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Database: UniProt
Entry: A0A0W1RTA6_9GAMM
LinkDB: A0A0W1RTA6_9GAMM
Original site: A0A0W1RTA6_9GAMM 
ID   A0A0W1RTA6_9GAMM        Unreviewed;       955 AA.
AC   A0A0W1RTA6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=AUR63_01205 {ECO:0000313|EMBL:KTG16712.1};
OS   Guyparkeria sp. XI15.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Thioalkalibacteraceae; Guyparkeria.
OX   NCBI_TaxID=1766620 {ECO:0000313|EMBL:KTG16712.1, ECO:0000313|Proteomes:UP000053033};
RN   [1] {ECO:0000313|Proteomes:UP000053033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XI15 {ECO:0000313|Proteomes:UP000053033};
RA   Zhang G., Stingl U., Rashid M.;
RT   "Haloferax marisrubri sp. nov., isolated from the Discovery deep brine-
RT   seawater interface in the Red Sea.";
RL   Submitted (DEC-2015) 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:KTG16712.1}.
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DR   EMBL; LOPX01000014; KTG16712.1; -; Genomic_DNA.
DR   RefSeq; WP_058574934.1; NZ_LOPX01000014.1.
DR   AlphaFoldDB; A0A0W1RTA6; -.
DR   STRING; 1766620.AUR63_01205; -.
DR   Proteomes; UP000053033; 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; 1.20.120.330; 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:UP000053033};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802}.
FT   DOMAIN          29..273
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          300..437
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          552..805
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          828..914
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   REGION          1..442
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT   REGION          454..955
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   955 AA;  108025 MW;  5287075A41B5E97A CRC64;
     MSDLDEITPD AELIDRLAAN ATGGDVDQEQ LRYVLRCSPF IQQSLAAEPA ILDYVLSGCD
     DGFLGDGIEK RFSGLSGSRE ERLALDATDF GRELRRLRRR EMILIAWRDL LGIDDTDATL
     RSLSRLADFC VAEALVYHEH HLQRRFGQPR DPEGNPVGLV VVGMGKLGGD ELNYSSDIDL
     IFAYASEGET DGRKTLSNAE YFIRLGQRLI RSLDEVTGHG FVFRVDMRLR PNGDEGPLAM
     SFDGLEIYYA TQGREWERYA WIKARVIAGD FTAGDELMNM LRPFVFRRYL DFGAFSQLRE
     MKRLIEREMT DAAMHNNIKL GPGGIREIEF IGQLFQLLRG GREPELQGRR LIPVLRILAE
     MGELEAHTVA DLSEGYDFLR RAENRLQMLY DHQTQTLPDN KFDQLRLAIA MEFDDWGSFL
     WALDQHRERI HGHFSQVLRL PDEGDDDEDP LERVWNGLGD KADRVAILER HDFEEPATLE
     RHLSAWRDTQ GPAINGTVAQ RLDQLMPDLL RDISEYRDQV AVLARMLDLL AAILRRSVYV
     ALLIEQPQAR RQLVRLVHGS PWIAELLTQH PILLDELIDP ETLYAPPDKA QLAHELNELL
     AKCPDDEERS LDELRRFKQL ATLRVAAADV VGALPVMRVS DQLTWIAEVI LEAVYERTRA
     QVERRHGQPQ ALDASGNPFT PGLAIIGYGK LGGIELGYGS DLDLVFLHDS TDREAVTNGE
     KSVDNSLFFA RLAQKIIHTL SIRTPAGVLY EVDTRLRPDG VGGLLVSSVN AFAQYQSENA
     WVWEIQAMCR ARFVAGTERV GESFAAIRRD ALTQQRDTDQ LREAVVGMRR KMRDNQTRTP
     TGFFHLKRDI GGITDIEFLV QYLLLRHAHE SPGILAFTDN IRQLESLDEA GLIDTEAAEA
     LTQAYRNLRD AGHHQALMGC RSVVDAQDFE EEREVVIQQW QALMGCLPPG ADTDD
//
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