GLNE_SHIDS
ID GLNE_SHIDS Reviewed; 946 AA.
AC Q32BR1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=SDY_3236;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB63244.1; -; Genomic_DNA.
DR RefSeq; WP_011378869.1; NC_007606.1.
DR RefSeq; YP_404735.1; NC_007606.1.
DR AlphaFoldDB; Q32BR1; -.
DR SMR; Q32BR1; -.
DR STRING; 300267.SDY_3236; -.
DR EnsemblBacteria; ABB63244; ABB63244; SDY_3236.
DR KEGG; sdy:SDY_3236; -.
DR PATRIC; fig|300267.13.peg.3865; -.
DR HOGENOM; CLU_006233_0_1_6; -.
DR OMA; EFMVQYA; -.
DR Proteomes; UP000002716; 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; Reference proteome; Transferase.
FT CHAIN 1..946
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_1000047016"
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; 108516 MW; 3B5CD0D317794C3F CRC64;
MKPLSSPLQQ YWQTVVERLP EPLAEESLSA QAKLVLTFSD FVQDSVIAHP EWLMELESQP
PQADEWQHYA AWLQEALSNV 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 PTLSVIAALH
LFSENDAKQL RVAYLFLRRL ENLLQSINDE QTQTLPSDEL NRARLAWAMD FADWPQLTGV
LTAHMTNVRR VFNELIGDDE SETQEESLSE QWRELWQDAL QEDDTTPVLA HLSEDDRKQV
LTLIADFRKE LDKRTIGPRG RQVLDHLMPH LLSDVCARED AAVTLSRITA LLVGIVTRTT
YLELLSEFPA ALKHLISLCA ASPMIASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ
YLLRVPEDDE EQQLEALRQF KQAQLLRIAA ADIAGTLPVM KVSDHLTWLA EAMIDAVVQQ
AWVQMVARYG KPNHLNEREG RGFAVVGYGK LGGWELGYSS DLDLIFLHDC PMDAMTDGER
EIDVRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGA AGMLVTSAEA FADYQKNEAW
TWEHQALVRA RVVYGDPQLT AHFDAVRREI MALPREGKTL QTEVREMREK MRAHLGNKHR
DRFDIKADEG GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMEEQEAMVL
TRAYTTLRDE LHHLALQELP GHVSEDCFTA ERDLVRASWQ KWLVEE
