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Database: UniProt
Entry: G2DW14_9GAMM
LinkDB: G2DW14_9GAMM
Original site: G2DW14_9GAMM 
ID   G2DW14_9GAMM            Unreviewed;       959 AA.
AC   G2DW14;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, 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-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=ThidrDRAFT_0075 {ECO:0000313|EMBL:EGV33920.1};
OS   Thiorhodococcus drewsii AZ1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiorhodococcus.
OX   NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV33920.1, ECO:0000313|Proteomes:UP000004200};
RN   [1] {ECO:0000313|EMBL:EGV33920.1, ECO:0000313|Proteomes:UP000004200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ1 {ECO:0000313|EMBL:EGV33920.1,
RC   ECO:0000313|Proteomes:UP000004200};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA   Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT   "The draft genome of Thiorhodococcus drewsii AZ1.";
RL   Submitted (JUN-2011) 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:EGV33920.1}.
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DR   EMBL; AFWT01000001; EGV33920.1; -; Genomic_DNA.
DR   RefSeq; WP_007038791.1; NZ_AFWT01000001.1.
DR   AlphaFoldDB; G2DW14; -.
DR   STRING; 765913.ThidrDRAFT_0075; -.
DR   PATRIC; fig|765913.3.peg.77; -.
DR   eggNOG; COG1391; Bacteria.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000004200; 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:EGV33920.1};
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|HAMAP-Rule:MF_00802,
KW   ECO:0000313|EMBL:EGV33920.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:EGV33920.1}.
FT   DOMAIN          43..280
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          308..446
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          561..813
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          834..921
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   REGION          1..450
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT   REGION          456..959
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   959 AA;  107939 MW;  51710639DEC11D96 CRC64;
     MSSNETNPVD PMMESHWRDW LAWADENGVM VSADGDFARI RERVWDASEY VAVSVQRHPD
     EFAELIASGD LARSYGAGDL DARLAAALAE VEGEPALHKA LRLFRRREMV RIIWRDIGQL
     APLAETLEDL SELADVCIRR TLDLLHDWTC AELGTPRDPE GRALRMVVLG MGKLGARELN
     LSSDIDLIFA FAHGGEVEGG PRVLSNEQFF VRLGQRLVQA LATKTIDGFV FRVDTRLRPF
     GEVGPLAMSF QAMEDYYQSQ AREWERYAMI KARPVAGDPD DVDALMGMLR PFVYRRYLDF
     GAFESLRDLK QMIVKELNRR GMEGNIKLGP GGIREIEFIG QAFQLVRGGR DPDLQVRPIL
     QVLALLAERE LMPAEAVVEL DTAYGFLRLV ENRLQAHRDK QTHTLPEDDQ GRARLARSMG
     FSDWAAFAVV LEEHRRVVQG HFDHVFAAPV QEPDRGGSAW VALWNGDQDE MRELSILEDA
     GFVDPAAART RIEHFRDGTA RKGLSSRGRD RLAQLMPQVL RIVAGCDLPD AALGRVLLVL
     EAVARRTAYL AMMIEHPSIL SQLARLASMS PWFTDKIQHH PLLLDELIDP RRLYAPLRRD
     ELESELDALL AHVDSEDLEQ QMERLHQFAQ GNMLRVAAAD LTEVIPLMVV SDYLTEIAEV
     AVGRVLEQAY AHLSVRHGHP TSILGETTGF LVLGYGKLGG IELGYGSDLD LVFLHGTESI
     NAMTDGQKEI SNEQFYARLG QRMIHMMTTQ TASGALYEVD MRLRPDGAKG MLVRSIGSFA
     AYQESEAWTW EHQALIRARP VAGDPALMRR FAEVRRAILC RERDPERLRI EVRDMRAKMR
     ANLDKTRDGR FDLKQGAGGI ADIEFMVQYA VLRWAAAYPA LVDWTDNIRL LETLAQLDLL
     PGQSAEDLAE AYKALRAAYH RGALQEQPKT IPVDQLLAER ERVRTLWHDL MEDGSVLDA
//
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