ID   GLNE_PSEPK              Reviewed;         977 AA.
AC   Q88QZ4;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=PP_0340;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN65971.1; -; Genomic_DNA.
DR   RefSeq; NP_742507.1; NC_002947.4.
DR   RefSeq; WP_010951694.1; NC_002947.4.
DR   AlphaFoldDB; Q88QZ4; -.
DR   SMR; Q88QZ4; -.
DR   STRING; 160488.PP_0340; -.
DR   EnsemblBacteria; AAN65971; AAN65971; PP_0340.
DR   KEGG; ppu:PP_0340; -.
DR   PATRIC; fig|160488.4.peg.367; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_1_6; -.
DR   OMA; EFMVQYA; -.
DR   PhylomeDB; Q88QZ4; -.
DR   BioCyc; PPUT160488:G1G01-373-MON; -.
DR   Proteomes; UP000000556; 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..977
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_0000209268"
FT   REGION          1..457
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          468..977
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   977 AA;  109433 MW;  1159DA2BC1589296 CRC64;
     MRLPLPSDLP ATLQPLVTRN QQFISDAVAG HPELDLQAWS PLHRQQFDQV AAASEFVLSL
     AQREPAMLFA LLASGELERR YAPGELRGQI AATAQAAQSE DELARNLRRA RNRQQLRIIW
     RDITRQAELG ETCRDLSDLA DAAIDEAYQW LYPRHCQQFG TPIGNRSGQP QHMVVLGMGK
     LGAVELNLSS DIDLIFGFPE GGETEGVKRS LDNQEFFTRL GQRLIKALDP VTVDGFVFRV
     DMRLRPYGSA GALVLSFNAL EQYYQDQGRD WERYAMIKAR VVAGDQAAGA QLQEMLRPFV
     YRRYLDFSAI EALRTMKQLI QQEVRRKGMA ENIKLGAGGI REVEFIAQAF QLIHGGRDLS
     LQQRPLLKVL ATLEGQGYLP PAVVAELREG YEFLRYTEHA IQAIADRQTQ MLPEGETDQA
     RVAYVLGFAD WQSFHDQLMY WRGRIDWHFR QVIADPDDED GEGELVVGGE WSPLWEQAQD
     EEAAGRQLQE AGFKQPAEAL RRLAGLRSSP QLRSMQRIGR ERLDAFIPRL LAQAVEHDNP
     DLVLERVLPL VEAVARRSAY LVLLTENPGA LRRLLTLCAA SPWIAEQIAL YPLLLDELLN
     EGRLFSPPLA PELASELRER LTRIPEDDLE QQMEALRHFK LAHSLRVAAS EISGNLPLMK
     VSDYLTWLAE AILDQVLALA WRQTVARHGQ PKRSDGSLCD PGFIIIGYGK MGGLELGHGS
     DLDLVFIHDG DPQAETDGAK PIDSAQFFTR LGQRIIHLLT TQTNSGQLYD VDMRLRPSGA
     SGLLVSSLGA FERYQQNEAW TWEHQALVRA RVLVGCKQVG AAFEGVRAKV LGQARDLEKL
     RGEVSEMRAK MRDNLGTKAT AAGTAANAFD AGVPFDIKQD AGGIVDIEFM VQYAALAWSH
     DHPAILRWTD NIRILEELEQ ANLMPASDAV LLREVYKAFR SASHRQALQK EAGVIDAAQF
     ADERREVRRI WGELGLS