ID   GLNE_YERPG              Reviewed;         951 AA.
AC   A9R7D6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
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};
GN   OrderedLocusNames=YpAngola_A0293;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX85091.1; -; Genomic_DNA.
DR   RefSeq; WP_002212194.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R7D6; -.
DR   SMR; A9R7D6; -.
DR   GeneID; 66844170; -.
DR   KEGG; ypg:YpAngola_A0293; -.
DR   PATRIC; fig|349746.12.peg.1242; -.
DR   OMA; EFMVQYA; -.
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..951
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_1000133928"
FT   REGION          1..440
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          449..951
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   951 AA;  108330 MW;  B9FFEF8FC128B97E CRC64;
     MLPLPSELQI QAQSIKQRFS ELPAPPDLRD EDIAVLALSD FVSDMLLIHP QWLEELHQQP
     PQPQEWQYYS QWLSQALAGV QDEAALLTAL RLFRRRVMVR IAWSQVLQTS GTAETLQQLS
     TLAESMIIAA RDWLYQVCCR ELGTPCNRQG VPQPLLILGM GKLGGGELNF SSDIDLIFAY
     PENGQTQGGR RELDNAQFFT RLGQRLIKAL DQHTIDGFVY RVDMRLRPFG DSGPLVLSFA
     ALEDYYQEQG RDWERYAMVK ARLMGGADDP YSQELRQMLR PFVFRRYIDF SVIQSLRNMK
     GMIAREVRRR GLKDNIKLGA GGIREIEFIT QVFQLIRGGR EPRLQERALL PTLQAVAELG
     LLPEQQVADL SGSYLFLRRL ENLLQAIADE QTQTLPNDPL NQARLAWGMG YADWAAMSTA
     LENHMQAVRV VFDDLIGDET PDIGEDPSHG LYKSLWQDVL EESDLAPLTP HLEEAARRQL
     LATISGFRHD VDKRTIGPRG REVLDQLMPR LFAEVCPRPD ANVALSRLIL LLLSIVTRTT
     YLELLVEYHA ALKHVIRLCS ASPMVASQLA RYPLLLDELL DPQSLYQPLA PSAYRDELRQ
     YLLRVPEDDE EQQLEALRQF KQAQQLRIAA GDITEALPVM KVSDHLTYLA EAIIDAVIQQ
     AWNQMVARYG QPSHLQQSEG RGFAVIGYGK LGGWELGYSS DLDLVFLLDC PLDVMTDGDR
     SIDGRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGE AGMLVSTIEA FADYQRNEAW
     TWEHQALVRA RIVYGSPKLH QQFDAIRQQI LCRHREDPQL QQEVREMREK MRNHLGSKQR
     DIFDIKADAG GITDIEFIAQ YLVLRYAASE PRLTRWSDNV RIFESMAHYD IMSPEEAAAL
     TRAYVTMRDE IHHLALQEQS SKVAADSFIA EREQVAASWH KWLAANDANV S