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Database: UniProt
Entry: A0A1E7R3J2_9GAMM
LinkDB: A0A1E7R3J2_9GAMM
Original site: A0A1E7R3J2_9GAMM 
ID   A0A1E7R3J2_9GAMM        Unreviewed;       921 AA.
AC   A0A1E7R3J2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
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:KAA8733183.1};
GN   ORFNames=BJI46_13945 {ECO:0000313|EMBL:OEY93847.1}, F4V57_08105
GN   {ECO:0000313|EMBL:KAA8733183.1};
OS   Acinetobacter qingfengensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1262585 {ECO:0000313|EMBL:OEY93847.1, ECO:0000313|Proteomes:UP000185895};
RN   [1] {ECO:0000313|EMBL:OEY93847.1, ECO:0000313|Proteomes:UP000185895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 4671 {ECO:0000313|EMBL:OEY93847.1,
RC   ECO:0000313|Proteomes:UP000185895};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAA8733183.1, ECO:0000313|Proteomes:UP000323633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 69710T {ECO:0000313|EMBL:KAA8733183.1,
RC   ECO:0000313|Proteomes:UP000323633};
RA   Pineiro-Iglesias B., Tunovic T., Unosson C., Inganas E., Ohlen M.,
RA   Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA   Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT   "Draft genome sequence of various Type strains from the CCUG.";
RL   Submitted (SEP-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   -!- 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:OEY93847.1}.
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DR   EMBL; VXKN01000005; KAA8733183.1; -; Genomic_DNA.
DR   EMBL; MKKK01000040; OEY93847.1; -; Genomic_DNA.
DR   RefSeq; WP_070070380.1; NZ_VXKN01000005.1.
DR   AlphaFoldDB; A0A1E7R3J2; -.
DR   STRING; 1262585.BJI46_13945; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000185895; Unassembled WGS sequence.
DR   Proteomes; UP000323633; 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: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; 1.20.120.330; 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:KAA8733183.1};
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:OEY93847.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185895};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:OEY93847.1}.
FT   DOMAIN          18..246
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          275..413
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          514..768
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          790..885
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   REGION          1..417
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT   REGION          425..921
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ   SEQUENCE   921 AA;  105711 MW;  61B2DCF0D2442D90 CRC64;
     MNQQHEESSS ARRVQFCSLY AGQVMQNQDG IWQQDYAQDQ FLTCLSTQQI FQKVDQSLQG
     IQDEAIWMQA LRKLRARLML RWIWQDCNAL TDVPQLTREL SDFADACVIA AKDFARPALV
     KKHGEPIGEN GQVQDLIVLA MGKHGAQELN LSSDIDLIFS FDENGESNGR KCIDVQQFCI
     LWGQKIIYLL DHITADGFVF RVDMRLRPWG NGSALAMSHA ALEKYLIQHG REWERYAWIK
     ARAITGGEVG QDLIRMSRPF VFRKYVDYTA FAAMREMKSM IEKEVARRQI DDDVKLGAGG
     IREIEFIVQV FQLLYGGSKL ELQDRQCLVA MQHLMNDQLI SMQAYEELKD AYLFLRRVEH
     AIQALQDQQT QNLPIDEQLR QRLIYALNFA SWDEFITQLN QRREKVSFYF SHLIQERIQE
     VDQPDDSLDN EDLKNYLDAQ AYQHVEQFWQ SNAVQRLPST ALKRLKQFWP HLIKAILNAQ
     QPQTALMRLL PLIESILRRS VYIVMLMESR GALQRLVKMA EVSPWICEEL AHYPVLLDEF
     LSMDFELPHR SDLENALRQQ LLRLTSDDVE DIMRVLRLFK KSNVLAVAAS DVLAESPLMR
     VSDVLTDIAE ITVKAALHLS YQMVAQRHGY PVNMQGERCS LDQLDFTVIG YGKVGGIELG
     YGSDLDLVFI HQYQEQTETD GKKSISGLEF AMRVAQKFMS LMTTQTLDGR VYDVDTRLRP
     NGDAGLLVCS LRAFEHYQLQ NAWLWEHQAL VRARSIAGDT ALCQAFEQLR CRILTQKRNE
     NEVRAEVLNM RQKMKDHLGS SAEQKKHGVF HLKHDTGGIV DIEFMAQYAV LAWSGTNPDL
     AHYSDNVRIL EDAAKAGCLP SNDATALTQA YLRERAESHR LALANQSLQV NAADWQDTRE
     VVYKLWQRLI DPNANVVLGG K
//
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