ID A0A221NW42_9ACTN Unreviewed; 1021 AA.
AC A0A221NW42;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=LK07_09220 {ECO:0000313|EMBL:ASN24191.1};
OS Streptomyces pluripotens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1355015 {ECO:0000313|EMBL:ASN24191.1, ECO:0000313|Proteomes:UP000031501};
RN [1] {ECO:0000313|EMBL:ASN24191.1, ECO:0000313|Proteomes:UP000031501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 137 {ECO:0000313|EMBL:ASN24191.1,
RC ECO:0000313|Proteomes:UP000031501};
RA Ser H.-L., Lee L.-H.;
RT "Genome sequence of Streptomyces pluripotens MUSC 137T.";
RL Submitted (JUL-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}.
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DR EMBL; CP022433; ASN24191.1; -; Genomic_DNA.
DR RefSeq; WP_043434968.1; NZ_CP022433.1.
DR AlphaFoldDB; A0A221NW42; -.
DR STRING; 1355015.LK06_008120; -.
DR KEGG; splu:LK06_008120; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000031501; 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:UP000031501};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:ASN24191.1}.
FT DOMAIN 88..311
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 346..476
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 634..843
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 883..1008
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..480
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 488..1021
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 1021 AA; 110765 MW; F27F57F5EA4D31CC CRC64;
MTPGRRSSTF TRLLRHGFTD PSAAERLLDC PELIPVRDDP VLLEALGGTA DPDLALHGLV
RLLEAQDGPT AHRELLDTLI AAKPLRDRLL GVLGASTALA DHLARHPGDW QALVTYEPHD
LHPGLTEFER GLEAATDPVS LRIAYRRCLL SIAARDVCGT TEMADTAAEL ADLATATLRA
ALTIAEAAAP EDAAACRLAV IAMGKCGGHE LNYVSDVDVI FVAESAEDTS EAKALRSATR
LASHLMRICS ESTVEGSIWP VDANLRPEGR NGPLVRTLSS HLAYYQRWAK TWEFQALLKA
RPVAGDTDLG RAYIDALEPL VWQAAERDNF VTDVQKMRRR VVENIPAAEV ERELKLGPGG
LRDVEFAVQL LQLVHGRTDA SLRSGTTLDA LQALAAGGYV GREDTARLDE AYRFLRSMEH
RIQLYRLRRT HLVPEAESDL RRLGRSLGLR TDPVAELHRE WKRHTGVVRR LHEKLFYRPL
LDAVAQLAPG ETRLSPEAAR ERLVALGYAD PAAALRHLEA LASGVTRKAA IQRTLLPVLL
GWFAESADPD AGLLNFRKVS DALGKTPWYL RLLRDEGAAA ENLARVLSAG RLAPDLLMRA
PEAVALLGDG TGMGAGMGTG TSAGSGRGLA PRDRAHLEQE VLAAAGRAEN VEQGVAAARG
VRRRELFRTA AADIVSSYGT ETSPAEADQG ALVDRVGAAV SDLTAATLAG TLRAVVRDGW
GDTLPTRFAI IGMGRFGGHE LGYGSDADVL FVHEPRDGVP EQEAATAAGK VVTEMRRLLQ
LPSSDPPLLI DADLRPEGKS GPLARTLKSY EAYYRRWSLV WESQALLRAE PVAGDEDLGR
RFTALIDPLR YPLHGLGEDA VREIRRLKAR MESERLPRGA DPKLHTKLGP GGLSDVEWTV
QLLQLRHGWH LPGLRTTRTR EALSAACEAG LLSVEDTETL DEAWVLATRV RNAVMLVRGR
AGDTFPTEPR ELAAVGRYLG YGAGHAGDML DAYRRTTRRA RAVVDELFYG DGVRAGAGSG
G
//
