(data stored in ACNUC7421 zone)

SWISSPROT: C5BHH0_EDWI9

ID   C5BHH0_EDWI9            Unreviewed;       946 AA.
AC   C5BHH0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 59.
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=NT01EI_0536 {ECO:0000313|EMBL:ACR67769.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67769.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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:SAAS00672577}.
CC   -!- CATALYTIC ACTIVITY: ATP + [glutamine synthetase]-L-tyrosine =
CC       diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-
CC       tyrosine. {ECO:0000256|HAMAP-Rule:MF_00802,
CC       ECO:0000256|SAAS:SAAS00633976}.
CC   -!- CATALYTIC ACTIVITY: [Glutamine synthetase]-O(4)-(5'-adenylyl)-L-
CC       tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP.
CC       {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000256|SAAS:SAAS00672575}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00802, ECO:0000256|SAAS:SAAS00344958};
CC   -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000256|HAMAP-
CC       Rule:MF_00802, ECO:0000256|SAAS:SAAS00540787}.
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DR   EMBL; CP001600; ACR67769.1; -; Genomic_DNA.
DR   RefSeq; WP_015869969.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0536; -.
DR   EnsemblBacteria; ACR67769; ACR67769; NT01EI_0536.
DR   GeneID; 7961561; -.
DR   KEGG; eic:NT01EI_0536; -.
DR   PATRIC; fig|634503.3.peg.486; -.
DR   eggNOG; ENOG4105CE6; Bacteria.
DR   eggNOG; COG1391; LUCA.
DR   HOGENOM; HOG000256491; -.
DR   KO; K00982; -.
DR   OMA; FTVQLLQ; -.
DR   OrthoDB; POG091H0675; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   HAMAP; MF_00802; GlnE; 1.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
PE   3: Inferred from homology;
DR   PRODOM; C5BHH0.
DR   SWISS-2DPAGE; C5BHH0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00015009};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Ligase {ECO:0000313|EMBL:ACR67769.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00423276};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00672573};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00015007};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00015011, ECO:0000313|EMBL:ACR67769.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802,
KW   ECO:0000256|SAAS:SAAS00015008, ECO:0000313|EMBL:ACR67769.1}.
FT   DOMAIN       32    268       GlnE. {ECO:0000259|Pfam:PF03710}.
FT   DOMAIN      294    433       GlnD_UR_UTase. {ECO:0000259|Pfam:
FT                                PF08335}.
FT   DOMAIN      552    803       GlnE. {ECO:0000259|Pfam:PF03710}.
FT   DOMAIN      824    915       GlnD_UR_UTase. {ECO:0000259|Pfam:
FT                                PF08335}.
FT   REGION        1    437       Adenylyl removase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00802}.
FT   REGION      443    946       Adenylyl transferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00802}.
SQ   SEQUENCE   946 AA;  106915 MW;  C5BA7517D569D3DE CRC64;
     MSETRALPTL LHSQGARQAA RLQGATSAAL PTLALSDFVA DSLAAYPAWW QQLQQMPPQV
     QEWQQYAGWL AERLAPAQDE ATLMQALRLF RRHMLTRIAW MQASAQADCQ QTLLQLSALA
     ETLVIGARDW LYHRCCQEWG VPCNAAGEAQ PLLILGMGKL GGGELNFSSD IDLIFVYPQA
     GATRGGRREL DNAQFFTRLG QRLIKALDQP TEDGFVYRVD MRLRPFGDSG PLVLSFSALE
     DYYQEQGRDW ERYAMVKARL LGEGQDRHGQ ELYRLLRPFV FRRYIDFSVI QSLRNMKGMI
     AREVRRRGLK ENIKLGAGGI REIEFITQVF QLIRGGRERS LQQRALLPAL AAIGELGLLT
     SAQVAALRCA YLFLRRLENL LQAIDDQQTQ TLPSDDLNRA RLAYGMGLTD WAALSRALQA
     HMVAVRAIFN ALIGDDDQDE DEGSDDAALR FAPLWQERLD ESELAALMPQ LDPAQRLRLQ
     QTLDAFRCDV DKRTIGPRGR EVLARLMPAL LAQVCVRDDA LVLQQRLMPL LLNIVTRTTY
     LELLMEFPAA LHQLIRLCAA SPMLAEQLAR YPLLLDELLD PVTLYRPVDQ GSYRDELRQY
     LLRIPDDEEQ RLEALRQFKH AQQLRIAASD IAGALPVMKV SDHLTYLAEA VIDAVVQQAW
     EQMVARYGQP THLADHGQRG FAVIGYGKLG GWELGYGSDL DLVFLLECPM EVMTDGPRCI
     DGRQFYLRLA QRIMHLFSAR TASGILYEVD ARLRPSGAAG MLVSTLTAFG DYQRSEAWTW
     EHQALVRARP VYGDAQMHRR FDAIRREILC RGRDAATLRC EVAEMREKMR THLGSRDAAQ
     FDIKADRGGI VDIEFIAQYL VLRYGAEQPG LTRWSDNVRI FELMAQYAVM PQEEADALTH
     AYVTLRNTLH HLALQAQPGV VESARFADER AQVCDSWQRW LGGAAR
//

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