GLNE_STRCO
ID GLNE_STRCO Reviewed; 999 AA.
AC Q8CK02; O86858;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=SCO2234;
GN ORFNames=SC10B7.29c, SCBAC17D6.01c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-784, AND FUNCTION.
RC STRAIN=A3;
RX PubMed=10517584; DOI=10.1099/00221287-145-9-2313;
RA Fink D., Falke D., Wohlleben W., Engels A.;
RT "Nitrogen metabolism in Streptomyces coelicolor A3(2): modification of
RT glutamine synthetase I by an adenylyltransferase.";
RL Microbiology 145:2313-2322(1999).
CC -!- FUNCTION: Adenylation and deadenylation of glutamate--ammonia ligase.
CC {ECO:0000269|PubMed:10517584}.
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; AL939111; CAD55299.1; -; Genomic_DNA.
DR EMBL; Y17736; CAA76840.2; -; Genomic_DNA.
DR PIR; T51759; T51759.
DR RefSeq; NP_733564.1; NC_003888.3.
DR RefSeq; WP_011028215.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q8CK02; -.
DR SMR; Q8CK02; -.
DR STRING; 100226.SCO2234; -.
DR GeneID; 1097667; -.
DR KEGG; sco:SCO2234; -.
DR PATRIC; fig|100226.15.peg.2271; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_1_0_11; -.
DR InParanoid; Q8CK02; -.
DR OMA; EFMVQYA; -.
DR PhylomeDB; Q8CK02; -.
DR BRENDA; 2.7.7.42; 5998.
DR BRENDA; 2.7.7.89; 5998.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..999
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209280"
FT REGION 1..483
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 489..999
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT CONFLICT 158..163
FT /note="CGTIDV -> RHHRL (in Ref. 2; CAA76840)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="R -> AA (in Ref. 2; CAA76840)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="L -> P (in Ref. 2; CAA76840)"
FT /evidence="ECO:0000305"
FT CONFLICT 782
FT /note="D -> N (in Ref. 2; CAA76840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 999 AA; 108777 MW; 33E2BDCDD791FAC9 CRC64;
MTPGRRSSTF TRLLRHGFTD PSAAERLLDG AGLAELRADP VLLEALGATA DPDLALHGLV
RLLEAQPDAT ARQELLDTLI AAKPLRDRLL GVLGASEALA DHLARHAGDW QTLVTYEPRD
LHRGVEEFER GLAEATDPVT LRVAYRRCLL SIAARDVCGT IDVAETAAEL ADLAIATLRA
ALALAEAAAP EDAARCRLAV IAMGKCGGHE LNYVSDVDVI FVGEAADTGP DADEAKAMRA
ATSLAAHMMR ICSETTVEGS IWPVDANLRP EGRNGPLVRT LSSHVAYYQR WAKTWEFQAL
LKARPVAGDP GLGAEYVAAL QPLVWQAADR ENFVPDVQKM RRRVVENIPL TEVDRQLKLG
PGGLRDVEFA VQLLQLVHGR ADTSLHSGTT LDALEALAAG GYVGRTDAAQ LDEAYRFLRS
MEHRIQLHRL RRTHLVPEDE ADLRRLGRSL GLRTDPVTGL LRAWKRHASV VRRLHEKLFY
RPLLDAVAQL APGEARLSPE AARERLVALG YADPAAALRH LEALASGVTR KAAIQRTLLP
VLLGWFADSA DPDTGLLNFR KVSDALGTTP WYLRLLRDEG AAAENLARVL SAGRLAPDLL
MRAPEAVALL GDGVAGGLRP RDRAQLEQET LAAVRRADDA VQAVTAVRGV RRRELFRTAA
ADIVGSYGTE TQPVEADQGA LVDLVGGAVS DLTSATLAGT LRAVVREKWG DVLPTRFAII
GMGRFGGHEL GYGSDADVLF VHEPRDGVAE REAGDAANKV VSEMRRLLQV PSADPPLLID
ADLRPEGRSG PLVRTLKSYE AYYRRWSLGW ESHALLRAEF VAGDEELGRR FIELIDPLRY
PEGGLGEDAV REIRRLKARM ESERLPRGAD PKLHAKLGPG GLSDVEWTVQ LLQLRHGHEI
AGLRTTRTRT ALAAARDAGL ISEEHTATLD EAWVLATRVR NAVMLVRGRA GDTFPTDPRE
LAAVGRYLGH GSGHAGDMLD EYRRTARRAR TVVEDLFYA
