ID   GLNE_NEIMA              Reviewed;         896 AA.
AC   Q9JX72; A1INQ4; Q9JPK5;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=NMA0035;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-896.
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10722605; DOI=10.1128/iai.68.4.2082-2095.2000;
RA   Klee S.R., Nassif X., Kusecek B., Merker P., Beretti J.-L., Achtman M.,
RA   Tinsley C.R.;
RT   "Molecular and biological analysis of eight genetic islands that
RT   distinguish Neisseria meningitidis from the closely related pathogen
RT   Neisseria gonorrhoeae.";
RL   Infect. Immun. 68:2082-2095(2000).
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; AL157959; CAM07361.1; -; Genomic_DNA.
DR   EMBL; AJ391262; CAB72042.1; -; Genomic_DNA.
DR   PIR; E81994; E81994.
DR   RefSeq; WP_002246770.1; NC_003116.1.
DR   AlphaFoldDB; Q9JX72; -.
DR   SMR; Q9JX72; -.
DR   EnsemblBacteria; CAM07361; CAM07361; NMA0035.
DR   KEGG; nma:NMA0035; -.
DR   HOGENOM; CLU_006233_0_1_4; -.
DR   OMA; EFMVQYA; -.
DR   BioCyc; NMEN122587:NMA_RS00175-MON; -.
DR   Proteomes; UP000000626; 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..896
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_0000209258"
FT   REGION          1..411
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          417..896
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   896 AA;  102035 MW;  57B1E3CB5249A9A8 CRC64;
     MSDNRLDTAR HHSLFLARQL DNGKLKPEIF LPMLDKVLTE ADFQAFADWD KIRAEENEEE
     LARQLRELRR YVVSQIIVRD INRISDLNEV TRTITLFADF AVNTALDFAY AYYRDMYGTP
     IGRYTKSPQH LSVVAMGKAG GYELNVSSDI DLIFVYPESG DTDGRRERGN QEFFTKVGQK
     LIALLNDITA DGQVFRVDMR LRPDGDSGAL VLSETALEQY LITQGREWER YAWCKGRVVT
     PYPNGIKSLV RPFVFRKYLD YSAYEAMRKL HRQISSEVSK KGMADNIKLG AGGIREVEFI
     AQIFQMIRGG QMRALQLKGT QETLKKLAET GIMPSENVET LLAAYRFLRD VEHRLQYWDD
     QQTQTLPTSP EQRQLLAESM GFDSYSAFSD GLNIHRNKVN QLFNEILSEP EEQTQDNSEW
     QWAWQEKPDE EERLGRLKEY GFDAETIATR LDQIRNGHKY RHLSAHAQPR FDAIVPLFVQ
     AAAEQNNPTD TLMRLLDFLE NISRRSAYLA FLNEHPQTLA QLAQIMGQSS WVAAYLNKYP
     ILLDELISAQ LLDTAFDWQA LAAALSDDLK ACGGDTEAQM DTLRRFQHAQ VFRLAVQDLA
     GLWTVESLSD QLSALADTIL AAALLCAWAD MPKKHRDTPQ FAIVGYGKLG GKELGYASDL
     DLVYLYDDPH PDAGDVYSRL ARRLTNWLST ATGAGSLYET DLRLRPNGDA GFLAHSIAAF
     EKYQRENAWT WEHQSLTRAR FICGTPEIQT AFDRIRTEIL TAERDQTALS GEIIEMREKM
     FPTHPPADSN VKYARGGVVD VEFIVQYLIL AHARQYPQLL DNYGNIALLN IAADCGLIDK
     TLAGQSRTAY RFYRRQQHNT KLRDAKKTEV TGELLAHYGN VRKLWREVFG EEAATA