GLNE_PSEAE
ID GLNE_PSEAE Reviewed; 982 AA.
AC Q9HUF4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=PA5014;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG08399.1; -; Genomic_DNA.
DR PIR; B83021; B83021.
DR RefSeq; NP_253701.1; NC_002516.2.
DR RefSeq; WP_003114555.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUF4; -.
DR SMR; Q9HUF4; -.
DR STRING; 287.DR97_2369; -.
DR PaxDb; Q9HUF4; -.
DR PRIDE; Q9HUF4; -.
DR EnsemblBacteria; AAG08399; AAG08399; PA5014.
DR GeneID; 881325; -.
DR KEGG; pae:PA5014; -.
DR PATRIC; fig|208964.12.peg.5254; -.
DR PseudoCAP; PA5014; -.
DR HOGENOM; CLU_006233_0_1_6; -.
DR InParanoid; Q9HUF4; -.
DR OMA; EFMVQYA; -.
DR PhylomeDB; Q9HUF4; -.
DR BioCyc; PAER208964:G1FZ6-5130-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..982
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209267"
FT REGION 1..460
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 473..982
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 982 AA; 110104 MW; 8E47E3B5AF685E6B CRC64;
MSLPSLANLP ATLLPAAERA GTALRSAVAA LDAAALARLE AWPEERLEDF RRVAAASDFV
AEQAVRDSAM LLELAERGEL ENPHAPGELR SQLQARLEDC ADEDELGRRL RRFRTRQQLR
IIWRDLTRRA ALAETCRDLS ALADACIDLA CEWLHRRQCE QFGTPIGRRS GEPQRMVVLG
MGKLGAVELN LSSDIDLIFG YPEGGETEGA KRSLDNQEFF TRLGQKLIKA LDAITVDGFV
FRVDMRLRPY GSSGPLVYSF AALEQYYQDQ GRDWERYAMI KARVVGGDQQ AGEQLLGMLR
PFVYRRYLDF SAIEALRTMK QLIQQEVRRK GMSENIKLGE GGIREVEFIA QAFQLIHGGR
DLSLQQRPLL KVLATLEGQG YLPPAVVEEL RGGYEFLRYA EHAIQALADR QTQMLPSDEY
DRIRVAFIMG FASWAAFHER LSHWRARIDW HFRQVIADPD EDESGEAACG SVGAEWIPLW
EEALDEESAS RQLADAGFVD AEAAWKRLSD LRHGPQVRAM QRLGRERLDA FVPRLLAMTV
ENPQPDLVLE RVLPLVEAVA RRSAYLVLLT ENPGALERLL TLCAASPMVA EQIARFPILL
DELLNEGRLF RPPQAAELAA ELRERLMRIP EDDLEQQMET LRHFKLAHGL RVAASEIAGT
LPLMKVSDYL TWLAEAILVE VLELAWRQLV QRHGRPLRAD GTPCDPDFVI VGYGKVGGLE
FGHGSDLDLV FIHDGDPQCE TDGGKSIDGA QFFTRLGQKI IHFLTAQTPS GTLYEVDMRL
RPSGAAGLLV SSLGAFQRYQ EQEAWTWEHQ ALVRARVLAG CRRVQASFEA VRAEVLARPR
DLDALRTEVS EMRAKMRDNL GTRATAAGTA SNAFEATAAF DLKHDAGGIV DIEFMVQYAV
LAWSGEHPAL LEFTDNIRIL EGLERAGLIA SEDVRLLQEA YKAYRAAAHR LALQKEAGVV
SGEHFQTERR EVIRIWRELR LG
