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Database: UniProt
Entry: A0A346NPA8_9ALTE
LinkDB: A0A346NPA8_9ALTE
Original site: A0A346NPA8_9ALTE 
ID   A0A346NPA8_9ALTE        Unreviewed;       967 AA.
AC   A0A346NPA8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=D0Y50_14010 {ECO:0000313|EMBL:AXR07365.1};
OS   Salinimonas sediminis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Salinimonas.
OX   NCBI_TaxID=2303538 {ECO:0000313|EMBL:AXR07365.1, ECO:0000313|Proteomes:UP000262073};
RN   [1] {ECO:0000313|EMBL:AXR07365.1, ECO:0000313|Proteomes:UP000262073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N102 {ECO:0000313|EMBL:AXR07365.1,
RC   ECO:0000313|Proteomes:UP000262073};
RA   Cao J.;
RT   "Salinimonas sediminis sp. nov., a piezophilic bacterium isolated from a
RT   deep-sea sediment sample from the New Britain Trench.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP031769; AXR07365.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A346NPA8; -.
DR   KEGG; salm:D0Y50_14010; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000262073; 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:AXR07365.1};
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|HAMAP-Rule:MF_00802,
KW   ECO:0000313|EMBL:AXR07365.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:AXR07365.1}.
FT   DOMAIN          38..281
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          312..449
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          570..827
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          848..943
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   REGION          1..456
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT   REGION          464..967
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   967 AA;  110519 MW;  931C78BA9CE48EE7 CRC64;
     MPTQMQMNRI IEQKGLAHWQ RLSEHAEAPD FSAFKDTVVA MFGHSDFIAE HCIAHPEWLA
     SLLDDNALHA FTQHSDTATV YIPPYASMLR ELLTGITSED AMHRALRLFR NQHMLTLAWL
     DLANQQPIEV SLARTSALAD ALIYQAYLWV YQQLAQRYGE PAGPHGPQPM LMLAMGKLGG
     MELNFSSDID LIFCYPYKGE TAGGKKSLEH QQFFNKVAQK LIGALNKVTV DGQVFRVDMR
     LRPFGESGPL VTHFSALEDY YQEQGRSWER FAMIKARPVN PRGDYNDELL QILRPFTFRR
     YLDFTTIDAL RHMKGLINRE IRRRGLSNNI KLGPGGIREV EFFAQSFQLI HGGREPLLRQ
     RGLKLTLAAL AELGIVEADA IATMYDNYLF LRKLEHTLQQ LNDEQTQTLP EDEWAQSVLT
     SVMGCASYSA LTTELDSRMA AIHAQFNELV EEHHEAHDET DTLFTQCQDA WQVDLSQEEF
     SRLLTPHLDP RESEQAFRLL ADFRTSLRQF RLGERGVSTL DELMPELLHT LIQAHPDRLE
     QVMRRVLDVI KAITGRTTYL NLLLENLDVL KQLVKLCERS EWIATQIKRF PLLLDELLTP
     LYLEQQNTSL EESRAQYSDE LRQLLLRVDP DDVELSMDTC RQFKLCQQLR IAASDISGSL
     PINKVSDKLT ILAEVILDTV IRQAWQQMAS RYGQPAHLPA DQLGFAVIGY GKLGGYELGY
     GSDLDLVFIH NAPRDVHTDG KRSVSAQQFY IKLAQRIMHL LNTTTLFGQL YETDLRLRPS
     GAAGLLCCHV EGFATYQREE AWTWEHQALV RARGVAGDGD LISTFEEVRK NILTLQRPLP
     SLVSDVTSMR EKMRSHLERT RDEGIDLKQC AGGITDVEFI TQYLVLGYSH KFDDLVRYTD
     NLRILDTACE LGVIDAQSSE HLQQAYLQLR DAYHQLTLAD DKFAQNTQTL DRLRNWVRKT
     WQQVLSV
//
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