GLNE_THISH
ID GLNE_THISH Reviewed; 970 AA.
AC B8GL43;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=Tgr7_0463;
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584; DOI=10.4056/sigs.1483693;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL71561.1; -; Genomic_DNA.
DR RefSeq; WP_012637050.1; NC_011901.1.
DR AlphaFoldDB; B8GL43; -.
DR SMR; B8GL43; -.
DR STRING; 396588.Tgr7_0463; -.
DR PRIDE; B8GL43; -.
DR EnsemblBacteria; ACL71561; ACL71561; Tgr7_0463.
DR KEGG; tgr:Tgr7_0463; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_6; -.
DR OMA; EFMVQYA; -.
DR OrthoDB; 427701at2; -.
DR Proteomes; UP000002383; 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..970
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_1000148546"
FT REGION 1..454
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 468..970
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 970 AA; 109710 MW; FB9E4A75AF79FAFC CRC64;
MNSLPPRPSL DVLPEALRPD LIRLLDDFES ACARDGIALD HWPEALVRVW AGSGFAARIA
IRRPNLLLEL IQDGTLARPL EAGEMAARVS AVVQAAQDEA ALMRDLRLLR QREMMRIAWR
DLSGEAGLDE TLGDLTDLAE HCIDQAAAWV HGQLVQRHGE PRDAEGRPQR LVVLGMGKLG
GRELNFSSDV DLIFTYAARG ETDGEKPLDN QQFFIRLGQR LIRLLDENTA EGFVFRVDMR
LRPFGDAGPL VMDFDTLEGY YESHGREWER YALIKARVVA GDREAGRELM RALRPFVFRR
YLDYGAFAAL RDMKAMINRE AARRSRGDDV KLGEGGIREV EFIGQAFQLI RAGRDPRLQL
RGIRPVLRRL AEMELMPGYV VDQLITAYEF LRRTENHLQM AQDQQTHRLP ESDEARLRLA
FSMGHDDWEG FSRELARHRR RVQEHFQQVF AAPQGEAEEA AGAEGPGQAV LASIWAGDRS
GERAQAVLAE AGFRDAPKAL EWIEDLREGA ACRSLTATGR ERLDQLMPLL LGAAAGAEDP
DTVLSRLVTL VRSIARRSVY LSLLVESPMA LSQLVKLCDA SPWIAQLLTR HPLLLDELLD
PRSLYAPMDR EGLSAELDEE LSQVPEDDME QMMDRLRQFQ QVQMLKVAAA DIMGVLPLMK
VSDHLTWIAE VVLERVLSLV MAQLHARYGR PRCLIDGRPY EPGFAIIGYG KLGGLELGYG
SDLDIVFLHD SAGEQQMTDG DKALDNSEFF ARLGQRIVHV LGTYTGAGRL YEVDTRLRPS
GASGLLVSSL KAFELYQETK AWTWEHQALV RARPVAGDAH IAEGFAEIRR RVLGICRDRE
KLRQEVREMR EKMWSEHASR DPSRFNLKRD PGGIADIEFM VQYWVLAYAC DHPPLLDYPD
NIRILERLVV TGVLPEEDAR FLTDTYREFR NRIHRLTLQE SDAVVDAAEF AEQRETVRAL
WRRVMEEGKA
