PYRH_XANCP
ID PYRH_XANCP Reviewed; 240 AA.
AC P59009;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=XCC1371;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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}.
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DR EMBL; AE008922; AAM40669.1; -; Genomic_DNA.
DR RefSeq; NP_636745.1; NC_003902.1.
DR RefSeq; WP_011036563.1; NC_003902.1.
DR PDB; 3EK5; X-ray; 2.56 A; A/B/C/D/E/F=1-240.
DR PDB; 3EK6; X-ray; 2.34 A; A/B/C/D/E/F=1-240.
DR PDBsum; 3EK5; -.
DR PDBsum; 3EK6; -.
DR AlphaFoldDB; P59009; -.
DR SMR; P59009; -.
DR STRING; 340.xcc-b100_2925; -.
DR EnsemblBacteria; AAM40669; AAM40669; XCC1371.
DR KEGG; xcc:XCC1371; -.
DR PATRIC; fig|190485.4.peg.1473; -.
DR eggNOG; COG0528; Bacteria.
DR HOGENOM; CLU_033861_0_0_6; -.
DR OMA; PIIVFDM; -.
DR UniPathway; UPA00159; UER00275.
DR EvolutionaryTrace; P59009; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033862; F:UMP kinase activity; IBA:GO_Central.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006225; P:UDP biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..240
FT /note="Uridylate kinase"
FT /id="PRO_0000143908"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 54
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 74
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 135..142
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT HELIX 1..3
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:3EK6"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:3EK6"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:3EK6"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3EK6"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:3EK6"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3EK6"
FT HELIX 70..94
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:3EK6"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3EK6"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3EK6"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:3EK6"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3EK6"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:3EK6"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3EK6"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:3EK6"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3EK6"
SQ SEQUENCE 240 AA; 25752 MW; 66058688E59F7A9C CRC64;
MSELSYRRIL LKLSGEALMG DGDYGIDPKV INRLAHEVIE AQQAGAQVAL VIGGGNIFRG
AGLAASGMDR VTGDHMGMLA TVINALAMQD ALEKLGAKVR VMSAIKINDV CEDFIRRRAI
RHLEKGRIAI FAAGTGNPFF TTDSGAALRA IEIGADLLLK ATKVDGVYDK DPKKHSDAVR
YDSLTYDEVI MQGLEVMDTA AFALARDSDL PLRIFGMSEP GVLLRILHGA QIGTLVQGRS
