GenomeNet

Database: UniProt
Entry: Q8UGQ4
LinkDB: Q8UGQ4
Original site: Q8UGQ4 
ID   GLNE_AGRFC              Reviewed;         988 AA.
AC   Q8UGQ4; Q7D079;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   05-DEC-2018, entry version 81.
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};
GN   OrderedLocusNames=Atu0981; ORFNames=AGR_C_1798;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium
OS   tumefaciens (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P.,
RA   Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L.,
RA   Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr.,
RA   Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C.,
RA   Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A.,
RA   Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D.,
RA   Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M.,
RA   Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M.,
RA   Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V.,
RA   Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M.,
RA   Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L.,
RA   Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F.,
RA   Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B.,
RA   Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G.,
RA   Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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: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-
CC         COMP:10661, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:83624, ChEBI:CHEBI:456216; EC=2.7.7.89;
CC         Evidence={ECO:0000255|HAMAP-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-
CC         COMP:10661, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.42;
CC         Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; AE007869; AAK86790.2; -; Genomic_DNA.
DR   PIR; AE2697; AE2697.
DR   PIR; E97479; E97479.
DR   RefSeq; NP_354005.2; NC_003062.2.
DR   RefSeq; WP_010971304.1; NC_003062.2.
DR   ProteinModelPortal; Q8UGQ4; -.
DR   SMR; Q8UGQ4; -.
DR   STRING; 176299.Atu0981; -.
DR   EnsemblBacteria; AAK86790; AAK86790; Atu0981.
DR   GeneID; 1133019; -.
DR   KEGG; atu:Atu0981; -.
DR   PATRIC; fig|176299.10.peg.993; -.
DR   eggNOG; ENOG4105CE6; Bacteria.
DR   eggNOG; COG1391; LUCA.
DR   HOGENOM; HOG000256492; -.
DR   KO; K00982; -.
DR   OMA; EFMVQYA; -.
DR   BioCyc; AGRO:ATU0981-MONOMER; -.
DR   Proteomes; UP000000813; Chromosome circular.
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   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; 1.
DR   Pfam; PF03710; GlnE; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Magnesium; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN         1    988       Bifunctional glutamine synthetase
FT                                adenylyltransferase/adenylyl-removing
FT                                enzyme.
FT                                /FTId=PRO_0000209226.
FT   REGION        1    472       Adenylyl removase. {ECO:0000255|HAMAP-
FT                                Rule:MF_00802}.
FT   REGION      476    988       Adenylyl transferase. {ECO:0000255|HAMAP-
FT                                Rule:MF_00802}.
SQ   SEQUENCE   988 AA;  109210 MW;  AB2EFD19B9BA64F1 CRC64;
     MTKRETVERR LSEVPPGVIR PYTQTELKSV FSTLKDIGKA EPAVAALLAG ESPLKDFIAA
     AFTLSPYLRD MAAADEGLLT LAISKPLEPL LTDLVRDARD CWKPAEDAVP VENEVMSRLR
     IAKRRLSFVA ALADLARIFT ARDTTRWLSE MADASLSAAI DHLLLSAHES GKLKLKNLAA
     PSEGSGLIVL GMGKLGAREL NYSSDIDAVV FFEPSAGIID DPYDATENFG RMMRRLVRIM
     QERTADGYVF RTDLRLRPDP GSTPLAIPVE AALLYYEGRG QNWERAAYIK ARPVAGDIKA
     GENFLRELTP FIFRKYLDYA AIADIHSIKR QIHAHKGHGA IAVKGHNVKL GRGGIREIEF
     FAQTQQLIAG GRMPPLRVRA TEDALAALTE AKWIDAETRD SLTEAYWFLR EVEHRIQMVR
     DEQTHVLPDT EAELKRIAFM LGFEDTKAFS EKLEEVLRLV ERRYSALFEQ ETKLSGEAGN
     LVFTGQKDDP DTLKTLSTLG FQRPEDISRV IRTWHNGRYR ATQSVEARER LTELTPDLLR
     AFGESKRADE ALLRFDNFLS GLPAGIQLFS LLGNNPALLS LLVTIMSSAP RLAEIIAARP
     HVFDGMLDPA LMSDVPTRDY LAHRMGNFLS NARHYEDILD RLRIFAAEQR FLIGVRLLTG
     AIRGEVAARA FTHLADLVIE AALNAVLSEM EAAHGPYPGG RVAVMGMGKL GSFELTAGSD
     VDLILLYDYD DTAQESTGAK PLDVVRYFTR VTQRLIAALS APTAEGVLYE VDMRLRPSGN
     KGPVATRISA FEKYQREEAW TWEHMALSRA RLICGDASLM EDARSIIASI LSQKRDVAKV
     STDVLDMRSL IEQEKPPENN WDFKLINGGL IDLEFIAQYL ALIGPVKGLG AHEPGRNTAE
     ALQALAAPVM ESQAFDDCMA AMGLYTEISQ IVRLCIDGAF NPKEAPAGLI DLVCRAGDCP
     DIPTLEGEVK RLSKAVRKAF VAVVKNGG
//
DBGET integrated database retrieval system