ID   GLNE_BRASO              Reviewed;         986 AA.
AC   A4YRN0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=BRADO2744;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
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}.
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DR   EMBL; CU234118; CAL76556.1; -; Genomic_DNA.
DR   RefSeq; WP_011925761.1; NC_009445.1.
DR   AlphaFoldDB; A4YRN0; -.
DR   SMR; A4YRN0; -.
DR   STRING; 114615.BRADO2744; -.
DR   EnsemblBacteria; CAL76556; CAL76556; BRADO2744.
DR   KEGG; bra:BRADO2744; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_0_5; -.
DR   OMA; EFMVQYA; -.
DR   OrthoDB; 427701at2; -.
DR   BioCyc; BSP114615:BRADO_RS12865-MON; -.
DR   Proteomes; UP000001994; 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..986
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_1000212984"
FT   REGION          1..473
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          478..986
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   986 AA;  109423 MW;  ECE27568ECEA14EE CRC64;
     MTSSAPGNAD GQSRLAARFV AGPHVRAPDT AEHRLQDWLA ELEPSLAASL RDQFASGWAR
     SILLGIVESS PYLFDLIRAD AQRLDRLLRC DPQTHLAELI ARTGREVFAC SGEADVMSLL
     RRLKSEAALL IALCDIGGVW PVMQVTAALT DVAVAAVQMA LRHLLRQEAA RGRLAPIDPA
     QPELGCGLFV LAMGKMGAGE LNYSSDIDLI VFFDPDATTL AHDIEPQPFF VRVTQALARL
     LQSRTADGYV FRVDLRLRPD PASTQVAMST EAALHYYERE GRTWERAAMI KARICAGDVA
     AGEAMLAELS PFVWRKHLDF QALTDVHDMK RQMQVYRGHS EIAVEGHNVK VGRGGIREIE
     FFAQTQQLIA GGRHPELRVR PTLQALDVLT ASNWITAQAR DELTSAYEFL RRVEHRLQMM
     ADEQIHSLPD DVDGVARFAC FFGYESRERF ATDLLFHLDI VQGHYARLFE GDPTGTVSLP
     PVNYGAGPDE PRLLEHLVAL GFRDPMMVAL TLQQWLAGDY RVFRAEATRT TFNEFLPALI
     DGLAHADEPD RAVVAFDRFL QALQLGGRLI TLLGQNRDLV ALVALVLGAA PRLGDMLARQ
     PRLMDGLIDP RFFGAIPDKR ELSTRLAATL QDAGSYEEFL DRLRLFGQES LFLIGTRILS
     GTVSAQQAGT AFADVAEGIV HTVHNLVIER FAAQHGRIRG QETAIIAMGR LGAREMTASS
     DLDLILLYDF DADAPDSDGE RPLQGAHYFA RFTQRLISAF TSRTNYGVLY DIDMRLRPSG
     RAGPLASHID SFAHYQEHEA WTWEHMALTR ARVISASPAF RARIEAIIQT ALRRSRDAQA
     IARDVADMRR AIAAEKGETD LWDLKHAAGG MVDIDFVAQY LQLVHAASKP EILDISSLQV
     LDHAERLGVL PRADAVILRH AARMYHDLTQ ILRLCVSDKF KPDQAGDDLL RVMTRAGDAP
     DFSALEARVR ETQSEVRRVF TALLER