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Database: UniProt
Entry: X7E3G3_9GAMM
LinkDB: X7E3G3_9GAMM
Original site: X7E3G3_9GAMM 
ID   X7E3G3_9GAMM            Unreviewed;       976 AA.
AC   X7E3G3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
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-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};
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};
GN   Name=glnE {ECO:0000256|HAMAP-Rule:MF_00802};
GN   ORFNames=MUS1_13580 {ECO:0000313|EMBL:ETX10609.1};
OS   Marinomonas ushuaiensis DSM 15871.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=1122207 {ECO:0000313|EMBL:ETX10609.1, ECO:0000313|Proteomes:UP000054058};
RN   [1] {ECO:0000313|EMBL:ETX10609.1, ECO:0000313|Proteomes:UP000054058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15871 {ECO:0000313|EMBL:ETX10609.1,
RC   ECO:0000313|Proteomes:UP000054058};
RA   Lai Q., Shao Z.S.;
RT   "Marinomonas ushuaiensis DSM 15871 Genome Sequencing.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|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-COMP:10661,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:83624; EC=2.7.7.42; Evidence={ECO:0000256|HAMAP-
CC         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:0000256|HAMAP-
CC         Rule:MF_00802};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00802};
CC   -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000256|HAMAP-
CC       Rule:MF_00802}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETX10609.1}.
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DR   EMBL; JAMB01000007; ETX10609.1; -; Genomic_DNA.
DR   RefSeq; WP_036161573.1; NZ_JAMB01000007.1.
DR   AlphaFoldDB; X7E3G3; -.
DR   STRING; 1122207.MUS1_13580; -.
DR   PATRIC; fig|1122207.3.peg.1857; -.
DR   eggNOG; COG1391; Bacteria.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000054058; Unassembled WGS sequence.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047388; F:[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase activity; 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   CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR   Gene3D; 1.20.120.1510; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 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:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME; 1.
DR   PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00802}; Ligase {ECO:0000313|EMBL:ETX10609.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00802};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00802};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00802};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00802}; Reference proteome {ECO:0000313|Proteomes:UP000054058};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:ETX10609.1}.
FT   DOMAIN          50..295
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          324..461
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          579..832
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          854..947
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   REGION          1..467
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT   REGION          473..976
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   976 AA;  111766 MW;  948B39486311B25C CRC64;
     MTPSNLNPSY ASFCEQSSSR SLLLEQIQEA RERHALVELS CEQIEILEPL WILSDYLHQQ
     LVRFPRWLDD LLILENLPEK PSQEALIAGE GFFSNDAKDC SPEASLVFDE AAFIKRLRLY
     RQWWMVRLIA LDIQHRLSLA ELTSRLSGLA DACVNASLRW SEQHYLNLYG QALDSQGVPQ
     SMIVIGMGKL GGNELNLSSD IDLIFAFREH GDTQGGKKSL SHQEYFTKLG QKLIQHLDQV
     TADGFVFRVD MRLRPFGQSG ALVLNMDSLE NYYQDQGRDW ERYAMIKARV MSGSEVDIRE
     FEALRKPFVY RKYLDFGAIG ALRDLKQMIA KEVRRKGIEH NIKLGEGGIR EVEFIAQALQ
     ILHGGRDQSL QTPALLKVLP YLAQQDYLSF TEVEELRDAY LLLRRTEHAL QAVNDEQTQL
     LPEDDRARQR IALIVGFASW DELNSRLWEV RKNVHRHFIS LIDDGEESSE EVKNQEAWRL
     LIKNPEDESA IIDAIESIKW QDQEAAVKRI TQLLGSRTVV FMQPIGHERL AVFLAAFMPK
     LNDEKSPDLV LERVFPILEA VLRRTAYLVL LCENQTAMTH LIRLCRESVW FTEAISTTPA
     LLDELLDAST LFCPPDKAML TEELKQILLR LPEDDEEAQM DAMRQFRRSI ILRIAACDIT
     EILPIMKVSD HLTWLAEVLL DQVLQQSWFY LTKKHGFPVS QGEVAYTPQL AIIGYGKSGG
     WELGYDSDLD LVFIHGAQST GYTDGGRSID NLTFYTRLGQ RLIHMITSFT AAGRLYEVDM
     RLRPSGNSGL LVSTLDAFRD YQQKEAWVWE HQALTRARGL AGEPTLLAQF EACRKDIISS
     VRDHDQLKAD VIKMREKMRA HLDTGGKEKG FDLKQGAGGI IDIEFMVQYL VLAWSHKYPE
     LMRFSDNVRQ LEAAALVELL DKEKAEKMIE TYTLYRARAH RLNLQQQGRV IQDDAFINNQ
     SLMSQYWASF VNSDNI
//
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