ID   A0A5B7KLH8_ECOLX        Unreviewed;       946 AA.
AC   A0A5B7KLH8;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   26-FEB-2020, entry version 3.
DE   RecName: Full=Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00802};
DE   AltName: Full=ATP:glutamine synthetase adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE   AltName: Full=ATase {ECO:0000256|HAMAP-Rule:MF_00802};
DE   Includes:
DE     RecName: Full=Glutamine synthetase adenylyl-L-tyrosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              EC=2.7.7.89 {ECO:0000256|HAMAP-Rule:MF_00802};
DE     AltName: Full=Adenylyl removase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AR {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AT-N {ECO:0000256|HAMAP-Rule:MF_00802};
DE   Includes:
DE     RecName: Full=Glutamine synthetase adenylyl transferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              EC=2.7.7.42 {ECO:0000256|HAMAP-Rule:MF_00802};
DE     AltName: Full=Adenylyl transferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AT {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AT-C {ECO:0000256|HAMAP-Rule:MF_00802};
GN   Name=glnE {ECO:0000256|HAMAP-Rule:MF_00802,
GN   ECO:0000313|EMBL:MPD07754.1};
GN   ORFNames=D9E74_003780 {ECO:0000313|EMBL:MPD07754.1};
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:MPD07754.1};
RN   [1] {ECO:0000313|EMBL:MPD07754.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CVM N17EC0326 {ECO:0000313|EMBL:MPD07754.1};
RA   Tyson G.H., Li C., Hsu C.-H., Bodeis-Jones S., Mcdermott P.;
RT   "Diverse Fluoroquinolone Resistance Plasmids from Retail Meat E. coli in
RT   the United States.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MPD07754.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CVM N17EC0326 {ECO:0000313|EMBL:MPD07754.1};
RG   NARMS: The National Antimicrobial Resistance Monitoring System;
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00802,
CC       ECO:0000256|SAAS:SAAS00959950}.
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:0000256|HAMAP-
CC         Rule:MF_00802, ECO:0000256|SAAS:SAAS01118276};
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:0000256|HAMAP-
CC         Rule:MF_00802, ECO:0000256|SAAS:SAAS01118275};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00802,
CC         ECO:0000256|SAAS:SAAS00959956};
CC   -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000256|HAMAP-
CC       Rule:MF_00802, ECO:0000256|SAAS:SAAS00959957}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MPD07754.1}.
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DR   EMBL; ROAP02000001; MPD07754.1; -; Genomic_DNA.
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:0016874; F:ligase activity; IEA:UniProtKB-KW.
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   HAMAP; MF_00802; GlnE; 1.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR30621; PTHR30621; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959941}; Ligase {ECO:0000313|EMBL:MPD07754.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000256|SAAS:SAAS00959949};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959951};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959952};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959943, ECO:0000313|EMBL:MPD07754.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959945, ECO:0000313|EMBL:MPD07754.1}.
FT   DOMAIN          31..276
FT                   /note="GlnE"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          297..436
FT                   /note="GlnD_UR_UTase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          553..805
FT                   /note="GlnE"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          825..916
FT                   /note="GlnD_UR_UTase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   REGION          1..440
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT   REGION          449..946
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   946 AA;  108448 MW;  9E97C6B42187AB85 CRC64;
     MKPLSSPLQQ YWQTVVERLP EPLAEESLSA QAKSVLTFSD FVQDSVIAHP EWLTELESQP
     PQADEWQHYA AWLQEALCNV SDEAGLMREL RLFRRRIMVR IAWAQTLALV TEESILQQLS
     YLAETLIVAA RDWLYDACCR EWGTPCNAQG EAQPLLILGM GKLGGGELNF SSDIDLIFAW
     PEHGCTQGGR RELDNAQFFT RMGQRLIKVL DQPTQDGFVY RVDMRLRPFG ESGPLVLSFA
     ALEDYYQEQG RDWERYAMVK ARIMGDSEGV YANELRAMLR PFVFRRYIDF SVIQSLRNMK
     GMIAREVRRR GLTDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLSAIAELH
     LLSENDAEQL RVAYLFLRRL ENLLQSINDE QTQTLPSDEL NRARLAWAMD FADWPQLTGA
     LTAHMTNVRR VFNELIGDDE SETQEESLSE QWRELWQDAL QEDDTTPVLA HLSEDDRKQV
     LTLIADFRKE LDKRTIGPRG RQVLDHLMPH LLSDVCARED AAVTLSRITA LLVGIVTRTT
     YLELLSEFPA ALKHLISLCA ASPMIASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ
     YLLRVPEDDE EQQLEALRQF KQAQLLRIAA ADIAGTLPVM KVSDHLTWLA EAMIDAVVQQ
     AWVQMVTRYG KPNHLNEREG RGFAVVGYGK LGGWELGYSS DLDLIFLHDC PMDAMTDGER
     EIDGRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGA AGMLVTSAEA FADYQKNEAW
     TWEHQALVRA RVVYGDPQLT AHFDAVRREI MTLPREGKTL QTEVREMREK MRAHLGNKHR
     DRFDIKADEG GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMEEQEAMAL
     TRAYTTLRDE LHHLALQELP GHVSEDCFTA ERELVRASWQ KWLVEE
//