GLNE_XANP2
ID GLNE_XANP2 Reviewed; 989 AA.
AC A7IL55;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=Xaut_3519;
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000781; ABS68748.1; -; Genomic_DNA.
DR RefSeq; WP_012115494.1; NC_009720.1.
DR AlphaFoldDB; A7IL55; -.
DR SMR; A7IL55; -.
DR STRING; 78245.Xaut_3519; -.
DR EnsemblBacteria; ABS68748; ABS68748; Xaut_3519.
DR KEGG; xau:Xaut_3519; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_0_5; -.
DR OMA; EFMVQYA; -.
DR OrthoDB; 427701at2; -.
DR PhylomeDB; A7IL55; -.
DR Proteomes; UP000002417; 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; Reference proteome; Transferase.
FT CHAIN 1..989
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_1000212990"
FT REGION 1..473
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 479..989
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 989 AA; 107062 MW; 882AE91914E21A60 CRC64;
MRGPLEPDSA DRPSLAILMR EAPVLGDAET AEIKLSQATE SLSPAERAAL DGLLSRAPIA
RAVCLGMAEG SPFLLDLVRA EPTRLLRVLS DDPHAHLARL MADCAATAAS GSEAEVMRAL
RRMRSEAALL IALADMGGAF DLIAVTAALT DVADAALRAA LAFLLGDAAR AGRLKPQDAA
DPAVGCGLAV IAMGKHGARE LNYSSDIDLV VVFDREKAPL AEEVSAAPFF VKITQGLVRL
LQERTADGYV LRVDLRLRPD PGSTAVALST AAALDYYERE GATWERAAYI KARPVAGDLA
VGRTFLAELS PFVWRRGLDF QAIADVHAMK REIHAFRGHD VVAVEGHNVK LGRGGIREVE
FFVQTQQLIA GGRDPLLRNS RTLEALDALT AHRWIEPSVR DALAEAYVFL RRVEHRIQMV
ADAQTHSLPE SRPAMEGFAR FMGYPDRDAF AAALVTRLQT VQTHYANLFE DVAPPAVLDA
DLMFPPDEND RKTLAALSRL GFRDPAAASG MVRRWLSGGP RALKGESARA HLARIVPLML
EALARGGDPD GALAAADRFL SDLPGPQLLT ALDRHPDLVR LLATILTAAP RLGETLARRP
SLTDALLDPA FFDVLPDEAG LTAHLEHLLD TADTDEEQLD RARRFRQEQH VLIGVRIASG
TLEAARAGEA YATLAEVIIR ALHRRVWARF REAHGTIAGA QTAVLAMGKL GGREMTAGSD
LDLIVLYDFD ADADPTSDGA RPLTGAQYFA RFTQRLVTAL TSLTNAGKLY DVDLRLRPSG
RSGPVATRLA SFATYQREEA WTWEHMALTR ARVIAAEPEF GAKVRDVICA VMGQPRDPRR
LAGDILDMRQ SIAAEKGEGD MWNLKHAAGG QVDVEFLAQY LVLAHACAHP EIVDTATARV
LATAARLGLL EPEDAHVLQR ACRLYQNLTQ VLRLAVDAHI VPADASPALR ALLARAGEMP
DFTTLDADLA DTQAKVRTIF ERILETAAE
