ID   GLND_AZOVI              Reviewed;         899 AA.
AC   P36223;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 101.
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}; Synonyms=nfrX;
OS   Azotobacter vinelandii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COMPLEMENTATION OF E.COLI GLND
RP   MUTANT, AND ROLE IN NITROGEN FIXATION.
RC   STRAIN=OP / UW136;
RX   PubMed=1683868; DOI=10.1128/jb.173.24.7741-7749.1991;
RA   Contreras A., Drummond M., Bali A., Blanco G., Garcia E., Bush G.,
RA   Kennedy C., Merrick M.;
RT   "The product of the nitrogen fixation regulatory gene nfrX of Azotobacter
RT   vinelandii is functionally and structurally homologous to the
RT   uridylyltransferase encoded by glnD in enteric bacteria.";
RL   J. Bacteriol. 173:7741-7749(1991).
RN   [2]
RP   FUNCTION AS PII URIDYLYLTRANSFERASE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=OP / UW136;
RX   PubMed=11320130; DOI=10.1099/00221287-147-5-1267;
RA   Colnaghi R., Rudnick P., He L., Green A., Yan D., Larson E., Kennedy C.;
RT   "Lethality of glnD null mutations in Azotobacter vinelandii is suppressible
RT   by prevention of glutamine synthetase adenylylation.";
RL   Microbiology 147:1267-1276(2001).
CC   -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC       regulatory protein GlnK, in response to the nitrogen status of the cell
CC       that GlnD senses through the glutamine level. Under low glutamine
CC       levels, catalyzes the conversion of the PII protein and UTP to PII-UMP
CC       and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP
CC       to PII and UMP (deuridylylation). Thus, controls uridylylation state
CC       and activity of the PII protein, and plays an important role in the
CC       regulation of nitrogen fixation and metabolism.
CC       {ECO:0000269|PubMed:11320130, ECO:0000269|PubMed:1683868}.
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   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not viable unless a
CC       second mutation occurs, either spontaneously or by design, resulting in
CC       the inability of glutamine synthetase (GS) to be adenylylated.
CC       {ECO:0000269|PubMed:11320130}.
CC   -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00277}.
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DR   EMBL; X59610; CAA42173.1; -; Genomic_DNA.
DR   PIR; S24223; S24223.
DR   RefSeq; WP_012702416.1; NZ_FPKM01000003.1.
DR   AlphaFoldDB; P36223; -.
DR   SMR; P36223; -.
DR   OMA; GLMQFDL; -.
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:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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; 3.30.460.10; 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; IPR003607; HD/PDEase_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; PF01842; ACT; 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   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
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   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Multifunctional enzyme; Nitrogen fixation;
KW   Nucleotidyltransferase; Repeat; Transferase.
FT   CHAIN           1..899
FT                   /note="Bifunctional uridylyltransferase/uridylyl-removing
FT                   enzyme"
FT                   /id="PRO_0000192717"
FT   DOMAIN          461..583
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          706..789
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT   DOMAIN          816..899
FT                   /note="ACT 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT   REGION          1..342
FT                   /note="Uridylyltransferase"
FT   REGION          343..705
FT                   /note="Uridylyl-removing"
SQ   SEQUENCE   899 AA;  102580 MW;  96AF63BC5EDE3C9D CRC64;
     MPQVDPDLFD PGQFQAELAL KSSPIPAYKK ALRCAREVLD ARFQEGRDIR RLIEDRAWFV
     DQILALAWNR FDWSEDADIA LIAVGGYGRG ELHPYSDIDL LILMDGADHE VFREPIEGFL
     TLLWDIGLEV GQSVRSLAEC AEEAQADLTV ITNLMESRTI AGPEHLRQRM QEVTSAQRMW
     PSRAFFLAKR DEQKTRHARY NDTEYNLEPN VKGSPGGLRD IQTLLWIARR QFGTINLHAM
     VGQGFLLESE YTLLASSQEF LWKVRYALHM LAGRAEDRLL FDLQRQIAGL LGYEDSDAKL
     AVERFMQKYY RVVLGIAELT ELVFQHFEEV ILPGDAAGRV EPLNERFQVR DGYLEVTHAG
     VFQETPSALL EIFVLLARRP EIRGVRADTI RLLRDHRYLI DDAFRRDPHN TGLFIELFKS
     RQGIHRNLRR MNRYGILGRY LPEFGHIVGQ MQHDLFHIYT VDAHTLNLIK NLRKLFWPEL
     AEKYPLASKL IEKLPKPELI YLAGLYHDIG KGRGGDHSEL GAADALAFCQ RHDLPAMDTQ
     LIVWLVRNHL LMSTTAQRKD LSDPQVIFDF AQKVRDQTYL DYLYVLTVAD INATNPTLWN
     SWRASLLRQL YTETKHALRR GLEQPVGREE QIRQTQKAAL DILVRSGTDP DDAEHLWTQL
     GDDYFLRHTS SDIAWHTEAI LQHPSSGGPL VLIKETTQRE FEGATQIFIY APDQHDFFAV
     TVAAMDQLNL SIHDARVITS TSQFTLDTYI VLDADGGSIG NNPARIQEIR QGLVEALRNP
     ADYPTIIQRR VPRQLKHFAF APQVTIQNDA LRPVTILEII APDRPGLLAR IGKIFLDFDL
     SLQNAKIATL GERVEDVFFV TDAHNQPLSD PELCARLQLA IAEQLADGDS YIQPSRISI
//