ID A0A3A3FKF7_9BURK Unreviewed; 915 AA.
AC A0A3A3FKF7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=D3871_15930 {ECO:0000313|EMBL:RJF94965.1};
OS Noviherbaspirillum saxi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=2320863 {ECO:0000313|EMBL:RJF94965.1, ECO:0000313|Proteomes:UP000265955};
RN [1] {ECO:0000313|Proteomes:UP000265955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1R23-30 {ECO:0000313|Proteomes:UP000265955};
RA Zhu H.;
RL Submitted (SEP-2018) 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:RJF94965.1}.
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DR EMBL; QYUO01000002; RJF94965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A3FKF7; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000265955; 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:RJF94965.1};
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:UP000265955};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:RJF94965.1}.
FT DOMAIN 35..246
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 270..414
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 535..769
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 790..884
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..423
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 433..915
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 915 AA; 101714 MW; 9DB9F724DF98EBCA CRC64;
MTPSLLTSDL ASRFYSRWLN ADSARTDMVT ELAELSITPE VFARLLQKET AAGMPLPRAM
RRVRNLVVAA LIDRDLGGQA ELSEVLAAIS AFADFAVQTH LAAITADLME LHGTPVGAES
GLPQEMIVIG MGKLGGNELN VSSDIDLIFV YPENGETRVT SPEQRQLSNH EFFIRVGKKL
IGALSELTED GFTFRVDMAL RPNGASGPLA ASLAMVEEYL LVQGREWERY AWVKARALTG
HPDDIAALEQ IVRPFVYRRY LDFGAIDALR NMHAQIRAEV KRQEIRHPER ANNVKLGRGG
IREIEFLAQV FQLIRGGRDP SLQDRSTRVT LDTLASKNLL SVEEVAQLQQ AYAFLRNIEH
RLQYLDDAQT HTFPSGPDDQ LRVARMMGFD DVTSLLAALD GHRAIVAAQF DAIFADKSSG
QPATPEEEHP RIVHSGFSDA ENREVVEARL NALGFDDVSS ASARLLATAQ SPRMHSLPDT
SRTRLMALIN AALPLIAATS ATHAATLGRL LDFLEAIARR AAYLALLTEF PHTLGRVIRM
MGASDWAAKY LTRHPILLDE LLDDRTLQST PDWPAFADEV TRQLDAIDGD TEQQMNVLRD
LHHAQLFRLL AQDLEGALTV ERLADHLSAL ADILVGATVR AVWKNIHNRH REVPRFAVIA
YGKLGGKELG YASDLDVIFL FDDDNHEAPA LYARLAQRFI TWMTTHTPAG ILFDIDIALR
PDGASGLLVS RVPAFEKYQA ENAWLWEHQA LTRARFCAGD AEIGARFEAI REQVLRQQRD
EEALRREVAA MRTKMHEAHP NRSQQFDLKH DAGGMIDIEF IVQFLVLSHA CTYPQLTADI
GNIALLKLCG ELGLIDAGLA GDVADAYRAF RKLQHQIRLQ GSERARVEVE KVEVQAARVR
QLWGMTLGRS RGAED
//
