ID   GLND_CAUVN              Reviewed;         940 AA.
AC   B8GWX0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=CCNA_00013;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(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; CP001340; ACL93480.1; -; Genomic_DNA.
DR   RefSeq; WP_010917903.1; NC_011916.1.
DR   RefSeq; YP_002515388.1; NC_011916.1.
DR   AlphaFoldDB; B8GWX0; -.
DR   SMR; B8GWX0; -.
DR   PRIDE; B8GWX0; -.
DR   EnsemblBacteria; ACL93480; ACL93480; CCNA_00013.
DR   GeneID; 7332895; -.
DR   KEGG; ccs:CCNA_00013; -.
DR   PATRIC; fig|565050.3.peg.14; -.
DR   HOGENOM; CLU_012833_1_0_5; -.
DR   OMA; WIAKYVY; -.
DR   OrthoDB; 162558at2; -.
DR   PhylomeDB; B8GWX0; -.
DR   Proteomes; UP000001364; 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   Gene3D; 3.30.460.10; -; 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; IPR010043; UTase/UR.
DR   PANTHER; PTHR47320; PTHR47320; 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   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..940
FT                   /note="Bifunctional uridylyltransferase/uridylyl-removing
FT                   enzyme"
FT                   /id="PRO_1000132527"
FT   DOMAIN          496..618
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          737..821
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT   DOMAIN          848..929
FT                   /note="ACT 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT   REGION          1..379
FT                   /note="Uridylyltransferase"
FT   REGION          380..736
FT                   /note="Uridylyl-removing"
SQ   SEQUENCE   940 AA;  103396 MW;  2F1985420353F8ED CRC64;
     MPRRLRPTRL EHVVDGHALR ARLSAAALDS IGNEAEQRAR AIDILKQALF RGRMIAKERL
     ENGASGVETS RLLSGVTDEV ITALYDFTTV HVFRARNPTE GERLCLLAVG GYGRGTLAPF
     SDIDLLFLRP YKQTPHAESV IEYMLYALWD LGFKVGHASR TIEECVRLSK EDFTIRTSIL
     EARRLTGDER LAEDLKKRFR DEVMKATGAQ FVAAKLKERD DRQARAGASR YMVEPNVKEG
     KGGLRDLHTL MWIAEYLHPV DRPEDVFKME VFSIRETKAF IRAFDFLHAV RAHLHFTTGR
     PEERLTFDLQ PEIARRMGYG DRGDAPAVER FMRRYFLIAK EVGTLTRAFS AKLEAEHFKN
     EPKGISRFLP GARPKRKALD VEGFYEDGGR LNIEGQEIFE ADPVNLIRLF KIADERDLDL
     HPDAFTAVTR ALPLITSRVR RDPDACRAFL DLLARGKRSY RTLTLMNDAG VLGRFIPEFG
     RVVAQMQFNM YHSYTVDEHT LRAVGVIGDI AAGRLVDDHP LAVSIMPLIE DREALFLAML
     LHDTGKGGVG GQEKAGARSA RSACERLGVE RSKVELVAWL VENHLVMSDF AQKRDVSDPG
     TVAAFARIVE NPERLRLLLV ITVADIRAVG PGVWNGWKGQ LLRELYNATE AVFRGGRGSD
     AAANVQRHQE STAEAARAAL LETDPAAKGW VAAMENAYFS AFSQDDLFHH AELARRAAIQ
     GGAAAEGQVR PGSNAAEVVI AAKDRRGLFA DLALAISSLG GNVVGARVFT SRQGQALDVF
     YVQDVTGAPF GCENPRALRR LADALEAAGK GDALAVEPRR GSEQTRAAAF AIAPSVTIDN
     DASNDATVVE ASGRDRPGLL HALAKTLADS ALSIQSAHID GYGERAVDAF YVQTTEGGKV
     TDTRKLNALK ADLLAALEQN EASAPAARPG LRRARASVAR