ID   GLND_AROAE              Reviewed;         862 AA.
AC   Q5NZH8;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 116.
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=AZOSEA34110; ORFNames=ebA5982;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(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 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; CR555306; CAI09536.1; -; Genomic_DNA.
DR   RefSeq; WP_011239196.1; NC_006513.1.
DR   AlphaFoldDB; Q5NZH8; -.
DR   SMR; Q5NZH8; -.
DR   STRING; 76114.ebA5982; -.
DR   KEGG; eba:ebA5982; -.
DR   eggNOG; COG2844; Bacteria.
DR   HOGENOM; CLU_012833_0_0_4; -.
DR   OrthoDB; 9758038at2; -.
DR   Proteomes; UP000006552; 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; 3.30.70.260; -; 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; 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; 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..862
FT                   /note="Bifunctional uridylyltransferase/uridylyl-removing
FT                   enzyme"
FT                   /id="PRO_0000192715"
FT   DOMAIN          447..563
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          686..765
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT   DOMAIN          794..862
FT                   /note="ACT 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT   REGION          1..328
FT                   /note="Uridylyltransferase"
FT   REGION          329..685
FT                   /note="Uridylyl-removing"
SQ   SEQUENCE   862 AA;  98195 MW;  FA31DCA7E434257E CRC64;
     MSTAAIPTDA AVQAAIAEAR ARLADGSMRI RMAYEGHPAT STVLKGRAHL VDETIHRLWR
     ACAMPADVAL LAVGGYGRGE LFPCSDVDLM VLLPDTADDA MQARLSVLLG ALWDVGLEIG
     HSARTVAEAI DAAEQDITVQ TNLLESRLLE GNRPLFEEFC RRYRALLDVR VFFKAKQLEQ
     EKRYARYNDT PYALEPNCKE SPGGLRDLQM LGWIARAAGL GRNWRDLARR RLITGAEARD
     LRSIERFLQH VRIRLHYLTG RSEDRLLFDY QERLASALGI EATAAKRASE VFMQRYYVNA
     KKVTQTNTIL LQNYGVEIFP RRAGAAIVIN ERFQAVRELL DMREDDTFAR HPSALLECFL
     ILQQRSELKG MTARTLRALW LNRKRINAAF RADPHNRELF VAILQQKRGI VHEFRRMNQY
     GILSGYLPSW RRIVGQMQHD LFHVYTVDQH IMMVLRNMRR FTMGEHAHEY PLMAQLIMAF
     DRHWLLYVAA LFHDIAKGRG GDHSKLGTID AREFCEHHHL AREDADLVVW LVEHHLTMSH
     VAQKEDTSDP AVIGRFADTV GTERRLTALY LLTHADIRGT SPKVWNGWKG KLLEDLFFAT
     RRLLRGATPQ EALGLDDRQE NARALLRYHG LRPGVEDALW AQLDAVYFMR HSAEEIAWHS
     RTLYYRPDAL EPVVKARVSD ADQGVQVMVF TRDQKDLFVR LTGFFGRLGF SILDAKVHTT
     RHGYALDSFM LQDPGNAEHY RDVITLIEHE LTERLKKSAP PDRPSAGRLS RQVKHFPITP
     RVSILPDESG RHYILSLTAA DRRGLLFAVA EVLAQNGIVL HTAKIATLGE RVEDTFLLSG
     NGLSQDARVV KIERELLQRL HI
//