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Database: UniProt
Entry: A0A1X1QH86_9GAMM
LinkDB: A0A1X1QH86_9GAMM
Original site: A0A1X1QH86_9GAMM 
ID   A0A1X1QH86_9GAMM        Unreviewed;       972 AA.
AC   A0A1X1QH86;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=A6F71_05505 {ECO:0000313|EMBL:ORU90424.1};
OS   Cycloclasticus sp. symbiont of Poecilosclerida sp. M.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=1840537 {ECO:0000313|EMBL:ORU90424.1, ECO:0000313|Proteomes:UP000193579};
RN   [1] {ECO:0000313|EMBL:ORU90424.1, ECO:0000313|Proteomes:UP000193579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Specimen M {ECO:0000313|EMBL:ORU90424.1};
RA   Rubin Blum M., Dubilier N.;
RT   "Short-chain alkanes fuel the metabolism of mussel and sponge
RT   Cycloclasticus symbionts from deep-sea gas and oil seeps.";
RL   Submitted (APR-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:ORU90424.1}.
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DR   EMBL; LWTN01000221; ORU90424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1QH86; -.
DR   STRING; 1840537.A6F71_05505; -.
DR   Proteomes; UP000193579; 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; 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}; Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00802};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193579};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802}.
FT   DOMAIN          63..304
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          330..467
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          580..831
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          866..945
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   REGION          1..471
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT   REGION          484..972
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   972 AA;  109036 MW;  FDCAD33EB50B9986 CRC64;
     MILFELSIYF LNTLMSKLKI NSCIKDIPEP LQEVTERQLL VFLEKCEEQA VDLKVADSQL
     ALVSQAFAMS KFIADYAVTR TEPFLELLSS GDLEKLREPD DIKAALALFL SSVETEEQLM
     AGMRAFRNRE MVRIAWRDLL GLASLDETLC DLSHLADACL IFALDFLYQK SCDLRGAPLD
     SSGRPIELVV LGMGKLGAKE LNYSSDIDLI YAYSEEGEFP GKREYSYHEF FTAICKKLTK
     VLNEQTADGF VFRVDTRLRP FGDSGPLVMS FAAMESYYLG QAREWERYAM VKARVITGDS
     ETGCALMNIL NPFIYRRYLD YSALDSLRGL KEQINKENER KSRANNVKLG LGGIREIEFI
     GQAFQLIRGG REKSLQERGI LKVLELLGEK NCLPSMLTSE LQEAYVYLRK VENRLQEYAD
     KQAHNLPEAE GDRIRLAWSM GHQNWDEFML ELNAFRKQVH EVFSQVFEAP HADTALVDKP
     ASIAWEQDEK VAIDALSGLG YEEPEDAVEQ LEQFRRSLAF KMAGSRAIEV FNRLMPLVLS
     AVGCCKSSKV ALQRILALLE TIARRTSYLS LLLEHPMVIS QLVKLSATSG WINQLIVRTP
     ILLDELLDPG VLYEPLSKAA LAADAEIRLA RVDAPDTERV VEELLHFKNA NVLRVATADV
     LELIPLMVVS DYLTDIAEVV LARVVDHAWQ LVSASSGVPE GQSIDKVGGF AVIAYGKMGG
     IELSYSSDLD LVFLHNGKAD GQTNGEQPIS AEAFYTRLGR RIMTILNSHE VGGRLYEVDM
     RLRPSGNSGL LVSNLDAFEY YQQNTAWTWE HQALVRARFV SGDSVVGERF SGIRLAVLQK
     ERDKKLLQQE VKAMREKMRV ALIHKDKAIF DLKQGGGGVA DIEFIVQFFV LSGALCGHNS
     LEFTDNIRLI KGLAKVGSLT ADEANGLVES YRAYRRKTHQ LALQEKPALV DDVEFAEFRE
     KVTSSWSKII GG
//
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