ID   GLNE_HAEIN              Reviewed;         981 AA.
AC   P44419;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=HI_0069;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC21747.1; -; Genomic_DNA.
DR   PIR; G64046; G64046.
DR   RefSeq; NP_438242.1; NC_000907.1.
DR   RefSeq; WP_005693853.1; NC_000907.1.
DR   AlphaFoldDB; P44419; -.
DR   SMR; P44419; -.
DR   STRING; 71421.HI_0069; -.
DR   EnsemblBacteria; AAC21747; AAC21747; HI_0069.
DR   KEGG; hin:HI_0069; -.
DR   PATRIC; fig|71421.8.peg.70; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_1_6; -.
DR   OMA; EFMVQYA; -.
DR   PhylomeDB; P44419; -.
DR   BioCyc; HINF71421:G1GJ1-70-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..981
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_0000209249"
FT   REGION          1..479
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          483..981
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   981 AA;  112759 MW;  8B2B82376B814883 CRC64;
     MTALSALIEQ KLQSLGTILC QSFPELSPEK IHEAIQQNSN HPELPVYQLG YAIAMSDFVE
     KVLQKYPHLV KQWWEKSPCF ADCTAYIERL NKELANVHDE TALYQTLRQF RNIEMAKLSF
     CQSLNLATVE EIFVQLSQLA ESLIIAARDW LYHQACAEIG TPMDEQGNPQ QLYILGMGKL
     GGFELNFSSD IDLIFTYPSQ GETSVENTNA RRSVDNGKFF TRLGQRLISA LDEFTSDGFV
     YRTDMRLRPF GDSGVLVLSF SAMEQYYQDQ GRDWERYAMI KGRVLGAQTK DPNVSKLKKM
     LRPFVYRRYI DFSVIQSLRE MKGKIEREVR RRGLKDNIKL GAGGIREVEF IVQVFQLIRG
     GREINLQQHS LLKILPEITK LRLITEQQFH DLRESYIFLR RVENILQAIN DQQTQTLPTD
     EIDQIRLVEA CKTFTCLNEN NQTIEKHYPI ENWDDFYRTL QQKQEKVRAV FTQLIGDEQD
     ESSQTDSQWQ DFLEADFEDI EQTLLESSVS ENNIDEVLEK LAQFKDGLNH RVIGSRGRDV
     LSHLMPTVLA LIFEQENYRT LLPRILNIIE KISSRTTYLE LLLENPRALQ QVIELCAQSQ
     LISEQLAHYP ILLDELLNTE ALRHPLPFTQ YPAELHQYLL RLPPDDEEQL IDALRQFKQA
     TLLKVAAADI LGALPVMKVS DHLTYLAEAI IEVVVNLAWK QVSSRFGVPE HLQNNEKGFL
     VIGYGKLGGI ELGYKSDLDL VFLYDAVESQ TTGGKKVIDS NQFYLRLAQK IVSIFSINTS
     AGVLYEADMR LRPSGDAGLI GCSLSAFSHY QLNDAWTWEK QALVRARPVF GESSLKAKFE
     HIRQQVLSAS RDIEQLKQDV VEMRKKMFAH LSHSKHSEFN LKTDRGGITD IEFIAQYLML
     ANAPKKPQLT KWSDNVRIFD DMAEAKIISQ TDCDTLKQCY VDLRNTIHHL NLLGKSSVVE
     DSEFVKERSF IQAFWDRLFV S