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Database: UniProt
Entry: Q4PKG7_9BACT
LinkDB: Q4PKG7_9BACT
Original site: Q4PKG7_9BACT 
ID   Q4PKG7_9BACT            Unreviewed;       851 AA.
AC   Q4PKG7;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 98.
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};
OS   uncultured bacterium MedeBAC82F10.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=332272 {ECO:0000313|EMBL:AAY78579.1};
RN   [1] {ECO:0000313|EMBL:AAY78579.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16008504; DOI=10.1371/journal.pbio.0030273;
RA   Sabehi G., Loy A., Jung K.H., Partha R., Spudich J.L., Isaacson T.,
RA   Hirschberg J., Wagner M., Beja O.;
RT   "New insights into metabolic properties of marine bacteria encoding
RT   proteorhodopsins.";
RL   PLoS Biol. 3:E273-E273(2005).
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 metabolism.
CC       {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00277};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00277};
CC   -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is inhibited
CC       by glutamine, while glutamine activates uridylyl-removing (UR)
CC       activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00277}.
CC   -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00277}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00277}.
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DR   EMBL; DQ073796; AAY78579.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4PKG7; -.
DR   SMR; Q4PKG7; -.
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; cd04899; ACT_ACR-UUR-like_2; 1.
DR   CDD; cd04873; ACT_UUR-ACR-like; 1.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR   HAMAP; MF_00277; PII_uridylyl_transf; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_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   NCBIfam; TIGR01693; UTase_glnD; 1.
DR   PANTHER; PTHR47320; BIFUNCTIONAL URIDYLYLTRANSFERASE/URIDYLYL-REMOVING ENZYME; 1.
DR   PANTHER; PTHR47320:SF1; BIFUNCTIONAL URIDYLYLTRANSFERASE/URIDYLYL-REMOVING ENZYME; 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   SUPFAM; SSF55021; ACT-like; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 1.
DR   SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR   PROSITE; PS51671; ACT; 2.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00277};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00277};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000313|EMBL:AAY78579.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00277, ECO:0000313|EMBL:AAY78579.1}.
FT   DOMAIN          440..549
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          675..746
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          781..851
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..326
FT                   /note="Uridylyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00277"
SQ   SEQUENCE   851 AA;  98929 MW;  442F8D6A5860948E CRC64;
     MKKALELKKK YQNEREKLFG TLIKSNDGVQ FNQNHTQLVD QIVKELVKEI QNQFPVSNFS
     LIAVGGYGRQ DLSPKSDVDL LFLYQKSNKN IREFITALNN SLWDLGLEVG ISFLTLKQAI
     IDSKKDIKTV TKFAESRHLI GDEDYYGEFV RSIKILIGKL NSLKLSEKKL LELVERHDYY
     LGIKSNLEPQ IKEGIGGLRD IHTIIWVSIF MFNILKLEDL IQINIFTSKE IKELRSAWKF
     LLTVRAFVHL FNDSKGDSLS IENQLKISKK LSYRNNQKEK GVERFMKHLF VNIAKIESLL
     NTFYSKLPEE LIIKTIHKSK PAKTKSLDKK YFIEKGFVHL KNYNSNNLLQ NWLGVFESSL
     KHNLFVHPRF LKVIEEKKKQ IKKSMTPDQY EIIIDIISSK KNPIQVLRNL NDTKVLNELF
     PEFGRVWGQV QFDIYHHYTT DEHLLLTLYH LHELKKKSFY KEIYSRLHQK VALHVALLFH
     DIGKKGPKSH SIYGKELTQK IFKRLPLSVE DQELSLWLIE NHLLMSDIAF KNDPQDPDVI
     ASFTAIANTQ EKVNSLFLFT LCDIAAVGPN ILNEWRISLL RSLLFNARDF LQRGLDTANY
     SSSVQESLKK MVLEQADKEM KLFIKKTMRY FPNLYWEAFA SKMILDIFGF YHDYQKNKKE
     LSVKFLNYNN NEYGAVIVIC PNRSGVLKDI VAGFHSSQIN ILGSRIISLN NNDIIDVFWV
     TSSIQKAIIE KNEQERVIQN ITASLNQEEL ETYQTLFQTK IKVEVEPRIT IDNQMSKLAT
     TFQILSGDRQ GLLMDILQIF HDQNMSVQSA KISTYGEKVF DIFQITDLKN KKVKDTKTLK
     TLEDQLLKIL S
//
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