ID   GLNE_BRASB              Reviewed;         985 AA.
AC   A5EGB0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=BBta_3086;
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=288000;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTAi1 / ATCC BAA-1182;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000494; ABQ35204.1; -; Genomic_DNA.
DR   RefSeq; WP_012043222.1; NC_009485.1.
DR   AlphaFoldDB; A5EGB0; -.
DR   SMR; A5EGB0; -.
DR   STRING; 288000.BBta_3086; -.
DR   EnsemblBacteria; ABQ35204; ABQ35204; BBta_3086.
DR   KEGG; bbt:BBta_3086; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_0_5; -.
DR   OMA; EFMVQYA; -.
DR   OrthoDB; 427701at2; -.
DR   Proteomes; UP000000246; 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..985
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_1000212983"
FT   REGION          1..472
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          477..985
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   985 AA;  109590 MW;  58F0682AD8152487 CRC64;
     MTSSAPGNAD GQILAERFVS GPHVRAPDKA EHRLNEWLAE LEPSLAASLR ALLAKGLPRS
     ILLGIAECSP YLFDLVRADA RRFERLLRSE PQAHLAELIS RTGREVFAAT SEADVMRLLR
     QLKSEAALLI ALCDIGGVWP VMQVTAALTD VAVSAVQMAL RYLLRQEAVR GRLAPRDADD
     PEQGCGLFVL AMGKMGAGEL NYSSDIDLIV FFDPEVHSLA RDIEPQPFFV RVTQALARLL
     QSRTADGYVF RVDLRLRPDP ASTQVAMSTE AALHYYEREG RTWERAAMIK ARICAGDVAA
     GEAMLAELSP FVWRKHLDFQ ALTDVHDMKR QMQVYRGHSE IAVEGHNVKV GRGGIREIEF
     FAQTQQLIAG GRHPELRVRP TLQALGVLTA SKWITEQARD ELTTAYEFLR RVEHRLQMMA
     DEQIHSLPDD AEGVSRFACF FGYESRERFA SDLLFHLNIV QGHYARLFEG DPTGTVSLPP
     VNYGAGPDEP RLMEHLAGLG FRDPVMVAKT LQQWLAGEYR VFRTEATRTS FTEFLPALID
     GLAHADEPDR AVVAFDRFLQ ALQLGGRLIS LLGQNRDLVA LVALVLGAAP RLGDMLARQP
     RLMDGLIDPR FFGAMPDKRE LSQRLAATLQ DAGTYEEFLD RLRLFGQESL FLIGTRILSG
     TVSAQQAGTA FADVAEGIVH TVHGLVTERF AAQHGRIKGQ ETAIIAMGRL GAREMTASSD
     LDLILLYDFD ADEPDSDGER SLQGAHYFAR FTQRLISAFT SRTNYGVLYD IDMRLRPSGR
     AGPLASHLDS FAHYQEREAW TWEHMALTRA RVISASPAFR ARIEEIIQTA LRRPRDPVAI
     ARDVADMRRA IAAEKGEADL WDLKHAAGGM VDIDFVAQYL QLVHAATKPE ILDVSSLQVL
     DHAERLGVLP RADAVILRHA ARLYHDLTQI LRLCVSDKFK PDQAGEDLLR VLARAGDAPD
     FSALEARLRE TQSEVRRVFT SLLEE