(data stored in SCRATCH zone)

SWISSPROT: Q3KJ48_PSEPF

ID   Q3KJ48_PSEPF            Unreviewed;       979 AA.
AC   Q3KJ48;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 114.
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   OrderedLocusNames=Pfl01_0464 {ECO:0000313|EMBL:ABA72208.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72208.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72208.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72208.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA72208.1; -; Genomic_DNA.
DR   RefSeq; WP_011332130.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0464; -.
DR   EnsemblBacteria; ABA72208; ABA72208; Pfl01_0464.
DR   KEGG; pfo:Pfl01_0464; -.
DR   eggNOG; ENOG4105CE6; Bacteria.
DR   eggNOG; COG1391; LUCA.
DR   HOGENOM; HOG000256491; -.
DR   KO; K00982; -.
DR   OMA; EFMVQYA; -.
DR   BioCyc; PFLU205922:G1G4S-469-MONOMER; -.
DR   Proteomes; UP000002704; 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: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; Q3KJ48.
DR   SWISS-2DPAGE; Q3KJ48.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959941};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Ligase {ECO:0000313|EMBL:ABA72208.1};
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:ABA72208.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00959945, ECO:0000313|EMBL:ABA72208.1}.
FT   DOMAIN       46    294       GlnE. {ECO:0000259|Pfam:PF03710}.
FT   DOMAIN      315    454       GlnD_UR_UTase. {ECO:0000259|Pfam:
FT                                PF08335}.
FT   DOMAIN      574    827       GlnE. {ECO:0000259|Pfam:PF03710}.
FT   DOMAIN      849    947       GlnD_UR_UTase. {ECO:0000259|Pfam:
FT                                PF08335}.
FT   REGION        1    458       Adenylyl removase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00802}.
FT   REGION      469    979       Adenylyl transferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00802}.
SQ   SEQUENCE   979 AA;  109998 MW;  C9D69409281525B9 CRC64;
     MTLPALAELP AILLPLVSRS EQSFRAAVAQ LEDDHGFSSW TPERWAQFAR VSAASDFVIE
     QGVRDPFMLL SLVQSGELDR PFARGELCGQ IAEAVSTAQT EDELGRVLRR QRTRHQVRII
     WRDLNRQADL VQTCRDLSDM ADASIDQAYQ WLYRRHCEQF GTPTGRRSGE PQQMVILGMG
     KLGAVELNLS SDIDLIFAYP EGGETVGVKR PLDNQEFFIR LGQRLIKALD PITVDGFVFR
     VDMRLRPYGS SGALVLSFNA LEQYYQDQGR DWERYAMIKS RVVAGDQVAG EQLQEMLRPF
     VYRRYLDFSA IEALRTMKQL IQQEVRRKGM ADNIKLGSGG IREVEFIAQA FQLIHGGRDL
     SLQQRPLLKV LSTLEGQGYL PPAVISELRE GYEFLRYTEH AIQAIADRQT QMLPDSAQDQ
     ARIAFMLGFS DWDAFHEKLM FWRGRVAWHF AQVIADPDED EGVESEVVVG GEWLPLWEEA
     QDEEAACRQL EEGGFADATK ALKALASLRA SPQLRAMQRL GRERLDAFIP RLLAQAVEHE
     NPDLVLERVL PLVEAVARRS AYLVLLTENP GALRRLLTLC AASPWIAEQI TRFPLLLDEL
     LNEGRLFKPP LAPELAAELR ERLTRIPEDD LEQQMEALRH FKLAHRLRVA ASEIAGSLPL
     MKVSDYLTWL AEAILEQVLA LAWRQTVAKY GTPLRTDGTL CDPGFIIVGY GKVGGIELGH
     GSDLDLVFIH DGDQQAETDG PKPIDGTQFF TRLGQRIIHL LTAQTNSGQL YEVDMRLRPS
     GASGLLVSSL GAFARYQENE AWTWEHQALV RARVLVGSKD VGQAFENVRA QVLGKARDLA
     KLQQEVSEMR AKMRDNLGSK STAAGTGANA FEATAPFDLK QDAGGIVDIE FMVQYAALAW
     SQTHPALLRW TDNIRILEEL EHEGLMPAED ASLLREAYKA YRSAAHRQAL QKDAGVIPGD
     QFADERRQVM RIWRELGLS
//

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