GLNE_MYCA1
ID GLNE_MYCA1 Reviewed; 998 AA.
AC A0QEW1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=MAV_2245;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) 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; CP000479; ABK69160.1; -; Genomic_DNA.
DR RefSeq; WP_009976481.1; NC_008595.1.
DR AlphaFoldDB; A0QEW1; -.
DR SMR; A0QEW1; -.
DR EnsemblBacteria; ABK69160; ABK69160; MAV_2245.
DR KEGG; mav:MAV_2245; -.
DR HOGENOM; CLU_006233_1_0_11; -.
DR OMA; EFMVQYA; -.
DR OrthoDB; 427701at2; -.
DR Proteomes; UP000001574; 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; Transferase.
FT CHAIN 1..998
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_1000072846"
FT REGION 1..487
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 492..998
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 998 AA; 108705 MW; FB7EC0F0AC5221C4 CRC64;
MVVTKPATQR PRLPSVGRLG LVDPQAAERM AQLGWYDHDD QAHVDLLWAL SRAPDPDAAL
LALVRLAETP DAGWDELGAA LLTERPLRGR LFAVLGSSLA LGDHLVAQPR SWKLLRGNVS
LPTHDELCAM FTGCVDEALA DPGSAMVRLR TLYRDRLLVL AALDLAATVE DEPVLPFTVV
AAHLSDLADA ALAAALRVAE HNVCGDRTPP RLAVIAMGKC GARELNYVSD VDVIFVGERA
DTVTTRVASE MMRLASEAFF QVDAGLRPEG RSGELVRTVE SHIAYYQRWA KTWEFQALLK
ARAAVGDAEL GRRYLDALMP MVWVACERED FVVEVQAMRR RVEQLVPADV RGREIKLGSG
GLRDVEFAVQ LLQLVHGRSD ESLHVASTVD ALAALGQGGY IGREDAANLT ASYEFLRLLE
HRLQLQRLKR THLLPEADDE EAVRWLARAA HIRPDGRHDA AGVLREELRH QNLRVSQLHA
KLFYQPLLES IGPAGLEIRH GMTSEAAERQ LAALGYEGPQ SALKHMSALV NQSGRRGRVQ
SVLLPRLLNW MSYAPDPDGG LLAYRRLSEA LAGESWYLST LRDKPAVARR LMHVLGTSAY
VPDLLMRAPR VIQDYGDGPS GPRLLETDPA AVARALVASA SRYSDPVRAI AGARTLRRRE
LARVASADLL GMLEVTDVCK ALTSVWVAVL QAALDAMIRA NLPDDGPQRG KAPAAIAVIG
MGRLGGAELG YGSDADVMFV CEPAPGVDDS AAVRWAASVA EQVRTLLGTP SVDPPLDVDA
NLRPEGRNGP LVRTLASYAA YYEQWAQPWE IQALLRAHAV AGDAELGQRF LLMADKTRYP
ADGVSPEAVR EIRRIKARVD AERLPRGADP NTHTKLGRGG LADIEWTVQL LQLLHAHEVP
ALHNTSTLEC LDAIAEAGLV PADEVDLLRQ AWLTATRARN ALVLVRGKPT DQLPGPGRQL
NAVAVAAGWP TDEGGEFLDN YLRVTRRAKA VVRKVFGS
