(data stored in SCRATCH zone)

SWISSPROT: D3UWF7_XENBS

ID   D3UWF7_XENBS            Unreviewed;       884 AA.
AC   D3UWF7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
DE            Short=UTase/UR {ECO:0000256|HAMAP-Rule:MF_00277};
DE   AltName: Full=Bifunctional [protein-PII] modification enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
DE   AltName: Full=Bifunctional nitrogen sensor protein {ECO:0000256|HAMAP-Rule:MF_00277};
DE   Includes:
DE     RecName: Full=[Protein-PII] uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00277};
DE              Short=PII uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00277};
DE              Short=UTase {ECO:0000256|HAMAP-Rule:MF_00277};
DE              EC=2.7.7.59 {ECO:0000256|HAMAP-Rule:MF_00277};
DE   Includes:
DE     RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
DE              Short=UR {ECO:0000256|HAMAP-Rule:MF_00277};
DE              EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_00277};
GN   Name=glnD {ECO:0000256|HAMAP-Rule:MF_00277,
GN   ECO:0000313|EMBL:CBJ79731.1};
GN   OrderedLocusNames=XBJ1_0587 {ECO:0000313|EMBL:CBJ79731.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79731.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79731.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79731.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC       regulatory proteins (GlnB and homologs), in response to the
CC       nitrogen status of the cell that GlnD senses through the glutamine
CC       level. Under low glutamine levels, catalyzes the conversion of the
CC       PII proteins and UTP to PII-UMP and PPi, while under higher
CC       glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP
CC       (deuridylylation). Thus, controls uridylylation state and activity
CC       of the PII proteins, and plays an important role in the regulation
CC       of nitrogen assimilation and metabolism. {ECO:0000256|HAMAP-
CC       Rule:MF_00277}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-
CC         L-tyrosine + diphosphate; Xref=Rhea:RHEA:13673, Rhea:RHEA-
CC         COMP:12147, Rhea:RHEA-COMP:12148, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:46858, ChEBI:CHEBI:90602;
CC         EC=2.7.7.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00277,
CC         ECO:0000256|SAAS:SAAS01174802};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-
CC         L-tyrosine + H(+) + UMP; Xref=Rhea:RHEA:48600, Rhea:RHEA-
CC         COMP:12147, Rhea:RHEA-COMP:12148, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:57865,
CC         ChEBI:CHEBI:90602; Evidence={ECO:0000256|HAMAP-Rule:MF_00277,
CC         ECO:0000256|SAAS:SAAS01174764};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00277, ECO:0000256|SAAS:SAAS00609838};
CC   -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is
CC       inhibited by glutamine, while glutamine activates uridylyl-
CC       removing (UR) activity. {ECO:0000256|HAMAP-Rule:MF_00277}.
CC   -!- DOMAIN: Has four distinct domains: an N-terminal
CC       nucleotidyltransferase (NT) domain responsible for UTase activity,
CC       a central HD domain that encodes UR activity, and two C-terminal
CC       ACT domains that seem to have a role in glutamine sensing.
CC       {ECO:0000256|HAMAP-Rule:MF_00277}.
CC   -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00277, ECO:0000256|SAAS:SAAS01174767}.
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DR   EMBL; FN667741; CBJ79731.1; -; Genomic_DNA.
DR   RefSeq; WP_012987185.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0587; -.
DR   EnsemblBacteria; CBJ79731; CBJ79731; XBJ1_0587.
DR   GeneID; 8830209; -.
DR   KEGG; xbo:XBJ1_0587; -.
DR   PATRIC; fig|406818.4.peg.540; -.
DR   eggNOG; ENOG4105E1P; Bacteria.
DR   eggNOG; COG2844; LUCA.
DR   HOGENOM; HOG000261778; -.
DR   KO; K00990; -.
DR   OMA; HTLFWIA; -.
DR   BioCyc; XBOV406818:XBJ1_RS02545-MONOMER; -.
DR   Proteomes; UP000002045; 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; IPR002912; ACT_dom.
DR   InterPro; IPR005105; GlnD_Uridyltrans_N.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   InterPro; IPR010043; UTase/UR.
DR   PANTHER; PTHR47320; PTHR47320; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF03445; DUF294; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 1.
DR   Pfam; PF01966; HD; 1.
DR   PIRSF; PIRSF006288; PII_uridyltransf; 1.
DR   SMART; SM00471; HDc; 1.
DR   TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR   PROSITE; PS51671; ACT; 2.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UWF7.
DR   SWISS-2DPAGE; D3UWF7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS01174769};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00204441};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00677267};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440786, ECO:0000313|EMBL:CBJ79731.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Repeat {ECO:0000256|SAAS:SAAS00300508};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440788, ECO:0000313|EMBL:CBJ79731.1}.
FT   DOMAIN      462    584       HD. {ECO:0000259|PROSITE:PS51831}.
FT   DOMAIN      703    787       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      810    884       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1    343       Uridylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00277}.
FT   REGION      344    702       Uridylyl-removing. {ECO:0000256|HAMAP-
FT                                Rule:MF_00277}.
SQ   SEQUENCE   884 AA;  102495 MW;  5E22EB2265E51269 CRC64;
     MSVDITFAHA PIPPLSPVEF SLDDLQCPVL KQHVDEFQLW LQQAFKAGIS PEALISARSD
     YIDRLLTRLW QAHGFDQNTS LSLIAVGGYG RRELHPLSDI DLLILSESQL TEDQAHNIGQ
     FITLLWDIRL EVGHSVRTFE ECLHEGLSDL TVATNLIESR LICGDLPLFL RLQKHIFSDD
     FWPSSTFFAA KLREQWERHQ RYHSTSYNLE PDIKSSPGGL RDIHTLLWVA RRHFGAASLD
     EMVDFGFLTR EERNELNECQ NFLWRIRFAL HLVVTRYDNR LLFERQFNVA QLLGYEGERN
     QPVERMMKNF YRVTRRVSEL NDMLLQLFDE AILTLQPDEK PRPLNEAFQL RGDLIDLSDE
     TLFIQDPTSI LKMFYHMAEH REIKGIYSTT LRQLRYARRN LKHPLCELPE ARKLFMDILR
     HPRAVKNALI PMHRHSVLGA YMPLWSNIVG QMQFDLFHAY TVDEHTLRVL QKLESFADEN
     NRVIHPLCVE LYPRIPQPEL LRLAAFFHDI AKGRNGDHSE LGAKDAFTFA RQHGLTTREA
     ELVEWLVRDH LLMSVTAQRR DIQDPDVIQQ FAGQVKNKNR LNYLLCLTVA DICATNSKLW
     NSWKQSLIRE LYFATETQLR QGIQNTPDLR ERVRHNRLQA LALLRQERAD EEQLHNIWSR
     CHADYFLRHT PDQLAWHAGH LIQHQSAEPM VLISTAFSHG GTEIFIWCQD RPSLFAAVVG
     ELDRRNLSVH DAQIFTNRDE MAMDTFIVLE PNGHPLALDR HEPIRRALLK VVNDPHPKAP
     KARNLPAKLR HFDVPTKVSF LPTQNARRSY MELVALDQPG LLARVGNIFA ELGVSLHGAR
     ITTIGERVED FFILADKDHQ ELDNKIKGEL SERLTEALNT KDKV
//

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