ID A0A399G376_9ACTN Unreviewed; 1004 AA.
AC A0A399G376;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=NI17_002320 {ECO:0000313|EMBL:UOE20103.1}, NI17_09175
GN {ECO:0000313|EMBL:RII02917.1};
OS Thermobifida halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=483545 {ECO:0000313|EMBL:RII02917.1};
RN [1] {ECO:0000313|EMBL:RII02917.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:RII02917.1};
RA Toth A., Tancsics T.A., Farkas T., Papp P., Olasz F., Balint B.,
RA Herczeg R., Nagy I., Baka E., Kukolya J.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UOE20103.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:UOE20103.1};
RA Nagy I., Horvath B., Kukolya J., Nagy I., Orsini M.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2020) 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; JRUV01000212; RII02917.1; -; Genomic_DNA.
DR EMBL; CP063196; UOE20103.1; -; Genomic_DNA.
DR RefSeq; WP_068692600.1; NZ_LIZN01000014.1.
DR AlphaFoldDB; A0A399G376; -.
DR STRING; 483545.GCA_001660385_01302; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000265719; 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: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; 3.30.460.10; Beta Polymerase, domain 2; 2.
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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000265719};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:RII02917.1}.
FT DOMAIN 77..323
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 345..490
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 595..831
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 872..1000
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..494
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 502..1004
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 1004 AA; 109289 MW; 55857B4A7B3165A0 CRC64;
MSVGALARRG FGDAARAARL LTEAGLDPVA HEPVVDAISR SADPDLALLG LGRIVERSEE
AADLRTALLD DADLRDRLIR VLGASRALAD HLVRHPGDWR ELRGADAARL PDAEELRAGL
LHVVGADPNS PAPTADLSAF DVAEVTHALR LAYRRRVLRL AGRDLTGVQD LKEVATELAD
LAAAVLEGSL AVARARFPKD AARCRLAVIG MGKCGGRELN YVSDVDVVFV AEPADGFSDE
HAALEAATRL AAAMMEIPRQ TDAEGTLWEV DAALRPDGRN GPLVRPLAGH VAYYERWAKT
WEFQALLKAR PIAGDAELGA AYARAISPMV WQAAGRPNFV EDVQAMRRRV ESHIPHTEVD
RQLKLGRGGL RDIEFAVQLL QLVHGRGDDS LRSGNTLEAL EALSRGGYVG RQDAAGMADS
YRFLRRVEHL LQLHRLRRTH LLPDSRTESG QQELRRLGRS LGFTANPVTD LAATWRRRAG
EVRRLHEKLF YQPLLKAVAR LPEDEARLSP EQARTRLEAL GFLDPAGALR HLEALTSGVT
RRAAIQRTLL PVMLGWFADS PAPDAGLLGF RQVSDALGTT PWYLRLLRDD IRVAERMAYL
LGTSRYVTDL LLRAPEAVAL LADDADLAQR RDAELIAEAN AALRRHDTAE NQVAGVRALR
RRELLRTAAA DLLGVTDIDG VGDALTAIAS VTIDAALRAA TERVAHQRGA EPCTRMCVIA
MGRFGGNELS YTSDADVMYV HDPLPGADPA EAAATAGAIV RELARLLELP AAEPPVRLDA
ALRPEGKSGP MVRTFDSYAA YYTRWASSWE SQALLRAMPV AGDAGLGERF TALIDPIRYP
EGGPSDQALR EIRRLKARME AERLPRGADP TLHTKLGRGG LSDVEWTVQL LQLRHAHAVP
ELRTTGTLQA LNAAVRGGLL DPDDGATLEV AWRLASRVRG AVTLVRGRGG DSIPTDLRER
TAIAGALGYR ADDSEAGPGE LMVEEYRRAT RRARAVMERV FYDS
//
