GLND_YERPS
ID GLND_YERPS Reviewed; 893 AA.
AC Q667I7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=YPTB3005;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH22243.1; -; Genomic_DNA.
DR RefSeq; WP_011192863.1; NZ_CP009712.1.
DR AlphaFoldDB; Q667I7; -.
DR SMR; Q667I7; -.
DR EnsemblBacteria; CAH22243; CAH22243; YPTB3005.
DR GeneID; 66844566; -.
DR KEGG; ypo:BZ17_3616; -.
DR KEGG; yps:YPTB3005; -.
DR PATRIC; fig|273123.14.peg.3796; -.
DR OMA; WIAKYVY; -.
DR Proteomes; UP000001011; 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 Repeat; Transferase.
FT CHAIN 1..893
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000231699"
FT DOMAIN 470..592
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 711..793
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 819..893
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..351
FT /note="Uridylyltransferase"
FT REGION 352..710
FT /note="Uridylyl-removing"
SQ SEQUENCE 893 AA; 103172 MW; 8307CE87897AC85C CRC64;
MSDNHTEHSL SLTLTPTISE QPVLPSTYLD SDINCPILKQ RLDAFQRWQA EAFNSGTSAE
VLIAARSDYI DHLLQRLWTF YGFDNVPETA LVAVGGYGRG ELHPLSDIDV LVLSKQRLND
EHAQRVGQLI TLLWDLKLEV GHSVRTLEEC LLEGLADLTI ATNMIESRLI CGDVALFLQM
QKHIFSDSFW PSPQFFHAKV VEQQERHKRY HGTSYNLEPD IKSSPGGLRD IHTLLWVARR
HFGATSLSEM VDFGFLTNAE RNELNESQSF LWRIRFALHL VLTRYDNRLL FDRQLSVAQL
LRYEGEGNEP VEHMMKDFYR MTRRVSELNN MLLQLFDEAI LALEANEKPR PLDEEFQLRG
DLIDLRDENL FVRQPEAIMR MFYLMVRNQD IKGIYSTTVR RLRHARRHLK APLCHIPEAR
KLFMAILRHP GAVSRALLPM HRHSVLWAYM PQWGSIVGQM QFDLFHAYTV DEHTIRVLLK
IESFADEDTR PRHPLCVELY PRLPQPELLL LAALFHDIAK GRGGDHSILG AHDAVEFAEQ
HGLNSRESQL VAWLVRCHLL MSVTAQRRDI QDPAVIQQFS AEVQSETRLR YLVSLTVADI
CATNENLWNS WKQSLLRELY FATEKQLRRG MQNSPDLRER VRHHRLQALA LLRMDNIDEE
ALHRIWSRCR ADYFLRHSPN QLAWHARHLL EHDSTKPLVL VSRQATRGGT EIFIWSPDRP
SLFAAVVGEL DRRNLSVHDA QIFTNRDGMA MDTFIVLEPD GSPLAQDRHP IISHALQQAI
NRSDYQHPPR VRRLSPKLRH FSVPTEANFL PTHNERRTYL ELIALDQPGL LARVGKIFAD
LGLSLHSARI TTIGERVEDL FVLADKDRRA LSLETRRELA QRLADTLNPN DKL
