ID A0A0F7LZ26_9GAMM Unreviewed; 974 AA.
AC A0A0F7LZ26;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=IMCC21906_00278 {ECO:0000313|EMBL:AKH67971.1};
OS Spongiibacter sp. IMCC21906.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Spongiibacter.
OX NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH67971.1, ECO:0000313|Proteomes:UP000035013};
RN [1] {ECO:0000313|EMBL:AKH67971.1, ECO:0000313|Proteomes:UP000035013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH67971.1,
RC ECO:0000313|Proteomes:UP000035013};
RA Cho J.-C., Yang S.-J., Kang I.;
RT "Complete genome sequence of IMCC21906 belonging to the
RT Gammaproteobacteria.";
RL Submitted (MAY-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}.
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DR EMBL; CP011477; AKH67971.1; -; Genomic_DNA.
DR RefSeq; WP_047010667.1; NZ_CP011477.1.
DR AlphaFoldDB; A0A0F7LZ26; -.
DR STRING; 1620392.IMCC21906_00278; -.
DR KEGG; spoi:IMCC21906_00278; -.
DR PATRIC; fig|1620392.3.peg.314; -.
DR Proteomes; UP000035013; Chromosome.
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:UP000035013};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:AKH67971.1}.
FT DOMAIN 56..299
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 323..462
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 579..828
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 852..947
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..466
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 477..974
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 974 AA; 110002 MW; 19418DBEB46F69E3 CRC64;
MKKQQSAPES LNISDTELPA SLHGEVDNRW LTLMERSEPS QQQWYREFAQ SSRRGELLRA
FSCSPALMDY CVRQPDLLPM LVESGELDQR LDHTFWGESL ARYCASAASA EEFASLLRAF
RNRHWVRVVW RDLNRLAELE ETVADLSHLA DACVQVATDY HHDELVKDWG QPLSRDGEPQ
RLLVIAMGKL GAGELNLSSD IDLIFTYPKA GQTSGGKRSG DNQEFFIRLG QRLIKALDAP
TPDGFVFRVD MRLRPYGQSG PLVVSADALE EYYQDQGRDW ERYALIKARV IAGDAAAGET
LMANLRPFIY RRYLDFSAFE SLRDMKGMIQ REVQRRGLKD NIKLGSGGIR EIEFIAQCFQ
LIRGGQEIEL QARGLQQVLQ HLLTGEFLPA AAVAELRDAY RFLRNTEHAI QAWRDQQTQQ
LPTADDVRAA LAFAMGFTDW TGFVDSLEEH RQRVANHFSQ LISPPEEDDS ASQDELRQWR
SVLDEPEQNE LKVALESADF DDGQEAARLL IALLNGAAVQ RMQPSSKDRL DDFMPLLLEA
LRAAEHPATA LLRIIPLIEA VLRRTAYLVL LMENPGALAR LVQLCDASPW ISRQLAANPV
LLDELLDARS LFHLPKKDGL RSELRQRLLR IDEDDLEAQM EALRYFRLAH VLRVAASEVT
GSLPLMKVSD YLTYIAEVVL EAVLDIAWQN LSEKHGVLSA DDRRHFVVIG YGKLGGIELG
YGSDLDLVFL HDVDSGAVSD GDKPLDSGTY FTRLGQRIIH ILTAHTRMGN LYEVDMRLRP
SGNSGLLVSS FKGFKEYQDN QAWTWEHQAL VRARVTAGDS QLAARFEALR QEVLGRDRNA
QKLRTEVVAM REKMRKHLLP AGDKEKNTGF DLKQSPGGIV DIEFMVQYAV LTWAHQHPPL
AEFTDNIRIL ESLQTEKLIS DADAQALIDA YKAFRSQAHR LSLQEQKGRV AASALPEQRA
AVVRLWHSLM EPSL
//
