GLNE_MANHA
ID GLNE_MANHA Reviewed; 963 AA.
AC Q9FD13;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 62.
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};
OS Mannheimia haemolytica (Pasteurella haemolytica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=75985;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Highlander S.K.;
RT "Mannheimia haemolytica glutamine synthetase adenylyltransferase.";
RL Submitted (AUG-2000) 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; AF293652; AAG02477.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9FD13; -.
DR SMR; Q9FD13; -.
DR STRING; 75985.WC39_04920; -.
DR PRIDE; Q9FD13; -.
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; Transferase.
FT CHAIN 1..963
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209262"
FT REGION 1..453
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 461..963
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 963 AA; 111282 MW; D2788541142AACEE CRC64;
MLTTLIPLSQ LNLPPNLQNS EQIQPLVTAE FASNFVHQTL QKQPDLLAEW LAKFPTPDDC
CNYTERLAKI LARVPNEEML GRVLRQFRHR ELARLSFIQS NKLATVELVF QHLSDLAESL
ILAARDWLFQ RCCAEYGTPK NTLGETQELL ILGMGKLGGR ELNFSSDIDL IFTYPDIGET
EGGRKSIENS KFFTRMAQRL IKVLDEITAD GFVYRTDMRL RPFGDSGRLV LSFTAMEDYY
QEQGRDWERY AMIKAKILGE DSQNLNHRYL KQMLRPFVYR RYLDFSAIQS LREMKEKISR
EVVRRNLTDN IKFGAGGIRE VEFIAQTFQM IRGGRDKILQ ERSLLKVLPR LAELNLLTQT
QVETLHNAYI FYRQIENVLQ AIDDKQTQTL PTDEASQARL VFACQSYYQQ DLYSEKTHWV
EHSFNDWQQF MAVLSQYQQA VRQIFNEIIG EEETQANCNP VNEKLAEWKD ILHYNIRLED
LSAVLKGYPK VAENDYTEIF RHFSTTFQDW VKRPIGVRGR EVLRNLMPRI ADSIFKGEDH
LLLLPRVLNI VDKITTRTTY LELMLEKEQI LPQLLALCSK SVMIAEQIAR YPMLLDELMS
HRGLTDVQAF EKYQSALQDY LIRIPEEDEE ALIDGLRQFK QTQILRIAAA DILGVLLVMK
ISDHLTYLAE AIINAVVNMA WKQVSQRFGV PEHLEADEKG FAVIGYGKLG GIELGYNSDL
DLVFLHNAPE DSQTVGGKKE ISSHQFYLKL AQKINSIFNL NTSAGVLYEV DMRLRPSGEA
GLLVSTFNAY EHYQKNEAWT WESQALVRTR CVFGAENLKQ AFEKIRQSTL AQPRASGQLR
QEICEMRQKM YQHLSSHSAE QFHIKQDQGG ITDIEFIAQY LVLAHSHQHP KMAVWSDNVR
IFDSAVECGI LSSEQSEQLQ HCYTALRNKI HHLKLLRKDS VVDASEFTTE RAFVREMWQR
LLA
