GLNE_BARHE
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 03-AUG-2022, entry version 87.
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=BH04800;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
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 derivative
RT 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, 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; BX897699; CAF27288.1; -; Genomic_DNA.
DR RefSeq; WP_011180411.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q6G488; -.
DR SMR; Q6G488; -.
DR STRING; 283166.BH04800; -.
DR PaxDb; Q6G488; -.
DR PRIDE; Q6G488; -.
DR EnsemblBacteria; CAF27288; CAF27288; BH04800.
DR GeneID; 64156761; -.
DR KEGG; bhe:BH04800; -.
DR eggNOG; COG1391; Bacteria.
DR OMA; EFMVQYA; -.
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 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; 1.
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..974
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209228"
FT REGION 1..464
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 468..974
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-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
