GLNE_CORGL
ID GLNE_CORGL Reviewed; 1045 AA.
AC Q79VE2; Q9AEL3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
GN OrderedLocusNames=Cgl2228, cg2446;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11445173; DOI=10.1111/j.1574-6968.2001.tb10738.x;
RA Nolden L., Farwick M., Kraemer R., Burkovski A.;
RT "Glutamine synthetases of Corynebacterium glutamicum: transcriptional
RT control and regulation of activity.";
RL FEMS Microbiol. Lett. 201:91-98(2001).
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; BA000036; BAB99621.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20569.1; -; Genomic_DNA.
DR EMBL; AJ310086; CAC34379.1; -; Genomic_DNA.
DR RefSeq; NP_601431.1; NC_003450.3.
DR RefSeq; WP_011014971.1; NC_006958.1.
DR AlphaFoldDB; Q79VE2; -.
DR SMR; Q79VE2; -.
DR STRING; 196627.cg2446; -.
DR KEGG; cgb:cg2446; -.
DR KEGG; cgl:Cgl2228; -.
DR PATRIC; fig|196627.13.peg.2165; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_1_0_11; -.
DR OMA; EFMVQYA; -.
DR BRENDA; 2.7.7.42; 960.
DR Proteomes; UP000000582; 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..1045
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209243"
FT REGION 1..527
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 533..1045
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 1045 AA; 116395 MW; 9939706285D680BD CRC64;
MSGPLRSERK VVGFVRDPLP KVGSLSLKSE HAQADLEHLG WRNVESLDLL WGLSGAGDPD
VALNLLIRLY QALEAIGEDA RNELDQEIRQ DEKLRVRLFA LLGGSSAVGD HLVANPLQWK
LLKLDAPSRE EMFQALLESV KAQPAVLEVE DFSDAHNIAR DDLSTPGFYT ASVTGPEAER
VLKWTYRTLL TRIAAHDLAG TYPTDMRRKG GDPVPFSTVT MQLSDLADAA LTAALAVAIA
NVYGEKPVDS ALSVIAMGKC GAQELNYISD VDVVFVAEPA NSKSTRTAAE LIRIGSNSFF
EVDAALRPEG KSGALVRSLD SHMAYYKRWA ETWEFQALLK ARPMTGDINL GQSYVDALSP
LIWTASQRES FVTDVQAMRR RVLDNVPEDL RDRELKLGRG GLRDVEFAVQ LLQMVHGRID
ETLRVRSTVN ALHVLVDQGY VGREDGHNLI ESYEFLRLLE HRLQLERIKR THLLPKPDDR
MNMRWLARAS GFTGSMEQSS AKAMERHLRK VRLQIQSLHS QLFYRPLLNS VVNLSADAIR
LSPDAAKLQL AALGYLHPSR AYEHLTALAS GASRKAKIQA MLLPTLMEWL SQTAEPDAGL
LNYRKLSDAS YDRSWFLRML RDEGVVGQRL MRILGNSPYI SELIISTPDF MKQLGDAASG
PKLLATAPTQ VVKAIKATVS RHESPDRAIQ AARSLRRQEL ARIASADLLN MLTVQEVCQS
LSLVWDAVLD AALDAEIRAA LNDPQKPDQP LANISVIGMG RLGGAELGYG SDADVMFVCE
PVAGVEEHEA VTWSIAICDS MRSRLAQPSG DPPLEVDLGL RPEGRSGAIV RTVDSYVKYY
EKWGETWEIQ ALLRAAWVAG DRELGIKFLE SIDRFRYPVD GATQAQLREV RRIKARVDNE
RLPRGADRNT HTKLGRGALT DIEWTVQLLT MMHAHEIPEL HNTSTLEVLE VLEKHQIINP
VQVQTLREAW LTATAARNAL VLVRGKRLDQ LPTPGPHLAQ VAGASGWDPN EYQEYLENYL
KVTRKSRQVV DEVFWGVDSM EQREF
