ID A0A1J7CZI3_9GAMM Unreviewed; 937 AA.
AC A0A1J7CZI3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BK025_08285 {ECO:0000313|EMBL:OIV46888.1};
OS Sodalis sp. TME1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1912097 {ECO:0000313|EMBL:OIV46888.1, ECO:0000313|Proteomes:UP000181913};
RN [1] {ECO:0000313|EMBL:OIV46888.1, ECO:0000313|Proteomes:UP000181913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TME1 {ECO:0000313|EMBL:OIV46888.1,
RC ECO:0000313|Proteomes:UP000181913};
RA Rosas-Perez T., Vera-Ponce De Leon A., Rosenblueth M., Ramirez-Puebla S.T.,
RA Rincon-Rosales R., Martinez-Romero J., Dunn M.F., Martinez-Romero E.;
RT "The Symbiome of Llaveia Cochineals (Hemiptera: Coccoidea: Monophlebidae)
RT Includes a Gammaproteobacterial Co-symbiont Sodalis TME1 and the Known
RT Candidatus Walczuchella monophlebidarum.";
RL Submitted (OCT-2016) 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:OIV46888.1}.
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DR EMBL; MNBX01000268; OIV46888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7CZI3; -.
DR Proteomes; UP000181913; 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: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; 1.10.4050.10; Glutamine synthase adenylyltransferase GlnE; 1.
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};
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:UP000181913};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:OIV46888.1}.
FT DOMAIN 30..272
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 294..433
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 546..797
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 819..910
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..439
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 447..937
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 937 AA; 104594 MW; 4A06DDA97C902B0B CRC64;
MMTRPLPPIL QRQGQQTAAA LPAPADDAAI SALAMSDFIS DALIGHPAWL QELAAQPPRP
GEWRDYAGLL ASRLAAVDDE TALMRELRLF RRRTLVRIGW AQILGLCDIG ETLTQLSQLA
ETLIIAARDW LWQACCREWG TPCGADGTPQ PLLILGMGKL GGGELNFSSD IDLIFAYPEN
GFTRGGRREL DNAQFFTRLG QRVIKALDQP TVDGFVYRVD MRLRPFGDSG PLVLSFAALE
DYYQEQGRDW ERYAMIKARL MGGDGDRYSQ ELRSMLRPFI FRRYIDFSVI QSLRNMKQMI
AREVRRRGLK DNIKLGAGGI REIEFIAQVF QLIRGGREPR LQARALLPTL AAIGELGLLA
PAQSARLGEA YLYLRRLENL LQGINDQQTQ TLPADALNQA RLAWGMDEAD WPQLTRTLAA
HMQAVRAVFD ELIGDDAPDA EDNDTPGAAA ALWQEPMSQA SEADVAGVPW PRLAQHVADF
RRDVAKRTLG PRGREVLDAL MPRLLTHIGD GDTADVAFER LAPVLLSIVS RTTYLELLLE
YPGALGHLIR LCAASPMIAS QLARHPLLLD ELLDPATLYH PPAPSAYGDE LRQYLLRVPE
EDEEQQLEAL RQFKQAQQLR IAAADIAGVL PVMQVSDHLT YLAEAMIHAV IQQAWKSMVA
RHGRPSHLGA GQDAGFAVIG YGKLGGWELG YSSDLDLVFL HQCPDDAITD GPRVIDGRQF
YLRLAQRVMH LFSTRTPAGV LYEVDARLRP SGAAGMLVST LAAFEDYQLN EAWTWEHQAL
VRARMVYGTS ALQEGFNAIR RRVLCRGRDP ATLRREVSEM RAKMRQHLAS KQSDVFDIKT
DEGGITDIEF LAQYLVLRHA AEKPELTRWS DNVRIFELMA QHGIIDGDDA DGLCASYTTL
RDTLHHLALQ ALPGRVPVAQ FARERALIGR CWRQWLD
//
