GLNE_NITEU
ID GLNE_NITEU Reviewed; 929 AA.
AC Q81ZZ7;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=NE1329;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD85240.1; -; Genomic_DNA.
DR RefSeq; WP_011111907.1; NC_004757.1.
DR AlphaFoldDB; Q81ZZ7; -.
DR SMR; Q81ZZ7; -.
DR STRING; 228410.NE1329; -.
DR EnsemblBacteria; CAD85240; CAD85240; NE1329.
DR KEGG; neu:NE1329; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_4; -.
DR OMA; EFMVQYA; -.
DR OrthoDB; 427701at2; -.
DR PhylomeDB; Q81ZZ7; -.
DR Proteomes; UP000001416; 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..929
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209260"
FT REGION 1..423
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 433..929
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 929 AA; 106323 MW; 8EDFD709635DE9DB CRC64;
MSTPIDSSRA ASIVASILPY SRYLKRTLAS EPGLQQELLD QLPNPFLWEE MLDFLQHPAI
SLEDEADLHR LLRQLRKRVI LRLAARDLAG LADLNEVMTT MTALADTTIR FALEFLHTAM
THPGHFGKPT GEKTGTEQQL LIVAMGKLGG GELNVSSDVD LIFIYPEDGE TDGRKSITNH
EFFVRLGRKL IASLSDYTVD GYVFRVDMRL RPHGENSPLA ISLPMLEDYF ITQGREWERH
AWIKSRVITG SSVAEATLME LIVRPFVFRK YLDFEAYEAM RSLHAQLRKE VDRRELHDNI
KLGPGGIREI EFITQVFQLI RGGRDADLCI RPTLGVLRRL RQKQPLPGQT IEELTEAYCF
LRKLEHRLQY LDDQQTQNLP QHPDEQTLIA RSMGFTGYGD FLDHLDLHRQ NVTRHFEQIF
AARRKSPRHD TFARIRPEQS GDHETVEAFS KQLQTLGYLD PGKITARVRQ FYDSTFFRQL
THSSQERIFE LMPTLMEVIA RFPPVDITLE RILRLLEKIG QYPAYLALLQ EHPQTLPRVA
KLASVSQWAS DYLGRHPILL DELLTSSGLH ILPDWPALKT ELTHQLHHVN IPKVQMVEWQ
MDVLRHFQHA QVFRLLVTDL EGDLLLEKLS DHLTELADLI LDNVLQLAWQ GLKKKHRELP
AFAIIGYGKL GGKELGYASD LDIVFLYRDD HPDAASIYTK LAQNINLWLT SHTSAGILYE
TDLRLRPNGT SGLLVNSIEA FTQYQYEQAW VWEHQALTRA RFVVGDREAG EMFEQMRKNM
LCQPRDLVKL KREILMMRSK MLEAHPNPTP LFDIKHDRGG IIDVEFIVQY LVLGYAHRYP
QLTGNIGNIA LLKLAGELGL TSAGKATAAL TAYRELRRTQ HQLRLSGTPE PAGTALSRDV
SQKFARVANN HLSDARQAVF QLWEDIFGT
