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Uridylate kinase (UK) (EC 2.7.4.22) (Uridine monophosphate kinase) (UMP kinase) (UMPK)

 A0A0H5ARD0_9VIBR        Unreviewed;       244 AA.
A0A0H5ARD0;
14-OCT-2015, integrated into UniProtKB/TrEMBL.
14-OCT-2015, sequence version 1.
25-OCT-2017, entry version 16.
RecName: Full=Uridylate kinase {ECO:0000256|HAMAP-Rule:MF_01220};
Short=UK {ECO:0000256|HAMAP-Rule:MF_01220};
EC=2.7.4.22 {ECO:0000256|HAMAP-Rule:MF_01220};
AltName: Full=Uridine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_01220};
Short=UMP kinase {ECO:0000256|HAMAP-Rule:MF_01220};
Short=UMPK {ECO:0000256|HAMAP-Rule:MF_01220};
Name=pyrH {ECO:0000256|HAMAP-Rule:MF_01220,
ECO:0000313|EMBL:BAR91685.1};
Vibrio algivorus.
Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
Vibrionaceae; Vibrio.
NCBI_TaxID=1667024 {ECO:0000313|EMBL:BAR91685.1};
[1] {ECO:0000313|EMBL:BAR91685.1}
NUCLEOTIDE SEQUENCE.
STRAIN=SA2 {ECO:0000313|EMBL:BAR91685.1};
Doi H., Chinen A., Fukuda H., Usuda Y.;
"Vibrio algivorus sp. nov., an alginate and agarose assimilating
bacterium isolated from the gut flora of a turban shell marine
snail.";
Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
-!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP.
{ECO:0000256|HAMAP-Rule:MF_01220, ECO:0000256|SAAS:SAAS00678169}.
-!- CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP. {ECO:0000256|HAMAP-
Rule:MF_01220, ECO:0000256|SAAS:SAAS00678158}.
-!- ENZYME REGULATION: Allosterically activated by GTP. Inhibited by
UTP. {ECO:0000256|HAMAP-Rule:MF_01220}.
-!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
pathway; UDP from UMP (UMPK route): step 1/1. {ECO:0000256|HAMAP-
Rule:MF_01220, ECO:0000256|SAAS:SAAS00678173}.
-!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01220,
ECO:0000256|SAAS:SAAS00678157}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220,
ECO:0000256|SAAS:SAAS00678159}.
-!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000256|HAMAP-
Rule:MF_01220, ECO:0000256|SAAS:SAAS00678160}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01220}.
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EMBL; LC060682; BAR91685.1; -; Genomic_DNA.
UniPathway; UPA00159; UER00275.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-EC.
GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.1160.10; -; 1.
HAMAP; MF_01220_B; PyrH_B; 1.
InterPro; IPR036393; AceGlu_kinase-like_sf.
InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
InterPro; IPR011817; Uridylate_kinase.
InterPro; IPR015963; Uridylate_kinase_bac.
Pfam; PF00696; AA_kinase; 1.
PIRSF; PIRSF005650; Uridylate_kin; 1.
SUPFAM; SSF53633; SSF53633; 1.
TIGRFAMs; TIGR02075; pyrH_bact; 1.
3: Inferred from homology;
Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_01220};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01220,
ECO:0000256|SAAS:SAAS00678168};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01220,
ECO:0000256|SAAS:SAAS00678172};
Kinase {ECO:0000256|HAMAP-Rule:MF_01220,
ECO:0000256|SAAS:SAAS00678165};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01220,
ECO:0000256|SAAS:SAAS00678168};
Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01220,
ECO:0000256|SAAS:SAAS00678167};
Transferase {ECO:0000256|HAMAP-Rule:MF_01220,
ECO:0000256|SAAS:SAAS00678165}.
DOMAIN 11 219 AA_kinase. {ECO:0000259|Pfam:PF00696}.
NP_BIND 15 18 ATP. {ECO:0000256|HAMAP-Rule:MF_01220}.
NP_BIND 138 145 UMP. {ECO:0000256|HAMAP-Rule:MF_01220}.
REGION 23 28 Involved in allosteric activation by GTP.
{ECO:0000256|HAMAP-Rule:MF_01220}.
BINDING 57 57 UMP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01220}.
BINDING 58 58 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01220}.
BINDING 62 62 ATP. {ECO:0000256|HAMAP-Rule:MF_01220}.
BINDING 77 77 UMP. {ECO:0000256|HAMAP-Rule:MF_01220}.
BINDING 165 165 ATP. {ECO:0000256|HAMAP-Rule:MF_01220}.
BINDING 171 171 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_01220}.
BINDING 174 174 ATP. {ECO:0000256|HAMAP-Rule:MF_01220}.
SEQUENCE 244 AA; 26305 MW; C107D199E1240F94 CRC64;
MTTNPKPAYQ RILLKLSGEA LQGEEGFGID PAILDRMAQE IKELVELGVQ VGVVIGGGNL
FRGAGLAEAG MNRVVGDHMG MLATVMNGLA MRDALHRAYV NARVMSAIQL KGVCDDYNWA
DAISQLRQGR VVIFSAGTGN PFFTTDSAAC LRGIEIEADI VLKATKVDGV YTADPVANPD
AVLCDKLSYN SVLEKELKVM DLAAFTLARD HKMPIRVFNM NKPGALRRVV MGEQEGTLIG
ELPE


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