ID   GLNE_RHOP2              Reviewed;         988 AA.
AC   Q2IUH4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=RPB_3440;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-2006) 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: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; CP000250; ABD08136.1; -; Genomic_DNA.
DR   RefSeq; WP_011442320.1; NC_007778.1.
DR   AlphaFoldDB; Q2IUH4; -.
DR   SMR; Q2IUH4; -.
DR   STRING; 316058.RPB_3440; -.
DR   PRIDE; Q2IUH4; -.
DR   EnsemblBacteria; ABD08136; ABD08136; RPB_3440.
DR   KEGG; rpb:RPB_3440; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_0_5; -.
DR   OMA; EFMVQYA; -.
DR   OrthoDB; 427701at2; -.
DR   Proteomes; UP000008809; 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; Transferase.
FT   CHAIN           1..988
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_1000212987"
FT   REGION          1..474
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          480..988
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   988 AA;  108893 MW;  F5CBB62206755DDA CRC64;
     MSSSAIDADI SPASLAARFA AGPQLHAPDE AEKRCADWLA DVPAELAAPI RAVADRCPNL
     RIALQSIAEA SPYLFDLIRA DPARLLRLLR SEPETGFRAL LDATAAAVAT ASDEAEVMAV
     LRRMKAEAAL SIALCDIGGL WPVLQVTQAL TDLAVQSVQM TLRFLLRQEA ARGRIHPPNP
     DAPEERSGLI VLAMGKMGAG ELNYSSDIDL IVFYELDAPT LAPDIEPQPF FVRVTQGLSR
     ILQQRRHDGY VFRVDLRLRP DPASTPVALS TASALNYYER EGRTWERAAM IKARACAGDV
     VAGEALLSEI APFVWRKHLD FAALSDVHDM KRQMQTFRGQ TEVAVEGHNV KVGRGGIREI
     EFFAQTQQLI AGGRHPELRV RPTLAALDIL ANRDWITFQA RDELSAAYQF LRRVEHRIQM
     IADEQTHTLP DSIEAVERFS RFFGYASREA FARDLLAHLD CVQGHYSKLF EGDPTGTAKL
     PIDYAGGAED TVLLDHLRAL GYKKPLMVAT TLQQWMAGGY RILKVEATQR AFNDFVPALI
     EELARAEEPD NAVNAFDRLL QALHRGGRLI SLLSQNRDLL TLIALVLGAA PRLGDMLARQ
     PQIMDGLIDP RFFGAMPDRT ELSARLAATL SDAGSYEEFL DRLRLFGQES LFLIGTRILS
     GTVSTQQASI AFADVAEGIV GTVHDLVSKQ FVSQYGRIKD QETAILAMGK LGSREMTAAS
     DLDLILIYDF DHEQPDSDGE RSLHGAQYFA RFTQRLISAF TTRTNYGVLY DVDMRLRPSG
     RAGPLASRLD SFAEYQEVEA WTWEHLALTR ARVISASPEF RARIEQVIRA VLTRPRDAAI
     ANDVAEMRAA IAQEKGEGDV WDLKYAAGGM VDIDFIAQYL QLVHAATMPD ILAVGTLSAI
     DNAARLGVLA QPDADVLRPA ARLYHDLTQI LRLCVSDKFK PETAGDDLLR VLVRAGDAPD
     FSSLQARVKE TQAEVRAIFN RLIGGNGE