GLNE_BRADU
ID GLNE_BRADU Reviewed; 995 AA.
AC Q89QJ5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=blr3133;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC48398.1; -; Genomic_DNA.
DR RefSeq; NP_769773.1; NC_004463.1.
DR RefSeq; WP_011085917.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89QJ5; -.
DR SMR; Q89QJ5; -.
DR STRING; 224911.27351391; -.
DR PRIDE; Q89QJ5; -.
DR EnsemblBacteria; BAC48398; BAC48398; BAC48398.
DR GeneID; 64022885; -.
DR KEGG; bja:blr3133; -.
DR PATRIC; fig|224911.44.peg.2766; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_0_5; -.
DR InParanoid; Q89QJ5; -.
DR OMA; EFMVQYA; -.
DR PhylomeDB; Q89QJ5; -.
DR Proteomes; UP000002526; 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..995
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209234"
FT REGION 1..474
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 122..333
FT /note="GlnE 1"
FT REGION 479..995
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 637..853
FT /note="GlnE 2"
SQ SEQUENCE 995 AA; 110119 MW; DCF10D729E67A533 CRC64;
MNHSAPGNAD KHGESLAARF AEAPHIAAST TDERRFESWL AELEPAQSAR LEALLVQPFG
RNILVGIAEF SPYLFDLVRA DPLRLIRLLE CDPDTHLAAL IAEARGAVLA APDEAEVMRL
LRRMKAEAAL LTALCDIGGV WPVMRVTSAL TDVAVSSVQA ALQYLLRQEA ARGKLFPPNP
EAPEEGCGLI VLAMGKMGAG ELNYSSDIDL IVFFDPDATT LAPDIEPQPF FVRVTQGMAR
ILQQRTYDGY VFRVDLRLRP DPSSTQVAIS RDAALHYYER EGRTWERAAM IKARACAGDA
RAGEALLAEI APFVWRKHLD FAALADVHDM KRQMQTYRGQ SEVAVEGHNV KVGRGGIREI
EFFAQTQQLI AGGRHPELRV RPTLAALDVL ASSNWITLAA RDELARAYEF LRRVEHRLQM
VADEQTHALP DDREAVERFA RFFGYPDREA FARDLLRQLE IVQGHYEKLF EGDDPTGTAK
LPALDYSAGP DDPRLFQHLT TLGFKKPAAV AQTVRDWITG DYRVFRNEAT RSAFIEFVPA
LIDGLALAEE PDRAVVAFDQ FLGALQRGGR LITLLGQNRD LVALVALVLG AAPRLGEMLA
RQPQLMDGLI DPRFFGAMPD RRELSGRLAA TVQDAASYEE FLDRLRLFGQ ESLFLIGTRI
LSGTVSAQQA STAFADVAEG VVHTVHDLVA DRFAAQHGRI KGQETAIIAM GRLGSREMTA
SSDLDLILLY DFDSENPDSD GPKSLQGAHY FARFTQRLIS AFTTRTNYGV LYEIDMRLRP
SGRAGPVASS LASFADYQAN EAWTWEHMAL TRARVVSASA EFGERIAGVI RDVLTRRRDP
ATIANDVADM RRAIAQEKGE TDYWDLKYAA GGMIDIDFIA QYLQLVHAHH KPDILDVSTL
QVLDNAARLG VLPQSEAEIL RAAARLYHDL TQILRLCVSD RFKPETAGTD LQRVMARAGD
APDFSSLEAR VKETQSEVRR VFRALLEGTS PASAR
