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Database: UniProt
Entry: Q6G488
LinkDB: Q6G488
Original site: Q6G488 
ID   GLNE_BARHE              Reviewed;         974 AA.
AC   Q6G488;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 77.
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};
GN   OrderedLocusNames=BH04800;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC   -!- FUNCTION: Involved in the regulation of glutamine synthetase GlnA,
CC       a key enzyme in the process to assimilate ammonia. When cellular
CC       nitrogen levels are high, the C-terminal adenylyl transferase (AT)
CC       inactivates GlnA by covalent transfer of an adenylyl group from
CC       ATP to specific tyrosine residue of GlnA, thus reducing its
CC       activity. Conversely, when nitrogen levels are low, the N-terminal
CC       adenylyl removase (AR) activates GlnA by removing the adenylyl
CC       group by phosphorolysis, increasing its activity. The regulatory
CC       region of GlnE binds the signal transduction protein PII (GlnB)
CC       which indicates the nitrogen status of the cell.
CC       {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-
CC         COMP:10661, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:83624, ChEBI:CHEBI:456216; EC=2.7.7.89;
CC         Evidence={ECO:0000255|HAMAP-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-
CC         COMP:10661, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.42;
CC         Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; BX897699; CAF27288.1; -; Genomic_DNA.
DR   RefSeq; WP_011180411.1; NZ_LRIJ02000001.1.
DR   ProteinModelPortal; Q6G488; -.
DR   SMR; Q6G488; -.
DR   STRING; 283166.BH04800; -.
DR   PaxDb; Q6G488; -.
DR   PRIDE; Q6G488; -.
DR   EnsemblBacteria; CAF27288; CAF27288; BH04800.
DR   GeneID; 29620491; -.
DR   KEGG; bhe:BH04800; -.
DR   eggNOG; ENOG4105CE6; Bacteria.
DR   eggNOG; COG1391; LUCA.
DR   HOGENOM; HOG000256492; -.
DR   KO; K00982; -.
DR   OMA; EFMVQYA; -.
DR   BioCyc; BHEN283166:G1GJ7-497-MONOMER; -.
DR   Proteomes; UP000000421; 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   HAMAP; MF_00802; GlnE; 1.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR30621; PTHR30621; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 1.
DR   Pfam; PF03710; GlnE; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Magnesium; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    974       Bifunctional glutamine synthetase
FT                                adenylyltransferase/adenylyl-removing
FT                                enzyme.
FT                                /FTId=PRO_0000209228.
FT   REGION        1    464       Adenylyl removase. {ECO:0000255|HAMAP-
FT                                Rule:MF_00802}.
FT   REGION      468    974       Adenylyl transferase. {ECO:0000255|HAMAP-
FT                                Rule:MF_00802}.
SQ   SEQUENCE   974 AA;  110251 MW;  34A11A226BC7D3C9 CRC64;
     MKNAFLKTQL LPLRPLDESG SQWLKDITEQ ARKENLESLV SSLSNQGKQI NFLNAVMTLS
     PFLREVLIAN PSYLSPLLYV DIETRLSEII EDITLIDKNK SIHETTLMAA LRRKKREAHV
     LIALADLGGV FTYEISCAWL TRLGEAALGV ALRFLLREAH DHGKINLSNR EDPEKDCGLI
     ILGMGKFGAG ELNYSSDIDL IVFIDEMSPH VGNLSESIDV FSKMVRRLIR IIQERTAEGY
     VFRLDFRLRP DPGSTPLALP VRTALRYYEG RGQNWERAAM IKARPVAGDK SAGFNFLKEL
     FPYVWRKYLD YAAIADIHSI KRQIHAYKNY DQISAYGHNI KLGRGGIREI EFFVQTQQLI
     AGGRFPQLRG RQTVAMLAEL HRLGWISEKT RDSLVKSYAF LRNVEHRIQM LADEQTHILP
     IDVSQFTSVA YLMGYQETNS FICDLLKTLQ VVEKHYAALF ENEQELGLEI GNLVFTGEED
     DPETLITLRR LGFERASDIC RIMRTLHCGR YKSTQSAEAR ERLTELTPAL LKAFGATKRA
     DEVMLRFDSF LQGLPSGIQL FSLLQSNPSL LDMLVLIMGA APRLAEIITH KPHVFDGMLD
     PTIFSELPTK TYLKNRLEYF LEGVISYEEI LDHLRVFADE QRFLIGIRIL NGAITGKKAG
     FAFTALADLI IAKTFATVQE EFSRLHGNIK GGRVGILGMG KLGSCELTAG SDVDLILLYE
     HDEDAEISDG GKPLYIFQYY TRLTQRLVAA LSTLTSQGIL YAVDLRLRPL GNKGPVAVSF
     EFFRKYYRKE AWIWEHLALT RARGIAGDLD FLQKLENEVY EIIAFSRNKK DVIKAVCEMH
     VLIGKGKPPE NRWDLKRMPG GIMHLEFIAQ FALITHVIVF QIGATTADIL TQLPNSFLNQ
     SFISDLHHAY GLYTNLSQII RLCLNDALDL NNMPPGLSDL LLSSVGEPDL LRVEKLIEET
     GQLVYSIFKQ VMKY
//
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