PYRH_MYCTU
ID PYRH_MYCTU Reviewed; 261 AA.
AC P9WHK5; L0TAX5; P65929; Q10791;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
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=Rv2883c;
GN ORFNames=MTCY274.14c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP45685.1; -; Genomic_DNA.
DR PIR; F70924; F70924.
DR RefSeq; NP_217399.1; NC_000962.3.
DR RefSeq; WP_003414665.1; NZ_NVQJ01000006.1.
DR PDB; 3NWY; X-ray; 2.54 A; A/B/C/D/E/F=1-261.
DR PDB; 7BIX; X-ray; 3.12 A; A/B/C/D/E/F/G/H/I/J/K/L=1-261.
DR PDB; 7BL7; X-ray; 3.33 A; A/B/C/D/E/F/G/H/I/J/K/L=1-261.
DR PDBsum; 3NWY; -.
DR PDBsum; 7BIX; -.
DR PDBsum; 7BL7; -.
DR AlphaFoldDB; P9WHK5; -.
DR SMR; P9WHK5; -.
DR STRING; 83332.Rv2883c; -.
DR iPTMnet; P9WHK5; -.
DR PaxDb; P9WHK5; -.
DR DNASU; 887709; -.
DR GeneID; 45426871; -.
DR GeneID; 887709; -.
DR KEGG; mtu:Rv2883c; -.
DR TubercuList; Rv2883c; -.
DR eggNOG; COG0528; Bacteria.
DR OMA; PIIVFDM; -.
DR PhylomeDB; P9WHK5; -.
DR BRENDA; 2.7.4.22; 3445.
DR UniPathway; UPA00159; UER00275.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0033862; F:UMP kinase activity; IDA:MTBBASE.
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; IDA:MTBBASE.
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; Acetylation; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..261
FT /note="Uridylate kinase"
FT /id="PRO_0000143863"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 77
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 97
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 158..165
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01220"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3NWY"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:3NWY"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3NWY"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:3NWY"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:3NWY"
FT TURN 86..90
FT /evidence="ECO:0007829|PDB:3NWY"
FT HELIX 93..117
FT /evidence="ECO:0007829|PDB:3NWY"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:3NWY"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3NWY"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3NWY"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:3NWY"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3NWY"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:3NWY"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:3NWY"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3NWY"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:3NWY"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:3NWY"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:3NWY"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3NWY"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:3NWY"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:3NWY"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:3NWY"
SQ SEQUENCE 261 AA; 27430 MW; D6CDFD6ACF59BCF3 CRC64;
MTEPDVAGAP ASKPEPASTG AASAAQLSGY SRVLLKLGGE MFGGGQVGLD PDVVAQVARQ
IADVVRGGVQ IAVVIGGGNF FRGAQLQQLG MERTRSDYMG MLGTVMNSLA LQDFLEKEGI
VTRVQTAITM GQVAEPYLPL RAVRHLEKGR VVIFGAGMGL PYFSTDTTAA QRALEIGADV
VLMAKAVDGV FAEDPRVNPE AELLTAVSHR EVLDRGLRVA DATAFSLCMD NGMPILVFNL
LTDGNIARAV RGEKIGTLVT T
