ID A0A199AWW2_9ACTN Unreviewed; 1029 AA.
AC A0A199AWW2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=AYO52_12135 {ECO:0000313|EMBL:OAV78651.1};
OS Dietzia sp. 111N12-1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=1785156 {ECO:0000313|EMBL:OAV78651.1, ECO:0000313|Proteomes:UP000092558};
RN [1] {ECO:0000313|EMBL:OAV78651.1, ECO:0000313|Proteomes:UP000092558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=111N12-1 {ECO:0000313|EMBL:OAV78651.1,
RC ECO:0000313|Proteomes:UP000092558};
RA Yu M.;
RT "Draft genome sequence of Dietzia sp.111N12-1 isolated from South China Sea
RT with petroleum hydrocarbons degradation activity.";
RL Submitted (FEB-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:OAV78651.1}.
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DR EMBL; LSSV01000025; OAV78651.1; -; Genomic_DNA.
DR RefSeq; WP_067714313.1; NZ_LSSV01000025.1.
DR AlphaFoldDB; A0A199AWW2; -.
DR STRING; 1785156.AYO52_12135; -.
DR Proteomes; UP000092558; 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; 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};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:OAV78651.1}.
FT DOMAIN 178..347
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 372..518
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 624..862
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 884..1013
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..522
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 530..1029
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 1029 AA; 112059 MW; 6A813920FEF3821A CRC64;
MVSRDSSRPR LPSPGRLGLL DDRAADWLDY LGWTDDDAVP VLWSLSRAPD PDLALGALVR
LHESLTAESH DEGPSARAGA DTGVAALDAA LRSDSRLRAR LLGLLGSSSA LGDHLVAEPT
RWALLRGGLP TFEDVLADML GAVEAVPEQA VEGAPPPSQR EDLRSVGTYR AGVTGGAAVS
VLRSTYRDHV ALLAAHDVAG SVDDDEPVLP FTEVGRRLSD LADAALTAAL AVAVATVHPD
SPMPARLGVV AMGKGGAREL NYISDVDVIF VAEPADARTG RVAGELMRIG SMAFFEVDAA
LRPEGKSGEL VRTLDSHTAY YKRWAKTWEF QAQLKARPMT GDLALAVEYH DTVHPMVWTA
AERDDFVHDV QAMRRRVEEN VPEALREREL KLGRGGLRDV EFAVQLLQMV HGRTDEDLRV
TSTVEALGAL RDGGYIARED GAELLAAYEF LRLLEHRLQL QRYKRTHLLP EDDDEEAYRW
LARAAHIRPD GPNDAAQVLR QSLRELRRRV RRLHSKLFYR PLLDSIASYD AEALSLSTEA
MERQLAALGF AAPRNALGHL RALAGQSSRR GRIQALLLPT FMEWLADTAD PDAGLLAYRR
LCEENEEITW FLRTLRDDSI VARRLVRVLG TSAFVAGLLM RNPEVIPDLT DGAQGPVLVA
SKVSDIASAL TASAARHPTP ERVIATARSL RRAELARIGA ADVLQMISVP DVGRRLSAVW
RAVLEASLAA VVRDMMPEGG AAPARLAYIG MGRLGGDELS YSSDADVMIV CDPVEGAKEE
EAVRWATQVA ERVGKLLASP SSDPPLDLDA DLRPEGRNGP LVRTLASYRA YYAKWAETWE
LQALLRASFA AGDRELGLDF LHMIDEFRYP EQGVPPKVVQ QIRRMKARID SERLPRGADP
ATHTKLGRGG LADVEWSAQL LTMQHAARVP GLHTTSTLEA LDAAASAELL PESERDALVD
SWLMAAHARN ALVLARGKAV DQLPGQGSIL AAVAMICTGS ADGAGFLNEY LRVTRLGRKA
VDHVFWGED
//
