GLNE_NOCFA
ID GLNE_NOCFA Reviewed; 1004 AA.
AC Q5YZ84;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=NFA_16610;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD56507.1; -; Genomic_DNA.
DR RefSeq; WP_011208192.1; NC_006361.1.
DR AlphaFoldDB; Q5YZ84; -.
DR SMR; Q5YZ84; -.
DR STRING; 247156.NFA_16610; -.
DR EnsemblBacteria; BAD56507; BAD56507; NFA_16610.
DR GeneID; 61132447; -.
DR KEGG; nfa:NFA_16610; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_1_0_11; -.
DR OMA; EFMVQYA; -.
DR Proteomes; UP000006820; 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..1004
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209261"
FT REGION 1..496
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 502..1004
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 1004 AA; 109461 MW; 3F296121C8A8F601 CRC64;
MVRPPSARSA VPGVGRLGLL DPTAAASLRE LGWDNVESIP VLWALSRAPD ADLALNTLMR
LREALGSDWQ RLDSAIRTDT SLRGRLFALL GSSTALGDHL VAEPAAWEVL RRGDLPDRDE
LLADLLAAVQ ATPEAGPHAG PMLFRAGIAG PEAVALLRCR YRDQLMLLAA LDLAATVENE
PVLPYRVVGR HLTDLADAAL TAALAVAVAR VCKDQPCPVR LAVIAMGKCG ARELNYVSDV
DVVFVAEPAD ATATRLAAEM MSVGSQAFFE VDAALRPEGK QGALVRTLDS HLTYYKRWAR
TWEFQALLKN RPMTGDLELG REYRDAVMPM VWTASERPDF VPEVQGMRRR VEDLVPAELR
ERELKLGRGS LRDVEFAVQL LQLVHGRVDE NLHVASTVDA LSALAAGGYV GRDDAANLTA
SYEFLRLLEH RLQLQRLKRT HTLPADDDEE GMRWLARAAH IRPDGRQDAM GVLRSEIRRN
AVRVRRLHAK LFYRPLLEAV VRMDPDALRL SPDAAVRQLA ALGYAAPENA FGHLKALTGG
VSRKGRIQAL LLPTLLEWLG ETPNPDAGLL AYRRVSEALD EQTWFLRELR DEGAVAQRLM
IVLGSSEFLP DLLINAPETI RMFADGPHGP LLLGPQPEEV ARGILTAAAR YDDPNRAVAA
ARSLRRHELA RVASADLLGM LEVPQVCRAL SSVWVAVLDA ALAAVIRAGE AESGEPAPAA
FAVIGMGRLG GMELGYGSDA DVLFVCEPRP GVDETKAVKW ANTVAERVQR LLGAPSTDPP
LHVDAGLRPE GRSGALVRTL SAYQAYYGQW AQSWEVQALL RAHQVAGDQE LGVRFLHAVD
KVRYPAGGVS EDAVREIRRI KARVDSERLP RGADPATHTK LGRGGLADIE WTVQLLQLRH
AHEVESLHNT ATLETLAAIE KAELLAAEDV ALLRDSWLLA TKARNALVLV RGKPSDQLPG
PGRLLSAVAT VAGWPNNDGG SEFLDHYLRI TRRARAVVER VFGS
