PYRH_HAEIN
ID PYRH_HAEIN Reviewed; 237 AA.
AC P43890;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
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; Synonyms=smbA; OrderedLocusNames=HI_1065;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, KINETIC PARAMETERS, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBUNIT.
RX PubMed=17210578; DOI=10.1074/jbc.m606963200;
RA Evrin C., Straut M., Slavova-Azmanova N., Bucurenci N., Onu A., Assairi L.,
RA Ionescu M., Palibroda N., Barzu O., Gilles A.-M.;
RT "Regulatory mechanisms differ in UMP kinases from Gram-negative and Gram-
RT positive bacteria.";
RL J. Biol. Chem. 282:7242-7253(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-237.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of uridylate kinase.";
RL Submitted (JUN-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
CC {ECO:0000269|PubMed:17210578}.
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: Allosterically activated by GTP. Inhibited by UTP.
CC {ECO:0000269|PubMed:17210578}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.57 mM for ATP (in the absence of GTP)
CC {ECO:0000269|PubMed:17210578};
CC KM=0.46 mM for ATP (in the presence of GTP)
CC {ECO:0000269|PubMed:17210578};
CC KM=40 uM for UMP {ECO:0000269|PubMed:17210578};
CC Vmax=57 umol/min/mg enzyme {ECO:0000269|PubMed:17210578};
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:17210578}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000305}.
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DR EMBL; L42023; AAC22719.1; -; Genomic_DNA.
DR PIR; H64180; H64180.
DR RefSeq; NP_439223.1; NC_000907.1.
DR RefSeq; WP_005693391.1; NC_000907.1.
DR PDB; 2A1F; X-ray; 2.10 A; A/B/C/D/E/F=2-237.
DR PDBsum; 2A1F; -.
DR AlphaFoldDB; P43890; -.
DR SMR; P43890; -.
DR STRING; 71421.HI_1065; -.
DR DNASU; 950042; -.
DR EnsemblBacteria; AAC22719; AAC22719; HI_1065.
DR KEGG; hin:HI_1065; -.
DR PATRIC; fig|71421.8.peg.1109; -.
DR eggNOG; COG0528; Bacteria.
DR HOGENOM; CLU_033861_0_0_6; -.
DR OMA; PIIVFDM; -.
DR PhylomeDB; P43890; -.
DR BioCyc; HINF71421:G1GJ1-1101-MON; -.
DR SABIO-RK; P43890; -.
DR UniPathway; UPA00159; UER00275.
DR EvolutionaryTrace; P43890; -.
DR Proteomes; UP000000579; 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; Allosteric enzyme; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..237
FT /note="Uridylate kinase"
FT /id="PRO_0000143847"
FT REGION 20..25
FT /note="Involved in allosteric activation by GTP"
FT /evidence="ECO:0000255"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250"
FT BINDING 135..142
FT /ligand="UMP"
FT /ligand_id="ChEBI:CHEBI:57865"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:2A1F"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:2A1F"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:2A1F"
FT HELIX 28..42
FT /evidence="ECO:0007829|PDB:2A1F"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2A1F"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2A1F"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:2A1F"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:2A1F"
FT HELIX 70..94
FT /evidence="ECO:0007829|PDB:2A1F"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2A1F"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2A1F"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2A1F"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:2A1F"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:2A1F"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:2A1F"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:2A1F"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2A1F"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:2A1F"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:2A1F"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:2A1F"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:2A1F"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:2A1F"
SQ SEQUENCE 237 AA; 25726 MW; FDB0D6CE2CBCDCE3 CRC64;
MSQPIYKRIL LKLSGEALQG EDGLGIDPAI LDRMAVEIKE LVEMGVEVSV VLGGGNLFRG
AKLAKAGMNR VVGDHMGMLA TVMNGLAMRD SLFRADVNAK LMSAFQLNGI CDTYNWSEAI
KMLREKRVVI FSAGTGNPFF TTDSTACLRG IEIEADVVLK ATKVDGVYDC DPAKNPDAKL
YKNLSYAEVI DKELKVMDLS AFTLARDHGM PIRVFNMGKP GALRQVVTGT EEGTTIC
