ID GLNE_SALTY Reviewed; 947 AA.
AC Q8ZLY6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 111.
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=STM3201;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL22075.1; -; Genomic_DNA.
DR RefSeq; NP_462116.1; NC_003197.2.
DR RefSeq; WP_000188309.1; NC_003197.2.
DR AlphaFoldDB; Q8ZLY6; -.
DR SMR; Q8ZLY6; -.
DR STRING; 99287.STM3201; -.
DR PaxDb; 99287-STM3201; -.
DR GeneID; 1254724; -.
DR KEGG; stm:STM3201; -.
DR PATRIC; fig|99287.12.peg.3396; -.
DR HOGENOM; CLU_006233_0_1_6; -.
DR OMA; EFMVQYA; -.
DR PhylomeDB; Q8ZLY6; -.
DR BioCyc; SENT99287:STM3201-MONOMER; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0047388; F:[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase activity; 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; IBA:GO_Central.
DR CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR Gene3D; 1.20.120.1510; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR Gene3D; 1.10.4050.10; Glutamine synthase adenylyltransferase GlnE; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 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:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME; 1.
DR PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 2.
DR Pfam; PF03710; GlnE; 2.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..947
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209276"
FT REGION 1..440
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 450..947
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 947 AA; 108037 MW; 4BE3CAFDB2E96B69 CRC64;
MTPLSSPLSQ YWQTVVERLP EGFTETSLSV QAKSVLTFSD FALDSVIAHP EWLAELESAS
PQADEWRHYA GWLQEALAGV CDDASLMREL RFFRRRIMVR IAWAQTLSLV DDETILQQLS
HLAETLIVGA RDWLYAACCR EWGTPCNPQG VPQPLLILGM GKLGGGELNF SSDIDLIFAW
PEHGETRGGR RELDNAQFFT RLGQRLIKAL DQPTMDGFVY RVDMRLRPFG DSGPLVLSFA
ALEDYYQEQG RDWERYAMVK ARLMGDNDDA WSRELRAMLR PFVFRRYIDF SVIQSLRNMK
GMIAREVRRR GLKDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLDAIAALH
LLPENDVAQL RVAYLFLRRL ENLLQSINDE QTQTLPADDL NRARLAWGMK AENWPQLVGE
LTDHMANVRR VFNELIGDDE ADTPQEEERS EPWREVWQDA LQEDDSTPVL AHLADEERRQ
VLTLIADFRK ELDKRPIGPR GRQVLDQLMP HLLADVCSRE DAAVTLSRIT PLLAGIVTRT
TYLELLSEFP GALKHLIMLC AASPMIASQL ARYPLLLDEL LDPGTLYQPT ATDAYRDELR
QYLLRVPEED EEQQLEALRQ FKQAQLLRIA AADIAGTLPV MKVSDHLTWL AEAMIDAVVQ
QAWTQMVARY GQPAHLDERQ GRGFAVVGYG KLGGWELGYS SDLDLIFLHD CPMDVMTNGE
REIDGRQFYL RLAQRIMHLF STRTSSGILY EVDARLRPSG AAGMLVTSAD AFADYQQHEA
WTWEHQALVR ARVVYGDPQL TSQFDAVRRT IMTTARDGKT LQTEVREMRE KMRAHLGNKH
RDRFDIKADE GGITDIEFIA QYLVLRYAHE KPKLTRWSDN VRILELLAQN GIMDEHEAQA
LTVAYTTLRD ELHHLALQEL PGHVAQTCFS KERALVQASW RKWLVAV
//
