GLNE_ECO8A
ID GLNE_ECO8A Reviewed; 946 AA.
AC B7LZK2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=ECIAI1_3200;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAR00014.1; -; Genomic_DNA.
DR RefSeq; WP_001365952.1; NC_011741.1.
DR AlphaFoldDB; B7LZK2; -.
DR SMR; B7LZK2; -.
DR PRIDE; B7LZK2; -.
DR KEGG; ecr:ECIAI1_3200; -.
DR HOGENOM; CLU_006233_0_1_6; -.
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..946
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_1000133900"
FT REGION 1..440
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 449..946
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 946 AA; 108361 MW; 0B1214C0CBE9BD74 CRC64;
MKPLSSPLQQ YWQTVVERLP EPLAEKSLSA QAKSVLTFSD FVQDSVIAHP EWLTELESQS
PQADEWQHYA AWLQEALSNV SDEAGLMREL RLFRRRIMVR IAWAQTLALV TEESILQQLS
HLAETLIVAA RDWLYDACCR EWGTPCNAQG EAQPLLILGM GKLGGGELNF SSDIDLIFAW
PEHGCTQGGR RELDNAQFFT RMGQRLIKVL DQPTQDGFVY RVDMRLRPFG ESGPLVLSFA
ALEDYYQEQG RDWERYAMVK ARIMGDSEGV YANELRAMLR PFVFRRYIDF SVIQSLRNMK
GMIAREVRRR GLTDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLSAIAALH
LLSENDAEQL RVAYLFLRRL ENLLQSINDE QTQTLPSDEL NRARLAWAMD FADWPQLTGA
LTAHMTNVRR VFNELIGDDE SETQEESLSE QWRELWQDAL QEDDTTPVLA HLSEDDRKQV
LTLIADFRKE LDKRTIGPRG RQVLDHLMPH LLSDVCARED AAVTLSRITA LLVGIVTRTT
YLELLSEFRA ALKHLISLCA ASPMIASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ
YLLRVPEDDE EQQLEALRQF KQAQLLRIAA ADIAGTLPVM KVSDHLTWLA EAMIDAVVQQ
AWVQMVARYG KPNHLNDREG RGFAVVGYGK LGGWELGYSS DLDLIFLHDC PMDAMTDGER
EIDGRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGA AGMLVTSAEA FADYQKNEAW
TWEHQALVRA RVVYGDPQLT AHFDAVRREI MTLPREGKTL QTEVREMREK MRAHLGNKHR
NRFDIKADEG GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMEEQEAMAL
TRAYTTLRDE LHHLALQELP GHVPEDCFTA ERELVRASWQ KWLVEE
