PYRH_SACS2
ID PYRH_SACS2 Reviewed; 227 AA.
AC Q97ZE2;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Uridylate kinase;
DE Short=UK;
DE EC=2.7.4.22;
DE AltName: Full=Uridine monophosphate kinase;
DE Short=UMP kinase;
DE Short=UMPK;
GN Name=pyrH; OrderedLocusNames=SSO0976;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-227 IN COMPLEX WITH UMP; ATP
RP ANALOG AND UTP, FUNCTION, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=17297917; DOI=10.1021/bi0618159;
RA Jensen K.S., Johansson E., Jensen K.F.;
RT "Structural and enzymatic investigation of the Sulfolobus solfataricus
RT uridylate kinase shows competitive UTP inhibition and the lack of GTP
RT stimulation.";
RL Biochemistry 46:2745-2757(2007).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP, with
CC ATP as the most efficient phosphate donor. Is also able to
CC phosphorylate dUMP, although much less efficiently.
CC {ECO:0000269|PubMed:17297917}.
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 -!- ACTIVITY REGULATION: Unlike most bacteria, is not activated by GTP. UTP
CC acts as a competitive inhibitor against both substrates. High
CC concentration of UMP abolishes the inhibition of UTP at low ATP
CC concentrations, indicating that UTP binds to the acceptor site (UMP
CC site). {ECO:0000269|PubMed:17297917}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for UMP (at pH 7.2) {ECO:0000269|PubMed:17297917};
CC KM=81 uM for ATP (at pH 7.2) {ECO:0000269|PubMed:17297917};
CC Vmax=5 umol/min/mg enzyme (at pH 5.5) {ECO:0000269|PubMed:17297917};
CC Vmax=45 umol/min/mg enzyme (at pH 7.2) {ECO:0000269|PubMed:17297917};
CC Vmax=12 umol/min/mg enzyme (at pH 8.5) {ECO:0000269|PubMed:17297917};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:17297917};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC UDP from UMP (UMPK route): step 1/1.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:17297917}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Catalysis proceeds by a sequential bi-bi reaction
CC mechanism of random order.
CC -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006641; AAK41250.1; -; Genomic_DNA.
DR PIR; C90249; C90249.
DR PDB; 2J4J; X-ray; 2.10 A; A/B/C/D/E/F=2-227.
DR PDB; 2J4K; X-ray; 2.20 A; A/B/C/D/E/F=2-227.
DR PDB; 2J4L; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-227.
DR PDBsum; 2J4J; -.
DR PDBsum; 2J4K; -.
DR PDBsum; 2J4L; -.
DR AlphaFoldDB; Q97ZE2; -.
DR SMR; Q97ZE2; -.
DR STRING; 273057.SSO0976; -.
DR DNASU; 1455217; -.
DR EnsemblBacteria; AAK41250; AAK41250; SSO0976.
DR KEGG; sso:SSO0976; -.
DR PATRIC; fig|273057.12.peg.975; -.
DR eggNOG; arCOG00858; Archaea.
DR HOGENOM; CLU_079546_0_0_2; -.
DR InParanoid; Q97ZE2; -.
DR OMA; MGGTHPG; -.
DR PhylomeDB; Q97ZE2; -.
DR BRENDA; 2.7.4.22; 6163.
DR UniPathway; UPA00159; UER00275.
DR EvolutionaryTrace; Q97ZE2; -.
DR Proteomes; UP000001974; 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; 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; cd04253; AAK_UMPK-PyrH-Pf; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR HAMAP; MF_01220_A; PyrH_A; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR011817; Uridylate_kinase.
DR InterPro; IPR011818; Uridylate_kinase_arch/spir.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF005650; Uridylate_kin; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR02076; pyrH_arch; 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..227
FT /note="Uridylate kinase"
FT /id="PRO_0000143927"
FT BINDING 7..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 44
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000269|PubMed:17297917"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 66
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000269|PubMed:17297917"
FT BINDING 114..120
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000269|PubMed:17297917"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2J4J"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:2J4J"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:2J4J"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2J4J"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:2J4J"
FT HELIX 62..84
FT /evidence="ECO:0007829|PDB:2J4J"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:2J4J"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:2J4J"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:2J4J"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:2J4J"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2J4J"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2J4J"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:2J4J"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2J4J"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:2J4J"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:2J4K"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:2J4J"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2J4J"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:2J4J"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:2J4J"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:2J4J"
SQ SEQUENCE 227 AA; 25120 MW; 25FB40F5D19B34F2 CRC64;
MMNIILKISG KFFDEDNVDN LIVLRQSIKE LADNGFRVGI VTGGGSTARR YIKLAREIGI
GEAYLDLLGI WASRLNAYLV MFSLQDLAYM HVPQSLEEFI QDWSHGKVVV TGGFQPGQST
AAVAALVAEA SSSKTLVVAT NVDGVYEKDP RIYADVKLIP HLTTQDLRKI LEGSQSVQAG
TYELLDPLAI KIVERSKIRV IVMNYRKLNR IIDILKGEEV SSIIEPV
