GLNE_PASMU
ID GLNE_PASMU Reviewed; 986 AA.
AC Q9CNQ2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=PM0375;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02459.1; -; Genomic_DNA.
DR RefSeq; WP_010906614.1; NC_002663.1.
DR AlphaFoldDB; Q9CNQ2; -.
DR SMR; Q9CNQ2; -.
DR STRING; 747.DR93_1150; -.
DR EnsemblBacteria; AAK02459; AAK02459; PM0375.
DR KEGG; pmu:PM0375; -.
DR PATRIC; fig|272843.6.peg.388; -.
DR HOGENOM; CLU_006233_0_1_6; -.
DR OMA; EFMVQYA; -.
DR Proteomes; UP000000809; 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..986
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209263"
FT REGION 1..475
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 481..986
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 986 AA; 113973 MW; EF5DBA01AD82869A CRC64;
MSFPLAHVDA TLNQLAKQLI AHFPEQYQDQ IFQHIATDKE KPTSNIGQLR YAIAMSDFFA
ETLQKQPHFL HQCWQQCPRL QDCEQYAERL TPLLAQVENE EQLYKVLRQF RHREMAKLSF
CQSLNLGSVE DIFIRLSQLA ESVIIGARDW LYQRACAEMG TPVDEQGTPL QLYILGMGKL
GGFELNFSSD IDLIFTYASN GETVGARRSI DNAKFFTRLG QRLINALDQY TCDGFVYRTD
MRLRPFGENG ALALSFAAME LYYQEQGRDW ERYAMIKGRI LGANAQDPHV NTLQQLLRPF
VYRRYIDFSV LQALRDMKHK IEREVRRRGL VDNIKLGAGG IREIEFIVQV FQLIRGGRES
ALQQPALLKV LPEISALELI SAQQQEDLRQ AYLFLRRTEN ILQAIHDQQT QQLPENTLDQ
QRLVLATQRF TQWDTQNKLE TVTYPIHDWA SFCEVLQQHQ QNVRTVFDHL IGEEKEELSE
TETLWHDFLE NEIEESEIEQ MLIEHHIEER DFHEIIEKLM QFRNEVTRRP IGTRGRIALT
QVMPTLLPQI FAHTAYLHLL PRMLNIVDKI LTRTTYLELL VENPQALTQL IELCAQSRMI
AEQVARHPIL LDELLDRNAL LNPPPYDHYA SELRQYLLRL TPDDEEQMID GLRQFKQATL
LRIAAADILG ALPVMKVSDH LTFLAEAIIH VVVELAWQQV TTRFGTPAHL AEGEKGFLVI
GYGKLGGIEL GYKSDLDLVF LYQSDEQSQT CGGKRSIESN QFYLRLAQKI ISIFSINTFA
GVLYEVDMRL RPSGESGLLC SSISAFKAYQ LHDAWTWEKQ ALVRSRAIYG EARLQTEFNA
IRAEVLSAPR DLATLQQDVV AMRQKMYAHL AHPDSDTFNI KTDRGGITDI EFIAQYLVLA
HAPQNPALTR WSDNVRIFEI MAESAVISQE ICDQLKQCYV DLRNRIHHLN LLGELSIVPQ
TEFQTERQFI QTIWHRLFEH NDKYEE
