ID   GLND_PHOLL              Reviewed;         882 AA.
AC   Q7N8P9;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 127.
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};
GN   OrderedLocusNames=plu0670;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01) (Photorhabdus luminescens subsp. laumondii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; Evidence={ECO:0000255|HAMAP-
CC         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; BX571861; CAE12965.1; -; Genomic_DNA.
DR   RefSeq; WP_011145046.1; NC_005126.1.
DR   AlphaFoldDB; Q7N8P9; -.
DR   SMR; Q7N8P9; -.
DR   STRING; 243265.plu0670; -.
DR   GeneID; 24167981; -.
DR   KEGG; plu:plu0670; -.
DR   eggNOG; COG2844; Bacteria.
DR   HOGENOM; CLU_012833_0_0_6; -.
DR   OrthoDB; 9758038at2; -.
DR   Proteomes; UP000002514; 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; cd04899; ACT_ACR-UUR-like_2; 1.
DR   CDD; cd04900; ACT_UUR-like_1; 1.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases 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; 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   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; PF01842; ACT; 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; ACT-like; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 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..882
FT                   /note="Bifunctional uridylyltransferase/uridylyl-removing
FT                   enzyme"
FT                   /id="PRO_0000192751"
FT   DOMAIN          462..577
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          701..778
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT   DOMAIN          808..882
FT                   /note="ACT 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT   REGION          1..343
FT                   /note="Uridylyltransferase"
FT   REGION          344..700
FT                   /note="Uridylyl-removing"
SQ   SEQUENCE   882 AA;  102232 MW;  12FEA798C315CBCD CRC64;
     MSADIATIQA PIPPLSPADF SSEDLRYPVL KQHLEEFQLW LEHAFKAGIS AEALISARSD
     YIDQLLQQLW YAYRFDKISS LSLIAVGGYG RRELHPLSDI DVLILSEQPL TPPQAQNVGQ
     FITLLWDIRL EVGHSVRTLE ECLLEGLSDL TIATNLIESR LICGDSSIFL RLQRHTFSDG
     FWPSTEFFDA KIVEQHERHQ RYHSTSYNLE PDIKSSPGGL RDIHTLLWVA RRHFGATSID
     EMVDFGFLTA EERNELNECQ SFLWRIRFAL HLVVNRYDNR LLFDRQFSIA QLLGYHGERN
     QPVERMMKDF YRMTRRVSEL NNMLLQLFDE AILALETNEK SRSLDSEFQL RGQLIDLIDE
     TLFIKEPAAI MRMFYRMAEH EEVQGIYSTT LRHLRYARRN LSQPLCELPE ARQIFMDILR
     HPRAVESAFV PMHRHSVLGA YTPLWGNIVG QMQFDLFHAY TVDEHTIRVL RKLESFANEN
     NRPAHPLCVE LYPRLPQPEL LHLAALFHDI AKGRTGDHSE LGADDALAFS LKHGLNSREA
     DLVAWLVRHH LLMSVTAQRR DIQDPEIIKQ FTHQILNETR LRYLICLTVA DICATNVNLW
     NSWKQSLLRE LYFSTENQLR QGNTPDFRER IRHNRFQALA LLRQDNINEQ KLHQLWSRCH
     ADYFLRHTPK QLAWHAHHLV QHDSQESLIL ISTKPTRGGT EIFIWSVDRP SLFAAVVGEL
     DRRNLSVHHA QIFTNRDGMT MDTFVVLEPN GHPLASDRHE IIRNALLQVV LAPHTKTPKT
     RKLPTKLRHF NVPTKVTFLP THNERRTYME LFALDQPGLL ARVGNIFAEM GVSLHGAHIT
     TIGERVEDFF VLADKDHKAL NKKVREELSE RLTATLNPKD KI
//