ID   GLNE_MYCS2              Reviewed;         999 AA.
AC   A0R082; I7GD80;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=MSMEG_4293, MSMEI_4192;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK72782.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP40649.1; -; Genomic_DNA.
DR   RefSeq; WP_011729708.1; NC_018289.1.
DR   RefSeq; YP_888570.1; NC_008596.1.
DR   AlphaFoldDB; A0R082; -.
DR   SMR; A0R082; -.
DR   STRING; 246196.MSMEI_4192; -.
DR   PRIDE; A0R082; -.
DR   EnsemblBacteria; ABK72782; ABK72782; MSMEG_4293.
DR   EnsemblBacteria; AFP40649; AFP40649; MSMEI_4192.
DR   GeneID; 66735638; -.
DR   KEGG; msg:MSMEI_4192; -.
DR   KEGG; msm:MSMEG_4293; -.
DR   PATRIC; fig|246196.19.peg.4213; -.
DR   eggNOG; COG1391; Bacteria.
DR   OMA; EFMVQYA; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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..999
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_1000072847"
FT   REGION          1..493
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          498..999
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   999 AA;  109400 MW;  FA89762C1BCE383B CRC64;
     MFVRKPATER PRLPSVGRLG LFDPHAPAHL DQLGWNTDDH VELLWSLSRA PDADAALLAM
     VRLADELKDD WDELNRLLLT DRPLRGRLFA VLGSSLALGD HLVAHPQSWR LLHGDVRLPS
     ARELRETFDD AARSVDIERG ASAAIPPLRD LYRDRLLVLA ALDVASTVEN EPVLPFVTVS
     AHLSDLADAA LSAALIVATR TVCGDLDPRL AVIAMGKCGA RELNYVSDVD VIFVGEDIEK
     DGRSDNLATA TRVAGEMMRF AGDAFFEVDA ALRPEGKRGQ LVRTLDSHVA YYRRWAKTWE
     FQALLKARPA AGDPELGQAY IDALMPMVWT ACEREDFVPE VQAMRRRVEE LVPADVRSRE
     IKLGTGGLRD VEFAVQLLQL VHGRTDESLH VASTVDALAA LGEGGYVGRD DAANMTASYE
     FLRLLEHRLQ LQRLKRTHML PDDNDDEAYR WLARAAHIRP DGTHDAQGVL REELKRQSLR
     VSRLHAKLFY QPLLESVGHT ALGIGEGMSA EAAERQLAAL GYERPQSALA HLAALTGATG
     RKGRIQQILL PTLLDWLSDT PDPDAGLLAY RRLSDEHSDL RWFLGTLRDE GAVAKRLMRV
     LGTSAYIPEL LMRAPEVIQM YADGPSGPKL LEDDRESRAR ALVASASRYA DPVRAIAAAR
     TLRRRELARI ASADVLGMLD VIDVCKSLTA VWVAVLQAAL DVVIRANTPD SGVPARIAVI
     GMGRLGGGEL GYGSDADVMF VCEPNSGVEE SVAVRWSVGV AEQVRALLGT PSADPPLEVD
     TGLRPEGRSG PLVRTLASYD AYYSQWAQPW EIQALLRAHR VAGDLELGER FLLMADKIRY
     PEGGVSASAV QEIRRIKARV DAERLPRGAD PNTHTKLGRG GLADIEWTVQ LLQLRYAHKV
     PALHNTSTLE ALNAIGAAEL VAEGDVELLR EAWLTATRAR NALVLVRGKP TDQLPGPGRQ
     LNAVALAAGW GSDDGGEFLD NYLRVTRRAK AVVRKIFGG