GLNE_RHOPT
ID GLNE_RHOPT Reviewed; 990 AA.
AC B3QBR5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Rpal_2144;
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=395960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-2008) 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; CP001096; ACF00665.1; -; Genomic_DNA.
DR RefSeq; WP_012495466.1; NC_011004.1.
DR AlphaFoldDB; B3QBR5; -.
DR SMR; B3QBR5; -.
DR EnsemblBacteria; ACF00665; ACF00665; Rpal_2144.
DR KEGG; rpt:Rpal_2144; -.
DR HOGENOM; CLU_006233_0_0_5; -.
DR OMA; EFMVQYA; -.
DR OrthoDB; 427701at2; -.
DR BioCyc; RPAL395960:RPAL_RS10650-MON; -.
DR Proteomes; UP000001725; 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..990
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_1000212989"
FT REGION 1..474
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 478..990
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 990 AA; 109385 MW; ACB35468FDD1DEFE CRC64;
MIFSAITADL DNTALAARFG AGPRLYDPVL AAERWAGWLV DLAPEQADAI AALGNAFPDL
QIALQSIAEA SPYLFDLIRG DPVRLLRVLR GAPEQRLAKL LEDAETFVAA ASAEDEVMAA
LRRLKAEAAL LIALCDIGGI WPVMQVTQAL TDLAGRSVQM ALRFLLRLEA GRGRIVPPNP
DCPEQGSGLI VLAMGKMGAG ELNYSSDIDL IVFYELDAPT LAPDIEPQPF FVRVTQGLSR
ILQQRRGDGY VFRVDLRLRP DPASTPVALS TVSALDYYER EGRTWERAAM IKARPCAGDL
VAGDALLSEI APFVWRKHLD FAALSDVHDM KRQMQTYRGQ TEIAVEGHNV KVGRGGIREI
EFFAQTQQLI AGGRHPELRV RPTLEALEIL AARNWITIQA RDELTEAYLF LRKVEHRVQM
IADEQTHALP DTVEAIERFS RFLGYDSRDS FARDLLGYLE RVQGHYAKLF EGDPTGTAKL
PPVDYGAGPE DTRLLDHLLS LGYKKPLMIA TTLQQWMTGG YRVLKVETTQ RAFREFVPAL
IEELARAEQP DDAVNAFDRL LQALHRGGRL ISLLSQNREL LTLVALVLGA APRLGDMLAR
QPQILDGLID PRFFGAMPDQ AELSARLAVT LADAGSYEEF LDRLRLFGQE SLFLIGTRIL
SGTVPTQQAA VAFADVAEGI VGTVHGLVSE QFASTYGRVK GQQTAILAMG KLGSREMTAS
SDLDLILIYD FDDDQPDSDG ERSLHGAQYF ARFTQRLISA FTTRTNYGVL YDVDMRLRPS
GRAGPVASRL DAFAAYQEQE AWTWEHLALT RARVISAPPE FRSRIEQVIR AVLTRPRDAA
IIANDVAEMR RAIAQEKGED DVWDLKYAAG GMVDIDFIAQ YLQLVHAHEA PDILHVNTLS
ALDNATRLGL LAQADAEVLR PAARLYQNLT QILRLCVSEK FNPDTAGDDL LRVMVRAGDA
PDFSSLQARV KETQSDVRAI FNRLIGGEDA