PYRH_ARCFU
ID PYRH_ARCFU Reviewed; 219 AA.
AC O28237;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=AF_2042;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of uridylate kinase from Archaeoglobus fulgidus.";
RL Submitted (OCT-2006) 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: 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; AE000782; AAB89213.1; -; Genomic_DNA.
DR PIR; A69505; A69505.
DR RefSeq; WP_010879534.1; NC_000917.1.
DR PDB; 2IJ9; X-ray; 2.90 A; A/B=1-219.
DR PDBsum; 2IJ9; -.
DR AlphaFoldDB; O28237; -.
DR SMR; O28237; -.
DR STRING; 224325.AF_2042; -.
DR EnsemblBacteria; AAB89213; AAB89213; AF_2042.
DR GeneID; 24795791; -.
DR KEGG; afu:AF_2042; -.
DR eggNOG; arCOG00858; Archaea.
DR HOGENOM; CLU_079546_0_0_2; -.
DR OMA; MGGTHPG; -.
DR OrthoDB; 48934at2157; -.
DR PhylomeDB; O28237; -.
DR UniPathway; UPA00159; UER00275.
DR EvolutionaryTrace; O28237; -.
DR Proteomes; UP000002199; 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; 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..219
FT /note="Uridylate kinase"
FT /id="PRO_0000143914"
FT BINDING 9..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 41
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 63
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 110..116
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2IJ9"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:2IJ9"
FT HELIX 16..32
FT /evidence="ECO:0007829|PDB:2IJ9"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2IJ9"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:2IJ9"
FT HELIX 59..80
FT /evidence="ECO:0007829|PDB:2IJ9"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:2IJ9"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:2IJ9"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2IJ9"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:2IJ9"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:2IJ9"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:2IJ9"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2IJ9"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:2IJ9"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:2IJ9"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2IJ9"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:2IJ9"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:2IJ9"
SQ SEQUENCE 219 AA; 23398 MW; 751B894ED5261B91 CRC64;
MKVVLSLGGS VLSNESEKIR EFAKTIESVA QQNQVFVVVG GGKLAREYIK RARELGASET
FCDYIGIAAT RLNAMLLISA IPSAAKKVPV DFMEAEELSK LYRVVVMGGT FPGHTTDATA
ALLAEFIKAD VFINATNVDG VYSADPKSDT SAVKYDRLSP QQLVEIVSRS SAKAGTNVVI
DLLAAKIIER SKIKTYVILG TPENIMKAVK GEAVGTVIA
