(data stored in ACNUC7421 zone)

SWISSPROT: PYRH_RHILO

ID   PYRH_RHILO              Reviewed;         240 AA.
AC   Q98MB7;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   11-DEC-2019, entry version 99.
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}; OrderedLocusNames=mll0643;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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=BAB48196.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BA000012; BAB48196.1; ALT_INIT; Genomic_DNA.
DR   SMR; Q98MB7; -.
DR   STRING; 266835.14021584; -.
DR   EnsemblBacteria; BAB48196; BAB48196; BAB48196.
DR   KEGG; mlo:mll0643; -.
DR   eggNOG; ENOG4105C41; Bacteria.
DR   eggNOG; COG0528; LUCA.
DR   HOGENOM; HOG000047187; -.
DR   KO; K09903; -.
DR   BioCyc; MLOT266835:G1G20-531-MONOMER; -.
DR   UniPathway; UPA00159; UER00275.
DR   Proteomes; UP000000552; 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   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;
DR   PRODOM; Q98MB7.
DR   SWISS-2DPAGE; Q98MB7.
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..240
FT                   /note="Uridylate kinase"
FT                   /id="PRO_0000143874"
FT   NP_BIND         13..16
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   NP_BIND         136..143
FT                   /note="UMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         55
FT                   /note="UMP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         56
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         60
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         75
FT                   /note="UMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         163
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         164
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         169
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT   BINDING         172
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
SQ   SEQUENCE   240 AA;  25184 MW;  ADA162788F78F178 CRC64;
     MTVKPLYRRV LLKASGEALM GEQHFGIDVS VVDRIAADIA EARGLGIEVG VVIGGGNIFR
     GVAVASKGGD RVTGDHMGML ATVINSLALR TSLHKIGVDA VVLSAIAMPE LCESFSQRQA
     DAYMNQGRVV IFAGGTGNPF FTTDSAAALR AAEIGADALF KGTQVDGVYS ADPKKDPNAT
     RFERISHAEV INRGLSIMDT AAIALARENN IPIIVYSIHE KGGFGDILRG GGRCTVVADD
//

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