ID   GLNE_XANC8              Reviewed;         937 AA.
AC   Q4UZ80;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=XC_0562;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
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; CP000050; AAY47643.1; -; Genomic_DNA.
DR   RefSeq; WP_011038683.1; NC_007086.1.
DR   AlphaFoldDB; Q4UZ80; -.
DR   SMR; Q4UZ80; -.
DR   PRIDE; Q4UZ80; -.
DR   EnsemblBacteria; AAY47643; AAY47643; XC_0562.
DR   KEGG; xcb:XC_0562; -.
DR   HOGENOM; CLU_006233_0_1_6; -.
DR   OMA; EFMVQYA; -.
DR   OrthoDB; 427701at2; -.
DR   Proteomes; UP000000420; 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; Transferase.
FT   CHAIN           1..937
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_1000047018"
FT   REGION          1..436
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          443..937
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   937 AA;  102203 MW;  3A026930D62F380E CRC64;
     MSQPIPSASP ALAALIERAV ARVRHALPAD APWPEGVEHP LARVALASDF VVDTLARQPA
     LLAHLAQPDP PPLPVPRLDP AQPQEWAAQL RRYRAAASAR LVWRDVLGLD DVDATLAGAT
     TLAETCLQCA LQALEQQFST RHGQVIAEDG SVQRLVVFGL GKLGGGELNF SSDVDLVYAY
     PQAGQSDGAR PLAAEEYFAR LGQQLARLLD ETTADGFSHR VDLRLRPFGS AGRVALSFNG
     MDQYFQREGR DWERYAWLKA RAVAGDIAAG EAWLETLRPF VYRRYLDFTA LDGLRDMKAA
     ITAEVAHHAR LDDIKRGPGG IREIEFLAQS LQLIRGGREA SLRERRLLPA LQALVDLGQI
     DPPTGQALAD AYRFLRRVEN RLQMLRDAQT HALPQGEPER ERIALGLGYA HWQALLEALA
     PHRTRVAAEF AELLAPRVHA TAPDTLADYW RALPEGDAAP LLGIGLHDPN NAHHMLADFA
     QSSGVRALSD GARTRLDRVM PALLHAAIRA TQPDAALRRV LGLLQATLRR TSYLALLDEQ
     PSALARLVDV LSRSALLAER LAAYPLLLDE LLDTRISGPL PDRAALHTAC VDTLQIDDTE
     AALRELNERR LALSFRIALA TLDGRQQPVD STQQLAWLAE AVVQTVLQLA RRELVAAHGQ
     VPGGAFAIIG YGSLGGLELG FGSDLDLVFL YDHPREVEAS DGKRPLEAGR WFARLAQKVM
     TLLGAETGAG RLYDIDVRLR PDGGKGALVS SLASYRDYQR DRAWTWEHQA LVRARAVAGD
     AALCEAFVQV RRETLTRVRD PALLHEDVRK MRARMRSELD RSDAGRLDLK QGAGGLVDLE
     FLLQAGVLGQ AAQHPALLLA CATPALIDAL VQVQWLPAES AAPLHHAHAT LVEAGLSCTL
     DRRPRLVVST PPIRDACQIV AAIADAQQLR FQPGKGA