PYRH_STRP1
ID PYRH_STRP1 Reviewed; 242 AA.
AC P65938; P59007; Q490H1; Q490H2; Q490H3; Q9A151;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
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};
GN OrderedLocusNames=SPy_0462, M5005_Spy0377;
GN ORFNames=M5005_Spy0378, M5005_Spy0379;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [3]
RP SEQUENCE REVISION.
RA Beres S.B., Musser J.M.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-242.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of a putative uridylate kinase (UMP-kinase) from
RT Streptococcus pyogenes.";
RL Submitted (APR-2005) to the PDB data bank.
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: Allosterically activated by GTP. Inhibited by UTP.
CC {ECO:0000255|HAMAP-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; AE004092; AAK33476.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ50995.2; -; Genomic_DNA.
DR RefSeq; NP_268755.1; NC_002737.2.
DR PDB; 1Z9D; X-ray; 2.80 A; A/B/C=2-242.
DR PDBsum; 1Z9D; -.
DR AlphaFoldDB; P65938; -.
DR SMR; P65938; -.
DR STRING; 1314.HKU360_00408; -.
DR PaxDb; P65938; -.
DR EnsemblBacteria; AAK33476; AAK33476; SPy_0462.
DR KEGG; spy:SPy_0462; -.
DR KEGG; spz:M5005_Spy0377; -.
DR PATRIC; fig|160490.10.peg.390; -.
DR HOGENOM; CLU_033861_0_0_9; -.
DR OMA; PIIVFDM; -.
DR UniPathway; UPA00159; UER00275.
DR EvolutionaryTrace; P65938; -.
DR Proteomes; UP000000750; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; Allosteric enzyme; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..242
FT /note="Uridylate kinase"
FT /id="PRO_0000143894"
FT REGION 19..24
FT /note="Involved in allosteric activation by GTP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 11..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 53
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 73
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 134..141
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 STRAND 6..12
FT /evidence="ECO:0007829|PDB:1Z9D"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:1Z9D"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:1Z9D"
FT HELIX 27..41
FT /evidence="ECO:0007829|PDB:1Z9D"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1Z9D"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1Z9D"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1Z9D"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:1Z9D"
FT HELIX 69..92
FT /evidence="ECO:0007829|PDB:1Z9D"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1Z9D"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1Z9D"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1Z9D"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1Z9D"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:1Z9D"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1Z9D"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:1Z9D"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:1Z9D"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1Z9D"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:1Z9D"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1Z9D"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:1Z9D"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1Z9D"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:1Z9D"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1Z9D"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:1Z9D"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1Z9D"
SQ SEQUENCE 242 AA; 25896 MW; B4517145A5160433 CRC64;
MEPKYQRILI KLSGEALAGE KGVGIDIPTV QAIAKEIAEV HVSGVQIALV IGGGNLWRGE
PAADAGMDRV QADYTGMLGT VMNALVMADS LQHYGVDTRV QTAIPMQNVA EPYIRGRALR
HLEKNRIVVF GAGIGSPYFS TDTTAALRAA EIEADAILMA KNGVDGVYNA DPKKDANAVK
FDELTHGEVI KRGLKIMDAT ASTLSMDNDI DLVVFNMNEA GNIQRVVFGE HIGTTVSNKV
CD
