ID   GLNE_RHOPS              Reviewed;         989 AA.
AC   Q139J0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=RPD_2014;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000283; ABE39249.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q139J0; -.
DR   SMR; Q139J0; -.
DR   STRING; 316057.RPD_2014; -.
DR   EnsemblBacteria; ABE39249; ABE39249; RPD_2014.
DR   KEGG; rpd:RPD_2014; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_0_5; -.
DR   OMA; EFMVQYA; -.
DR   OrthoDB; 427701at2; -.
DR   BioCyc; RPAL316057:RPD_RS10115-MON; -.
DR   Proteomes; UP000001818; 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; Transferase.
FT   CHAIN           1..989
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_1000212988"
FT   REGION          1..474
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          480..989
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   989 AA;  108894 MW;  0D1AD4819158F9F9 CRC64;
     MNSSAIDADI PPSALAARFA AGPQLHAPEE AEKRLADWLG DVPADLAGAI RSVADRHPHV
     GVALRSIAEA SPYLFDLIRA DPARLLGLLR SDPEAGFVAL LDRASAAVAA ASDEAEVMAV
     LRKMKAEAAL SIALCDIGGL WPVMQVTQAL TDLAVNSVQM TLRFLLRQEA ARGRIIPPNS
     DAPEQGSGLV VLAMGKMGAG ELNYSSDIDL IVFYDLDAPT LAPDIEPQPF FVRVTQGLSR
     ILQQRRHDGY VFRVDLRLRP DPASTPVALS TVSALNYYER EGRTWERAAM IKARACAGDL
     VAGEALLGDI APFVWRKHLD FAALSDVHDM KRQMQTFRGQ TEVAVEGHNV KVGRGGIREI
     EFFAQTQQLI AGGRHPELRV RPTLAALDIL AARDWITYQA RDELSVAYQF LRRVEHRIQM
     IADEQTHTLP DSVEAVERFS RFFGYESREA FARDLLAYFD CVQGHYGKLF EGDPTGTVKL
     PIDYAGGPDD TGLLDHLHGL GYKKPLMVAT TLQQWMTGGY RILKVETTQR AFHEFVPMLI
     EELARAEEPD NAVNAFDRLL QALHRGGRLI SLLSQNRDLL TLVALVLGAA PRLGDMLARQ
     PQILDGLIDP RFFGAMPDRA ELSARLAATL ADAGPYEEFL DRLRLFGQES LFLIGTRILS
     GTVSTQQASV AFADVAEGIV GTVHDLVSEQ FISQYGRIKD QQTAILAMGK LGSREMTASS
     DLDLILIYDF DHEQPDSDGE RSLQGAQYFA RFTQRLISAF TTRTNYGVLY DVDMRLRPSG
     RAGPLASRLD SFAEYQEVEA WTWEHLALTR ARVISASPEF RERIEQVIRA VLTRPRDAAI
     IANDVAEMRH AIAQEKGEDD VWDMKYAAGG MVDIDFIAQY LQLVHAAATP EILGVSTLGA
     IDNAARLGVL AQSDAEVLRP AARLYHDLTQ ILRLCVSDKF KPETAGEDLL RVLVRAGDAP
     DFSSLEARVK ETQAEVRAIF NRLIGGDSA