ID   GLNE_MYCMM              Reviewed;         995 AA.
AC   B2HHM1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=MMAR_3293;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; CP000854; ACC41719.1; -; Genomic_DNA.
DR   RefSeq; WP_012394947.1; NC_010612.1.
DR   AlphaFoldDB; B2HHM1; -.
DR   SMR; B2HHM1; -.
DR   STRING; 216594.MMAR_3293; -.
DR   EnsemblBacteria; ACC41719; ACC41719; MMAR_3293.
DR   KEGG; mmi:MMAR_3293; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_1_0_11; -.
DR   OMA; EFMVQYA; -.
DR   OrthoDB; 427701at2; -.
DR   Proteomes; UP000001190; 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..995
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_1000133908"
FT   REGION          1..487
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          492..995
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   995 AA;  108542 MW;  F3FF5B4E2D5AC3FB CRC64;
     MNVTKPATQR PKLPSVGRLG LVDALAGARL AELGWTEHDD QAHVDLLWSL SRAPDADAAL
     KVLVRLAENP DTGWDELNAA LLNERSLRGR LFAVLGSSLS LGDHLVANPQ SWKLLRGKVA
     LPSHAALLES FVDLAEEVAA APASAVHRLR ALHRDHVLVL AGLDLAATVE DEPVLPFTVV
     AAHLADIADA ALAAALRLAE KTVCRDRTPP RLAVIAMGKC GARELNYVSD VDVIFVAERA
     DPISIRVAGE MMRVASSTFF EVDAGLRPEG RSGELVRTVE SHIAYYQRWA KTWEFQALLK
     ARAAVGDAEL GQSYLAALMP MVWTACERDD FVAEVQAMRR RVEQLVPADI RGRELKLGTG
     GLRDVEFVAQ LLQLVHGRSD ESLHVASTVD ALSALGEGGY IGREDAANMI ASYEFLRLLE
     HRLQLQRLKR THLLPEFDDE EAVRWLARAA HIRPDGRHDA AGMLREELKH QNVRVSRLHA
     KLFYQPLLES IAPAGLEIAG RGMTSEAAER QLAALGYEGP QTALKHMAAL VNHSGRRARV
     QSVLLPRLLD WLSYAPDPDG GLLAYRRLSE ALATQSWYLS TLRDKPTVGR RLMHVLGTSA
     FVPDLLMRAP EVIQNYGDGR TGPKLLETEP AAVARALIAS AGRYSDPLRA IAAARTLRRR
     ELARIGSADL LGLLEVTEVC RALTSVWVAV LQSALEAMIR ANTPEGGRPL ARIAVIGMGR
     LGGSELSYGS DADVMYVCEP ASGVTDAQAV KWSTAVAEQV RAKLGTPSVD PPLEVDANLR
     PEGRNGPLVR TLASYEAYYA QWAQAWEIQA LLRAHAVAGD AELGQRFLLL VDHTRYPPDG
     VSAEAVHEIR RIKARVESER LPRGADPNTH TKLGRGGLAD IEWTVQLLQL QNAHEIEALH
     NTSTLESLDA IAEAKLVAED EVKLLRQAWL TATRARNALV LVRGKPTDQL PGPGRQLNAV
     AVAAGWHNDD GGEFLDNYLR VTRRAKAVVR KVFGS