GLNE_BRUME
ID GLNE_BRUME Reviewed; 983 AA.
AC Q8YG35;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=BMEI1327;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL52508.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008917; AAL52508.1; ALT_INIT; Genomic_DNA.
DR PIR; AI3417; AI3417.
DR RefSeq; WP_004683327.1; NZ_GG703778.1.
DR AlphaFoldDB; Q8YG35; -.
DR SMR; Q8YG35; -.
DR STRING; 224914.BMEI1327; -.
DR PRIDE; Q8YG35; -.
DR EnsemblBacteria; AAL52508; AAL52508; BMEI1327.
DR GeneID; 29594178; -.
DR KEGG; bme:BMEI1327; -.
DR PATRIC; fig|224914.52.peg.79; -.
DR eggNOG; COG1391; Bacteria.
DR OMA; EFMVQYA; -.
DR PhylomeDB; Q8YG35; -.
DR Proteomes; UP000000419; Chromosome I.
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..983
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209235"
FT REGION 1..468
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 473..983
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 983 AA; 109444 MW; 012BD3A12F7F2A9D CRC64;
MTVENAKALF FERNLCALTP LDPERASAFL ADLEARAREE ELAGVVALLG RKKAADFLSA
ILDLSPFIRE ALTRQPRILD RIVSATPESA LEAILDEISA SGTVAGVSES ELMTSLRQLK
REAHVLIALC DLARIFNTET TTDRLTDLAE ACTGAAVRFL LLDADAAGRI NLPDRSNPEK
DCGWIVLGMG KFGARELNYS SDIDLIVFID ETKPAIGDPY ECVDTFSRLT RRLVRILQDR
TGDGYVFRVD LRLRPDPGST PLAIPVGAAL HYYEGRGQNW ERAAMIKARP VAGDRLSGKQ
ILAELSPYVW RKYLDYAAIA DVHSIKRQIH AHKGHGDIAV RGHNVKLGRG GIREIEFFVQ
TQQLIAGGRF PELRGNQTVP MLARLAERGW ITQQARDALA QEYWFLRDVE HRIQMIADEQ
THILPEDDEG FARVSHMMGY ADPAEFSEIF LAALKVVEKQ YAALFEQAPE LGAASGNLVF
TGDVDDPGTL ETLSAMGYER SSDICRVIRT WHFGRYRATQ SAEARERLTE LTPALLKAFA
ETRRADESLL RFDGFLQGLP AGIQLFSLLQ SNPRLLNLLV MIMSAAPRLA DIITRNPHVF
DGLLDPAIFS EVPTRAYLEE RLRAFLGSAT DFEEVLDRLR IFAAEHRFLI GIRLLTGAIN
GVRAGQAFSD LAELMVGRAL EAVEAELQRR HGKVKGAKVA LLAMGKLGSR ELTAGSDVDL
ILLYDHDKDA EESDGEKPLA PSKYYIRLTQ RLIAALSAPT AEGVLYEVDM RLRPSGNKGP
VATHIEAFGK YQRNDAWTWE HMALTRARPI HGDEAFIARI KVDIEDVLAM PRDVRKLAGD
VREMRELIAQ EKPPRDDWDL KLKPGGIIDL EFIAQFATLA GYVKKTPRPF ATEEVLANLD
PFFADPAMVD GLVEAHRFYT NLSQAIRLCL NDSAGLDQFP PGMRELLCRV AGLPDIERIE
YELLEHYRLV RAAFDKLVGH GAD
