ID   GLNE_VIBVY              Reviewed;         950 AA.
AC   Q7MNY4;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=VV0581;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC93345.1; -; Genomic_DNA.
DR   RefSeq; WP_011149486.1; NC_005139.1.
DR   AlphaFoldDB; Q7MNY4; -.
DR   SMR; Q7MNY4; -.
DR   STRING; 672.VV93_v1c05210; -.
DR   EnsemblBacteria; BAC93345; BAC93345; BAC93345.
DR   KEGG; vvy:VV0581; -.
DR   PATRIC; fig|196600.6.peg.600; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_1_6; -.
DR   OMA; EFMVQYA; -.
DR   OrthoDB; 427701at2; -.
DR   Proteomes; UP000002675; Chromosome I.
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..950
FT                   /note="Bifunctional glutamine synthetase
FT                   adenylyltransferase/adenylyl-removing enzyme"
FT                   /id="PRO_0000209284"
FT   REGION          1..443
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT   REGION          450..950
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   950 AA;  108919 MW;  4E2E3D363CBF6C0C CRC64;
     MSLPSPLLPV AELAMQNAQQ SGYLEHWPQA LITQFQFISG LSKFVVETVQ RDAQLAEGLP
     EMLAQESRQE AYRTRLAEQL QACHDEVAGH RVLRQFRNRE MVYIAWKDFT QAWSLEASLS
     HLSELAEAMI FETYQWQYQL CCQEWGTPTN AQGEAQPMLI IGMGKLGGGE LNFSSDIDLI
     FTYPENGETQ GARRSIANAQ FFTRLGQRLI KALDQQTFDG FCYRVDMRLR PFGESGPLVM
     SYAALEDYYQ EQGRDWERYA MIKARVMGRE MYPEYQELRQ MLRPFVFRRY IDFSAIQSLR
     RMKSMISSEV RRRGLSNNIK LGAGGIREIE FIAQVFQLIR GGREPALRQR GLLVTLEAIK
     QLQLLEEAQV CHLVEAYKYL RRLENLLQAM ADKQTQTLPD NELEQLALAV AMGYSQWQAL
     QNDVQQHMAK VHAVFVTLIG DEEDEVSPVE RHFNELWDMA HNPEVIEQIL QNDLACQNAA
     TMSEQIIQFK ADLAKKTLGP RGREVLNRLM PKLFSAIFAD ADAQFGLPRV LHLLHNIATR
     TTYLELLDEH PAALTQLVRL CTASPMISEQ LARYPILLDE LIDPQQLYNP IALDAYRTEL
     RDFLARIPED DVEQQMDALR QFKQICSLRI AAADIAGVLP VMKVSDHLTY LAEAIVEAVV
     HQAWQQVAEK YGEPTHLKDR EGKGFAVVGY GKVGGWELGY NSDLDVVFLH DCPVNVYTDG
     KKEIDGRQFY LRLAQRIIHI FSTRTASGIL YEVDTRLRPS GASGLLVCPV DAFEEYQHND
     AWTWEHQALV RARMIYGDEH LASEFHRVRH QVLAKPREQA KLQKEVADMR AKMRDHLGGK
     KSDRFMLKQD QGGITDIEFL AQYLVLNYSA EKPKLTRWCD NVRIFETLIA QGVMEEAQAM
     LLTQAYTTMR DEIHRRNLLN LDADVALDKF VALRQGVSKA WQEWLESSTI