ID S5MUK9_SALBN Unreviewed; 947 AA.
AC S5MUK9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 ORFNames=A464_3232 {ECO:0000313|EMBL:AGR60416.1};
OS Salmonella bongori N268-08.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1197719 {ECO:0000313|EMBL:AGR60416.1, ECO:0000313|Proteomes:UP000015042};
RN [1] {ECO:0000313|EMBL:AGR60416.1, ECO:0000313|Proteomes:UP000015042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N268-08 {ECO:0000313|EMBL:AGR60416.1,
RC ECO:0000313|Proteomes:UP000015042};
RA Marti R., Hagens S., Loessner M.J., Klumpp J.;
RT "Genome sequence of Salmonella bongori N268-08 - a rare clinical isolate.";
RL Submitted (JUL-2013) 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 -!- 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};
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00802};
CC -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000256|HAMAP-
CC Rule:MF_00802}.
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DR EMBL; CP006608; AGR60416.1; -; Genomic_DNA.
DR RefSeq; WP_020845274.1; NC_021870.1.
DR AlphaFoldDB; S5MUK9; -.
DR GeneID; 66757499; -.
DR KEGG; sbz:A464_3232; -.
DR PATRIC; fig|1197719.3.peg.3224; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_6; -.
DR Proteomes; UP000015042; 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 activity; 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 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00802}; Ligase {ECO:0000313|EMBL:AGR60416.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00802};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00802};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00802};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00802};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:AGR60416.1}.
FT DOMAIN 31..273
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 297..436
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 554..806
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 826..918
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
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..947
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 947 AA; 108008 MW; 38C6F51FF02C57CD CRC64;
MTLLSSPLPQ YWQTVVERLP AQFTETSLSA QAKSVLTFSD FVLDSVAAHP EWLAGLESAS
PQADEWRHYA AWLQETLAEV CDEISLMREL RLFRRRIMVR IAWAQALSLV EDEHILQQLS
HLAETLIIGA RDWLYAACCR EWGTPCNLQG VPQPLLILGM GKLGGGELNF SSDIDLIFAW
PEHGSTQGGR RELDNAQFFT RLGQRLIKVL DQPTMDGFVY RVDMRLRPFG DSGPLVLSFA
ALEDYYQEQG RDWERYAMVK ARIMGDNDDA WSRELRAMLR PFVFRRYIDF SVIQSLRNMK
GMIAREVRRR ELKDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLKAIAMLH
LLPERDVAQL RSAYLFLRRL ENLLQSINDE QTQTLPGDDL NRARLAWGMH SDSWPQLVDK
LTEHMANVRR VFNELIGDDE NDTPQEEALS EPWREVWQDA LQEDDSTPVL AHLTRDARQQ
VLTLIADFRK ELDKRPIGPR GRLVLDQLMP HLLADVCSRE DAAVTLSRIM PLLAGIATRT
TYLELLSEFP GALKHLITLC AASPMIASQL ARYPLLLDEL LDPGTLYQPT ATDAYRDELR
QYLLRVPEED EEQQLEALRQ FKQAQLLRIA AADIAGTLPV MKVSDHLTWL AEAMIDAVVQ
QAWTQMVARY GQPTHLDERS GRGFAVVGYG KLGGWELGYG SDLDLIFLHD CPMDVMTNGQ
REIDGRQFYL RLAQRIMHLF STRTSSGILY EVDARLRPSG AAGMLVTSME AFADYQQNEA
WTWEHQALVR ARVVYGDPQL TSQFDAVRHT ILTAARDGKT LQTEVREMRE KMRAHLGNKH
RDRFDIKADE GGITDIEFIA QYLVLRYAHE NPKLTRWSDN VRILALLAQN GIMDEHETQA
LTVAYTTLRD ELHHLALQEL PGHVAQTCFS KARALVQASW RKWLAAV
//
