ID   GLNE_NITEC              Reviewed;         929 AA.
AC   Q0AGL4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=Neut_1266;
OS   Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=335283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101675 / C91 / Nm57;
RX   PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA   Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA   Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT   "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT   eutropha C91: implications for niche adaptation.";
RL   Environ. Microbiol. 9:2993-3007(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; CP000450; ABI59518.1; -; Genomic_DNA.
DR   RefSeq; WP_011634337.1; NC_008344.1.
DR   AlphaFoldDB; Q0AGL4; -.
DR   SMR; Q0AGL4; -.
DR   STRING; 335283.Neut_1266; -.
DR   EnsemblBacteria; ABI59518; ABI59518; Neut_1266.
DR   KEGG; net:Neut_1266; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_1_4; -.
DR   OMA; EFMVQYA; -.
DR   OrthoDB; 427701at2; -.
DR   Proteomes; UP000001966; 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..929
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_1000212986"
FT   REGION          1..422
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          429..929
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   929 AA;  106389 MW;  90084B4FF322989E CRC64;
     MTTPISTSRA ASIVSSILPY SRYLKRVLEN ESELQQELLE QLHNPFTREE MLGFLQDSTA
     HLIDEADLHR LLRQLRKRVI LRLAARDLAG LADLNEVMAT MTALADVTIQ FSLEFLHAAM
     VQPGHFGKPK GEKTGTEQQL LIVAMGKLGG GELNVSSDVD LVFIYPEDGE TDGSKSITNH
     EFFLRLGRKL IASLNDYTVD GYVFRVDMRL RPYGENSPLA ISLPMLEDYF VTQGREWERH
     AWIKSRVITG SSIAEAALME LIVRPFVFRK YLDFEAYEAM RSLHTQLRKE VDRRELHDNI
     KLGPGGIREI EFITQVFQLI RGGRDADLCI RPTLGVLQRL KQKQPLPEQT VEELIEAYYF
     LRKLEHRLQY LDDQQTQNLP QHSDDQILIA KSMGFTDYTG FLKHLDLHRQ NVTRHFEQIF
     AVRRKAIKLG TFARIRPEQT NDNEIVKVFS NQLKTLGYID PDKITARVQQ FYDGTTFRQL
     SHPNQERILE LMPTLMEVVT RFPPVEITLE RMLRLLEKIG QYSAYLALLQ EYPQTLPRVA
     KLVSISQWAS DYLGSHPILL DELLAPSGLH TLPDWPTLKT ELIHQLHHGN IPKAQIIEWQ
     MDVLRHFQHA QVFRLLAVDL EGNLLLETLS DHLTALADLI LDNVLQLAWQ GLKKKHRKSP
     AFAIIGYGKL GGKELGYVSD LDIVYLYQDN HPDAMEIYTK LAQNINLWLT SHTSAGVLYE
     TDLRLRPNGT SGLLVNSIEA FSLYQHEQAW VWEHQALTRA RFVIGDSEVG EKFEQMRKNI
     LCQPRDMENL KREILMMRTK MLEAHPNSTP LFDVKHDHGG IIDVEFIVQY LVLGYAHRYP
     QLTSNIGNIA LLKLAGELGL TSAEKANAAF IAYRELRRTQ HQLRLSGIPE ATGTALPKDV
     SQKFARVTSD YLSSARRAVF QLWEDVFGT