ID   GLNE_RALSO              Reviewed;         955 AA.
AC   Q8XW19;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00802};
DE   AltName: Full=ATP:glutamine synthetase adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00802};
DE   AltName: Full=ATase {ECO:0000255|HAMAP-Rule:MF_00802};
DE   Includes:
DE     RecName: Full=Glutamine synthetase adenylyl-L-tyrosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_00802};
DE              EC=2.7.7.89 {ECO:0000255|HAMAP-Rule:MF_00802};
DE     AltName: Full=Adenylyl removase {ECO:0000255|HAMAP-Rule:MF_00802};
DE              Short=AR {ECO:0000255|HAMAP-Rule:MF_00802};
DE              Short=AT-N {ECO:0000255|HAMAP-Rule:MF_00802};
DE   Includes:
DE     RecName: Full=Glutamine synthetase adenylyl transferase {ECO:0000255|HAMAP-Rule:MF_00802};
DE              EC=2.7.7.42 {ECO:0000255|HAMAP-Rule:MF_00802};
DE     AltName: Full=Adenylyl transferase {ECO:0000255|HAMAP-Rule:MF_00802};
DE              Short=AT {ECO:0000255|HAMAP-Rule:MF_00802};
DE              Short=AT-C {ECO:0000255|HAMAP-Rule:MF_00802};
GN   Name=glnE {ECO:0000255|HAMAP-Rule:MF_00802}; OrderedLocusNames=RSc2656;
GN   ORFNames=RS04556;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
CC   -!- FUNCTION: Involved in the regulation of glutamine synthetase GlnA, a
CC       key enzyme in the process to assimilate ammonia. When cellular nitrogen
CC       levels are high, the C-terminal adenylyl transferase (AT) inactivates
CC       GlnA by covalent transfer of an adenylyl group from ATP to specific
CC       tyrosine residue of GlnA, thus reducing its activity. Conversely, when
CC       nitrogen levels are low, the N-terminal adenylyl removase (AR)
CC       activates GlnA by removing the adenylyl group by phosphorolysis,
CC       increasing its activity. The regulatory region of GlnE binds the signal
CC       transduction protein PII (GlnB) which indicates the nitrogen status of
CC       the cell. {ECO:0000255|HAMAP-Rule:MF_00802}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine +
CC         phosphate = [glutamine synthetase]-L-tyrosine + ADP;
CC         Xref=Rhea:RHEA:43716, Rhea:RHEA-COMP:10660, Rhea:RHEA-COMP:10661,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624,
CC         ChEBI:CHEBI:456216; EC=2.7.7.89; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00802};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[glutamine synthetase]-L-tyrosine + ATP = [glutamine
CC         synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + diphosphate;
CC         Xref=Rhea:RHEA:18589, Rhea:RHEA-COMP:10660, Rhea:RHEA-COMP:10661,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:83624; EC=2.7.7.42; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00802};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00802};
CC   -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00802}.
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DR   EMBL; AL646052; CAD16363.1; -; Genomic_DNA.
DR   RefSeq; WP_011002566.1; NC_003295.1.
DR   AlphaFoldDB; Q8XW19; -.
DR   SMR; Q8XW19; -.
DR   STRING; 267608.RSc2656; -.
DR   EnsemblBacteria; CAD16363; CAD16363; RSc2656.
DR   GeneID; 60502159; -.
DR   KEGG; rso:RSc2656; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_1_4; -.
DR   OMA; EFMVQYA; -.
DR   Proteomes; UP000001436; Chromosome.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047388; F:[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000820; P:regulation of glutamine family amino acid metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.460.10; -; 2.
DR   HAMAP; MF_00802; GlnE; 1.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR30621; PTHR30621; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
DR   SUPFAM; SSF81301; SSF81301; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..955
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_0000209270"
FT   REGION          1..458
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          464..955
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   955 AA;  106370 MW;  78037681294C581A CRC64;
     MTAQAPLSVA PFLQTPACPS EAPGAVLPFS LNYSRYVQRL AQARAGWAER VQAAAAGPIS
     VAWLSARFGE LFEAAAAEPE QALKRALRLL RNEVFAALAE RDLSGAATLD EVTGAMTDFA
     EFAVRAAIAV IGQELGALHG QPVGQSSGEV QELVVVGMGK LGGRELNVSS DIDLIFLYDE
     EGDTQGGPRP LSNHEYFTKL GRRLINALAD VTEDGYVFRV DMRLRPNGDA GPLACSLGML
     EEYFVVQGRE WERYAWIKGR VITDPGSPHA ARVIQQLERV TTPFVFRRYL DYGVIAAIRA
     LHAQIRAEAA KRSNAANRQH GGHDSQVQAH APNIKLGRGG IREIEFVAQV FQLIRGGQDF
     GLRIRPTLEV LRAAAERGLI GADAVARLTD AYRFLRQLEH RLQYVDDAQT HNLPGAPEDQ
     LRIARMMGFA DYAALVAQLE RYQDEVAQQF EQTFSDKQDN QPPCAAIWHA DLLDDERTES
     ARAQLLELGY ADADSVLERL RASRHSPRYR ALSEVSRQRF DLLINRALDH AARQTDADVT
     IARFLDFFDA ISRRSSYLSL LSEYPQAMAR VAHTLHASRW AADYLTRHPQ LLDELLDTEA
     LSAAPDWQGF RERVRERLRA AGDHVEMQMD ILRQEHHAET FRILLQDLQG MLTVEPISDR
     LSDLADAVLD LTLETVWQQV STRHREVPRF AVVAYGRLGG KELGYASDLD LIFLYDDDDE
     RAPEVYAAYA RKLITWLTSH TAAGMLFDVD TRLRPNGAAG LMVTHFEAFR RYQMREGDNA
     AWVWEHQALT RARFCAGDPE IGARFEALRI AVLRQPREAG PLRDEIAAMR ERVLEGHANP
     TPLFDLKHDR GGMVDIEFTV QFLVLLHSAA YAELTRNAGN IALLRMAGEL GLIDAARAAR
     VADAYRDFRA RQHKLRLDGQ SAARVPAGTC AHEAAHVRAL WEQVFGSIDA ASPTP