDEGTLVYA
//
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