ID   GLNE_RHOPA              Reviewed;         990 AA.
AC   Q6N8H0;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=RPA1933;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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; BX572599; CAE27374.1; -; Genomic_DNA.
DR   RefSeq; WP_011157488.1; NC_005296.1.
DR   AlphaFoldDB; Q6N8H0; -.
DR   SMR; Q6N8H0; -.
DR   STRING; 258594.RPA1933; -.
DR   PRIDE; Q6N8H0; -.
DR   EnsemblBacteria; CAE27374; CAE27374; RPA1933.
DR   GeneID; 66892976; -.
DR   KEGG; rpa:RPA1933; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_0_5; -.
DR   OMA; EFMVQYA; -.
DR   PhylomeDB; Q6N8H0; -.
DR   BioCyc; RPAL258594:TX73_RS09875-MON; -.
DR   Proteomes; UP000001426; 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..990
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_0000209273"
FT   REGION          1..474
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          478..990
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   990 AA;  109348 MW;  1CCE4F428FD90AF2 CRC64;
     MIFSAITADL DNTALAARFG AGPRLYDPVL AAERWAGWLA DLAPEQADAI AALGNAFPDL
     QIALQSIAEA SPYLFDLIRG DPVRLLRVLR GAPEQRLAKL LEDAETFVAA ASAEDEVMAA
     LRRLKAEAAL LIALCDIGGI WPVMQVTQAL TDLAGRSVQM ALRFLLRQEA GRGRIVPPNP
     DCPEQGSGLI VLAMGKMGAG ELNYSSDIDL IVFYELDAPT LAPDIEPQPF FVRVTQGLSR
     ILQQRRGDGY VFRVDLRLRP DPASTPVALS TVSALDYYER EGRTWERAAM IKARPCAGDL
     VAGDALLSEI APFVWRKHLD FAALSDVHDM KRQMQTYRGQ TEIAVEGHNV KVGRGGIREI
     EFFAQTQQLI AGGRHPELRV RPTLEALEIL AARNWITLQA RDELTEAYLF LRKVEHRVQM
     IADEQTHALP DTVEAIEQFS RFLGYDSRDS FARDLLGYLE RVQGHYAKLF EGDPTGTAKL
     PPVDYGAGPE DTRLLDHLLS LGYKKPLMIA TTLQQWMTGG YRVLKVETTQ RAFREFVPAL
     IEELARAEQP DDAVNAFDRL LQALHRGGRL ISLLSQNREL LTLVALVLGA APRLGDMLAR
     QPQILDGLID PRFFGAMPDQ AELSARLAVT LADAGSYEEF LDRLRLFGQE SLFLIGTRIL
     SGTVPTQQAA VAFADVAEGI VGTVHGLVSE QFASTYGRVK GQQTAILAMG KLGSREMTAS
     SDLDLILIYD FDDDQPDSDG ERSLHGAQYF ARFTQRLISA FTTRTNYGVL YDVDMRLRPS
     GRAGPVASRL DAFAAYQEQE AWTWEHLALT RARVISAPPE FRSRIEQVIR AVLTRQRDAA
     IIANDVAEMR RAIAQEKGED DVWDLKYAAG GMVDIDFIAQ YLQLVHAHEA PDILHVNTLS
     ALDNATRLGL LAQADAEVLR PAARLYQNLT QILRLCVSEK FNPDTAGDDL LRVMVRAGDA
     PDFSSLQARV KETQSDVRAI FSRLIGGEDA