ID A0A1S1NS07_9GAMM Unreviewed; 981 AA.
AC A0A1S1NS07;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ECO:0000313|EMBL:QEL10175.1};
GN ORFNames=BH688_15930 {ECO:0000313|EMBL:OHV07678.1}, FY550_02865
GN {ECO:0000313|EMBL:QEL10175.1};
OS Kushneria phosphatilytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Kushneria.
OX NCBI_TaxID=657387 {ECO:0000313|EMBL:OHV07678.1, ECO:0000313|Proteomes:UP000179907};
RN [1] {ECO:0000313|EMBL:OHV07678.1, ECO:0000313|Proteomes:UP000179907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCWA18 {ECO:0000313|EMBL:OHV07678.1,
RC ECO:0000313|Proteomes:UP000179907};
RA Wang C., Qu L.;
RT "The draft genome suquence of Kushneria sp. YCWA18.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QEL10175.1, ECO:0000313|Proteomes:UP000322553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCWA18 {ECO:0000313|EMBL:QEL10175.1,
RC ECO:0000313|Proteomes:UP000322553};
RA Du G.-X., Qu L.-Y.;
RT "Complete genome sequence of Kushneria sp. YCWA18, a halophilic phosphate-
RT solubilizing bacterium isolated from Daqiao saltern in China.";
RL Submitted (AUG-2019) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MKZT01000024; OHV07678.1; -; Genomic_DNA.
DR EMBL; CP043420; QEL10175.1; -; Genomic_DNA.
DR RefSeq; WP_070981526.1; NZ_MKZT01000024.1.
DR AlphaFoldDB; A0A1S1NS07; -.
DR STRING; 657387.BH688_15930; -.
DR KEGG; kuy:FY550_02865; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000179907; Unassembled WGS sequence.
DR Proteomes; UP000322553; 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: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; 1.10.4050.10; Glutamine synthase adenylyltransferase GlnE; 1.
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:QEL10175.1};
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:UP000179907};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:OHV07678.1}.
FT DOMAIN 39..287
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 308..446
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 566..825
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 847..937
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..450
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 461..981
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 981 AA; 110537 MW; 028E2E9063D7C2FC CRC64;
MSLEIALAIL PEDLQKPVRE TLSQLDEALC AGLGENRLRE LVTVLAGSVF VGEALRRDPQ
LIGRLEAGDE LERAPASAQL SKWLEAALVE VEDEAGMHSA LRRFRRDRMV GIIWRDRNDR
ADAWVTAAAV SRLAEVCVEV ALQWCERHYE ARWGLPSPDE EGRPQRLVVF GMGKLGAGEL
NLSSDIDLIL AYPEKGETVG GRRCLDHQEY FTRLGQKLIN ALDAITEDGF VFRVDMRLRP
LGEGGPLVGS FNTLINYYQD QGREWERYAM LKARPVAGDV AAGRELLETL RPFVYRRYID
FGAIESLREM KTLINREVRR RGREDDIKLG AGGIREAEFV VQAFQLIRGG QMTELQTPSL
HQALSQLVAL DMMGRRDAES LEADYVFLRD LEHALQALHD RQTQTLPEDA LERSRLAFAL
GADDWTALCE RLDEVRQRVR QHFDSVIAPE DEAGEGSEET SLSEWRALWQ SALDEEQALA
LLDEHGFSDA NGALRRIRQL RDSRTVTTMQ RIGFERLEAL MPSLFATVAE VDNPDVTLER
VLTLIEAVLR RTAYLSLLRE NPGALTQFVN LCAASAWIAE QLARHPMLLD ELLDPRTLYS
PAERDQLDEE LRSRLARLAE DDEEAQMEAL RHFRHAQILS VAASDIAGAR TLMHVSDYLT
LIAEVVLQAV VRIAWRALTR KYGHPQARAD RPTADSDDEV ADFLVVGYGK LGGIEMGYGS
DLDLVFLHDA EPQGQTDGPR KIDNSIFFTR LGQRIIHMLT TTTPAGVLYE VDMRLRPSGA
SGLLVSTLEA FADYQRHQAW TWEHQALVRA RAVAGSQALA ARFDEVRREI LSRPRDPATL
REEVLSMRQR MREHLGSSAG ERRAGRFHIK QDPGGMIDIE FMNQYAVLAL SQRFPPLMTF
TDNMRILETL ESAGQLSAEE TRALRTAWLD YRNATHRAAL TRAGSLVDAE RFRGHRNAVT
ARWQALFETS AEANSARNDI E
//
