ID A0A1T0CQS5_9GAMM Unreviewed; 949 AA.
AC A0A1T0CQS5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=B0680_04520 {ECO:0000313|EMBL:OOS24693.1};
OS Moraxella pluranimalium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=470453 {ECO:0000313|EMBL:OOS24693.1, ECO:0000313|Proteomes:UP000189800};
RN [1] {ECO:0000313|EMBL:OOS24693.1, ECO:0000313|Proteomes:UP000189800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 54913 {ECO:0000313|EMBL:OOS24693.1,
RC ECO:0000313|Proteomes:UP000189800};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Jaen-Luchoro D.,
RA Gonzales-Siles L., Karlsson R., Yazdan S., Boulund F., Johnning A.,
RA Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Moraxella pluranimalium CCUG 54913T type
RT strain.";
RL Submitted (FEB-2017) 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:OOS24693.1}.
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DR EMBL; MUYU01000009; OOS24693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0CQS5; -.
DR STRING; 470453.B0680_04520; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000189800; 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; 1.
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:UP000189800};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:OOS24693.1}.
FT DOMAIN 71..261
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 289..426
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 537..791
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT REGION 1..433
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 433..949
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 949 AA; 108215 MW; 7623956186BAC27D CRC64;
MSSFDFIPNQ EQLDILALAS PFALQIYQKH TERAQAFLGE FGFGTPMARA DFDALVRRFV
GLGTTNYLDS INEDMVMKGL RELRKFLMLK WIWQDALAVI TLEDLTRELS DFADSCIEFS
KDFVYHKLTI RYGDPIIRRK TKQIKDELAI IAMGKLGARE LNLSSDIDLI FVHIDNGDTD
GKKCIDSHKF MRDLGRGVIK LLDENTEHGF VFRVDMRLRP WGDGSPLVLH LQALEKYFNQ
HGRTWERFAW LKARVVNHIS DEFATQLRQI TKNFVHRYYI DYSAFSALRE MKAMIINQQT
QRQDLDNVKL GVGGIRDIEF IVQAFALIYG GHHVRIAEHP ACLECMQVLT ELGYIDAEES
KQLSSAYRFL RRLEHAIQAR HDHQSQRLPS DSDELLAIAK TLGFESVTSF RSVLDAHRQN
VSRPFGRMVT DRQSPKQESL NAKQIGDSLH ETLGDDAMAQ LDEFMNSRLV GSLDDVSKER
LSQAYPIILH ALLTHAQMDG VQSAMTALPR LIALLEAICR RSIYLVMLTE NPDATVRLIP
MLTASPWIAK ELAHYPVLLD TFLQKRYLHL PDKSELTDIL RQSLLRVEPF DDEGYLSAIR
LFKKTQVLAV ATADVLGLRH IMKVSDSLTF IAEVVLESAL YRAFDELTAK HGFPLLQNGE
RAGVDDCGFA IVGYGKLGGL EMSYASDLDL VFLHRIDEKG ETDGEKPISG MKFAARLIQK
LMTYLATQTR DGRAYEIDTR LRPSGNAGVA VISTHAFEMY QDEKAWAWEH QALVRARGLI
GDEKVLTEFD RIRKKVLTAK RDTAQVRSDV IEMRQKMQTH LGTKPATRHG TDGEQFHIKQ
DFGGLVDIEF LAQFMVLSLS HDYPTLAIWP DNVRIFEEMG KAQIWDVYRC ERLTQAYLDL
RKKTHELALS EQKTIVDDEE WHELRRFVRD VWQDVLGDDA VASDGGLGG
//
