(data stored in ACNUC7421 zone)

SWISSPROT: Q145F9_PARXL

ID   Q145F9_PARXL            Unreviewed;       948 AA.
AC   Q145F9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 97.
DE   RecName: Full=Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00802};
DE   AltName: Full=ATP:glutamine synthetase adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE   AltName: Full=ATase {ECO:0000256|HAMAP-Rule:MF_00802};
DE   Includes:
DE     RecName: Full=Glutamine synthetase adenylyl transferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              EC=2.7.7.42 {ECO:0000256|HAMAP-Rule:MF_00802};
DE     AltName: Full=Adenylyl transferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AT {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AT-C {ECO:0000256|HAMAP-Rule:MF_00802};
DE   Includes:
DE     RecName: Full=Glutamine synthetase adenylyl-L-tyrosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              EC=2.7.7.89 {ECO:0000256|HAMAP-Rule:MF_00802};
DE     AltName: Full=Adenylyl removase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AR {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AT-N {ECO:0000256|HAMAP-Rule:MF_00802};
GN   Name=glnE {ECO:0000256|HAMAP-Rule:MF_00802};
GN   ORFNames=Bxe_A3969 {ECO:0000313|EMBL:ABE29030.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29030.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29030.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29030.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Involved in the regulation of glutamine synthetase GlnA,
CC       a key enzyme in the process to assimilate ammonia. When cellular
CC       nitrogen levels are high, the C-terminal adenylyl transferase (AT)
CC       inactivates GlnA by covalent transfer of an adenylyl group from
CC       ATP to specific tyrosine residue of GlnA, thus reducing its
CC       activity. Conversely, when nitrogen levels are low, the N-terminal
CC       adenylyl removase (AR) activates GlnA by removing the adenylyl
CC       group by phosphorolysis, increasing its activity. The regulatory
CC       region of GlnE binds the signal transduction protein PII (GlnB)
CC       which indicates the nitrogen status of the cell.
CC       {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000256|SAAS:SAAS00959950}.
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-
CC         COMP:10661, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.42;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00802,
CC         ECO:0000256|SAAS:SAAS01118276};
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-
CC         COMP:10661, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:83624, ChEBI:CHEBI:456216; EC=2.7.7.89;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00802,
CC         ECO:0000256|SAAS:SAAS01118275};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00802, ECO:0000256|SAAS:SAAS00959956};
CC   -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000256|HAMAP-
CC       Rule:MF_00802, ECO:0000256|SAAS:SAAS00959957}.
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DR   EMBL; CP000270; ABE29030.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_A3969; -.
DR   EnsemblBacteria; ABE29030; ABE29030; Bxe_A3969.
DR   KEGG; bxe:Bxe_A3969; -.
DR   eggNOG; ENOG4105CE6; Bacteria.
DR   eggNOG; COG1391; LUCA.
DR   HOGENOM; HOG000256491; -.
DR   KO; K00982; -.
DR   OMA; EFMVQYA; -.
DR   Proteomes; UP000001817; Chromosome 1.
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:0016874; F:ligase activity; IEA:UniProtKB-KW.
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   HAMAP; MF_00802; GlnE; 1.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR30621; PTHR30621; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q145F9.
DR   SWISS-2DPAGE; Q145F9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959941};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Ligase {ECO:0000313|EMBL:ABE29030.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959949};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959951};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959952};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959943, ECO:0000313|EMBL:ABE29030.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959945, ECO:0000313|EMBL:ABE29030.1}.
FT   DOMAIN       29    275       GlnE. {ECO:0000259|Pfam:PF03710}.
FT   DOMAIN      301    444       GlnD_UR_UTase. {ECO:0000259|Pfam:
FT                                PF08335}.
FT   DOMAIN      571    809       GlnE. {ECO:0000259|Pfam:PF03710}.
FT   DOMAIN      830    919       GlnD_UR_UTase. {ECO:0000259|Pfam:
FT                                PF08335}.
FT   REGION        1    458       Adenylyl removase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00802}.
FT   REGION      464    948       Adenylyl transferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00802}.
SQ   SEQUENCE   948 AA;  105474 MW;  C26903F4284F4090 CRC64;
     MLLRIEQRLS SNERARPLKT DATLLSSSYS HYAARAAAAR PQLVAQVAAL ASAPLTRERI
     DARFDALCAE AAGASGAPLS EDALKRALRQ LRTEVFCAVM ERDLAGEADV AEVTGAMTDL
     AETTIQRALA VLSAELEVLY GEPRGPHGER LSLGVVGMGK LGGRELNVSS DIDLIFIYEE
     DGETAGGHRS PIATQEFFTR LGKRLIGALA EVTADGYVFR VDMRLRPNGD SGPLVCSLGM
     LEEYFYVQGR EWERYAWIKG RLVSEGTSDA AQRLQKQLDA IVTPFVYRRY LDFGVISAIR
     ALHLQIRQEA QRRASMRPDK ADDIKLGRGG IREIEFSAQV FQLIRGGQDA GFRVRPTLAV
     LRHAATHGLI DTSVCVKLSQ AYRFLRELEH RLQYRNDAQT HAMPVDPEER VALAHAMGCD
     DYAALMAKLD AHREFVEQQF DQIFADKVSG RDGCGAPEDG AAAWVWSSAL ADDSADDVLQ
     ARLVELGVAE PGELLARLRA VWQSSRYAGL AERSRQRFDI VAQRALEAAR TLEPAERRGD
     TVARFFDLLE AVSRRGAYLA LLTEYPQALH HVLSVLGGSR WAAGYLIRHP QLLDELLDDE
     AMDSPFDWPE FKRTLRLRLA AADGVEQQMD LLRHAHQAEV FRILLIDLAG KLSVEHVSDR
     LSELADAVLD VTLEAVWRQL PKRHRDVPRF AVIAYGKLGG KELGYASDLD VIFLYDDTDE
     AAAEVYSTYT RRLITWLTTA TGAGTLFDVD LRLRPNGESG LLVTDLDAFR RYQLREGDAA
     NTAWVWEHQA LSRARYCAGD AGIGAKFEAI REQVLTTPRE AAPLAKEIVE MRERVEAGHP
     NHTALFDLKH DRGGMVDIEF TVQYWVLLHA ASDPELIRNT GNIALLREVS RFGLMSEAEA
     ETVGAAYRTY RKLQHKLRLD GMEKARVEPA LVATEREAVL GLWKRVFG
//

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