GLND_CUPMC
ID GLND_CUPMC Reviewed; 857 AA.
AC Q1LNG0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UTase/UR {ECO:0000255|HAMAP-Rule:MF_00277};
DE AltName: Full=Bifunctional [protein-PII] modification enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE AltName: Full=Bifunctional nitrogen sensor protein {ECO:0000255|HAMAP-Rule:MF_00277};
DE Includes:
DE RecName: Full=[Protein-PII] uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=PII uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UTase {ECO:0000255|HAMAP-Rule:MF_00277};
DE EC=2.7.7.59 {ECO:0000255|HAMAP-Rule:MF_00277};
DE Includes:
DE RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UR {ECO:0000255|HAMAP-Rule:MF_00277};
DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_00277};
GN Name=glnD {ECO:0000255|HAMAP-Rule:MF_00277}; OrderedLocusNames=Rmet_1433;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
CC -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC regulatory proteins (GlnB and homologs), in response to the nitrogen
CC status of the cell that GlnD senses through the glutamine level. Under
CC low glutamine levels, catalyzes the conversion of the PII proteins and
CC UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD
CC hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls
CC uridylylation state and activity of the PII proteins, and plays an
CC important role in the regulation of nitrogen assimilation and
CC metabolism. {ECO:0000255|HAMAP-Rule:MF_00277}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-
CC tyrosine + diphosphate; Xref=Rhea:RHEA:13673, Rhea:RHEA-COMP:12147,
CC Rhea:RHEA-COMP:12148, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:90602; EC=2.7.7.59;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-L-
CC tyrosine + H(+) + UMP; Xref=Rhea:RHEA:48600, Rhea:RHEA-COMP:12147,
CC Rhea:RHEA-COMP:12148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:57865, ChEBI:CHEBI:90602;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277};
CC -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is inhibited
CC by glutamine, while glutamine activates uridylyl-removing (UR)
CC activity. {ECO:0000255|HAMAP-Rule:MF_00277}.
CC -!- DOMAIN: Has four distinct domains: an N-terminal nucleotidyltransferase
CC (NT) domain responsible for UTase activity, a central HD domain that
CC encodes UR activity, and two C-terminal ACT domains that seem to have a
CC role in glutamine sensing. {ECO:0000255|HAMAP-Rule:MF_00277}.
CC -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000255|HAMAP-
CC Rule:MF_00277}.
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DR EMBL; CP000352; ABF08316.1; -; Genomic_DNA.
DR RefSeq; WP_011516184.1; NC_007973.1.
DR AlphaFoldDB; Q1LNG0; -.
DR SMR; Q1LNG0; -.
DR STRING; 266264.Rmet_1433; -.
DR EnsemblBacteria; ABF08316; ABF08316; Rmet_1433.
DR KEGG; rme:Rmet_1433; -.
DR eggNOG; COG2844; Bacteria.
DR HOGENOM; CLU_012833_0_0_4; -.
DR OMA; WIAKYVY; -.
DR OrthoDB; 162558at2; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-UniRule.
DR CDD; cd00077; HDc; 1.
DR HAMAP; MF_00277; PII_uridylyl_transf; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR010043; UTase/UR.
DR PANTHER; PTHR47320; PTHR47320; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR PIRSF; PIRSF006288; PII_uridyltransf; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Multifunctional enzyme; Nucleotidyltransferase;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..857
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_1000078810"
FT DOMAIN 441..563
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 680..760
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 788..857
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..322
FT /note="Uridylyltransferase"
FT REGION 323..679
FT /note="Uridylyl-removing"
SQ SEQUENCE 857 AA; 97774 MW; 0BFF1E5B9F7498A8 CRC64;
MDTTPELLLC QRIRDKLKAD KQVLFAEFDA NNQVNPLVTK LRRAVDVALT EAWTGLELPG
DVALVAVGGY GRGELFPHSD VDVLLLLPGE PDAKMAAKLE RFIGLCWDLG LEIGSSVRTV
DDCIRESAAD ITIRTSLLEA RLLIGNKALF KSLQTRYQAD MDAADFFQAK LLEMRQRHAK
YQDTPYALEP NCKESPGGLR DLQVILWMTE AARLGDSWKQ LFERGLLTER EAQELTRNER
LLRTIRARLH LLAGRRQDVL VFDLQTALAE AFGYRQTTNK RASEQLMRRY YWAAKAVTQL
NSVLLLNIEA MLFPSESMVT REINDRFVER QGMLEITSDD LYERNPHAIL ETFLLYERTP
GVKGLSPRTL RGLYNARTVM DASWRNDPVN RRLFLAIVQE PQGITHALRL MNQTSVLGRY
LINFRRIVGQ MQHDLFHVYT VDQHILMVVR NMRRFAIVEH THEFPFCSQL MAGFDRPWVL
WVAALFHDIA KGRGGDHSKL GTVDARRFCK QHGISREDTD LIAWLVEHHL TMSHVAQKQD
LTDPDVVKAF AQVVGNGRYL TALYLLTVAD IRGTSPKVWN AWKGKLLEDL YRITLRVLGG
ARLDTHSLWA QKRDDTIAQL RLKAFDPELA KPLWDKLDMS FFMRQDARDI AWLTRSLFNK
VNSPNPVVKA RISPAGEGLQ VAVYVKDQPD LFARICGYFE RKAFSIQDAK IETTRDGYAL
DTFQITDPGL AGDYRDILTL VEHELGERVR LECPLPDPTQ GRLSRQSRSF PIKPRVDLRP
DERGQYYLLS VSANDRTGLL YAIARVLAKH RVSVHSARIN TLGERVEDVF LVDGSRLAAD
NRLQIQLEQD LLDALAI
