ID   GLNE_BIFLO              Reviewed;        1076 AA.
AC   Q8G654;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-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=BL0795;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN24610.1; -; Genomic_DNA.
DR   RefSeq; NP_695974.1; NC_004307.2.
DR   RefSeq; WP_011068132.1; NC_004307.2.
DR   AlphaFoldDB; Q8G654; -.
DR   SMR; Q8G654; -.
DR   STRING; 206672.BL0795; -.
DR   EnsemblBacteria; AAN24610; AAN24610; BL0795.
DR   KEGG; blo:BL0795; -.
DR   PATRIC; fig|206672.9.peg.496; -.
DR   HOGENOM; CLU_006233_1_0_11; -.
DR   OMA; EFMVQYA; -.
DR   PhylomeDB; Q8G654; -.
DR   Proteomes; UP000000439; 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; 2.
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..1076
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_0000209230"
FT   REGION          1..521
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          524..1076
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          1042..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1056
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1076
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1076 AA;  120297 MW;  46952BB350066E7D CRC64;
     MESSIFKPSS MDLIRAGLQD LDKARALFDQ LKADDIPDER CAELLSALAH ACDPDMALSN
     FVDIVNAMQS SQRDLEHVIP DNDALKRLVT VLGVSDAMGK FMRFKPQLVE AAAVDNCNSH
     LFNHAQRRAR LLKAVGADPD EPAMPVASKD LAEAATALRS SYRNQLAAII AQDAVADDPA
     SIQPTISREL SDLADAALEG ALAIARHETE GSEHVRFTII GMGKLGAQEL NYVSDVDLIY
     VVEPADKDVD HQTLIRVGTK MGTMLQRVCQ SAIMGVAEQP LWQIDGGLRP EGKDGALVRV
     LSSHKNYYEQ WAENWEFQAL LKARPVAGDP DLGRAYMDMT RPFVWSASKR KNFVYDCQKM
     RKRVEDLIPA PLKDREIKLG RGGLRDVEFT VQMLQLVHGR TDESLRTSNT LDSLQRLSEG
     GYVSRKQAVR MSQDYRFERV MEHRQQIWSL KRTHLFPDLG RASVGGLEKK RDIDVDELNQ
     NQELRRLARA FGLHPEELVD KYDDTRREVR HLHLDIYYRP MLPVNAQMEN DQIVLSVEAA
     QERFESIGFG DPDAAIRHVQ ALTAGVGRAA KINRIILPAV LQWLGEGQNP DMGLLNWRKL
     EENFGTESGY LGFLRDSTSA AQRLCHILSN SRFLGDALNK SVESISWLGD DDNLQARTRE
     ALDVQTGSAL ERFGSNINEF ATSMRAMRRH EIERIGLSWM SGVISDSDSL KAMTDVYDAI
     IDASLTWAVR HQIAEFGVET APAGITVIAM GRYGGREVNF SSDADAILIY RPADDADDGQ
     ANAFAKKVVE DLRNILQGPT TLEPKIELDL DLRPEGKNGP LVRSYASCEE YYESWASTWE
     RQALLRARYA AGDAELARDF LINIADPLRY PTTELTEAEL QNIRKLKARM EAERLPRGVR
     RERHLKLGKG GLSDVEWTVQ LMQLQHAGDI KDLRVNGTLE ALDVLEAKKL ISAIDAIQLR
     KAWTLCTAAR NGSYLWSGRA NQADILPDDI YSLGGIAVYL GYGAHRGQHF ENDLLAVMRK
     CRDVCQRLFY GKTEGEAAAA TTATASAATQ QPQTAPRPRM HVIAPRLERN RRRAQR