GLNE_METCA
ID GLNE_METCA Reviewed; 948 AA.
AC Q605D9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=MCA2345;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017282; AAU91502.1; -; Genomic_DNA.
DR RefSeq; WP_010961573.1; NC_002977.6.
DR AlphaFoldDB; Q605D9; -.
DR SMR; Q605D9; -.
DR STRING; 243233.MCA2345; -.
DR PRIDE; Q605D9; -.
DR EnsemblBacteria; AAU91502; AAU91502; MCA2345.
DR KEGG; mca:MCA2345; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_6; -.
DR OMA; EFMVQYA; -.
DR OrthoDB; 427701at2; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; ISS:JCVI.
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:0006542; P:glutamine biosynthetic process; ISS:JCVI.
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..948
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209253"
FT REGION 1..445
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 451..948
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 948 AA; 106527 MW; 0EB7140FB6C9A957 CRC64;
MAPPPDTSGS CSAFHECERI FAQWGYPFQD YSESFRQSLD TVCRCSRFFL GVVKRDAHVI
PLLASLFEGQ TPERNPSADL QQRVAEVADR NGLMRVLRQW RNREMAIIAW QDICGLLDID
SVLTRISETA ESAIRTALDW LFDDACRRWG VPRRKDGSAQ SLVVLGMGKL GGYELNFSSD
IDLVFAYVED GELPGRNGAT YAEFYTRLAQ SLVHVLDAVT EDGFVFRVDV RLRPFGESGP
LVVSFDSCER YYQAQARDWE RYAMVKVRAV GGDAKDGREF ERFFHPFVYR RYLDYRVFGE
LRSLKARIMA ELRRKDRGDN IKLGAGGIRE IEFIGQAFQL IRGGRNVELQ DRRILVVLER
LGRLRLLEHG TASFLCAAYR FLRKVENRLQ QYEDKQTHEL PVSEERRGLL AFSMGFESWE
GFLHRLDEVR RRVHEIFTEV IAEPPQPARG EPLLDGGEAE LSQALAGFDG AAEAMTGALV
KFRASAPVRR LGAGARAELQ RVIGKLLAEL AAFRVSDPVG VLGRILELFE SIAGRGVYFS
LLAENPSALS QLVRLAAASP WIVRLIAGAP ILLDELLDPR TLYSPLTRES LGREADILFS
SLAPDDDEQL MLRLRQFKAA HQLRIAAADI MNVIPVMVVS DYLTDLAEVV IERVLRLAWK
FAAARHGIPP VEAETSVDFP GFGIIAYGKL GGIELGYGSD LDLVFLYDGV ASDAVTDGPR
PISAAEFYAR VVQRMVSLLT ADMPGGALYE VDLRLRPSGS SGLLVSKADA YENYQLHQAW
TWERQALVRA RFVAGDPKVG ARFDAIRRNV LCRERDSRQV RLDVRSMREK MREHLADRRP
GVFDLKQGVG GIADIEFIVQ FGVLISAAKH CEITRWTDTV RLLDSLRAIN FLELGQADRL
RCAYCDYRGR VHRLALQEMP ALAASSEFPG HRTAVEAVWK QIIEAPVF
