GLNE_HAHCH
ID GLNE_HAHCH Reviewed; 963 AA.
AC Q2SN48;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00802};
DE AltName: Full=ATP:glutamine synthetase adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00802};
DE AltName: Full=ATase {ECO:0000255|HAMAP-Rule:MF_00802};
DE Includes:
DE RecName: Full=Glutamine synthetase adenylyl-L-tyrosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_00802};
DE EC=2.7.7.89 {ECO:0000255|HAMAP-Rule:MF_00802};
DE AltName: Full=Adenylyl removase {ECO:0000255|HAMAP-Rule:MF_00802};
DE Short=AR {ECO:0000255|HAMAP-Rule:MF_00802};
DE Short=AT-N {ECO:0000255|HAMAP-Rule:MF_00802};
DE Includes:
DE RecName: Full=Glutamine synthetase adenylyl transferase {ECO:0000255|HAMAP-Rule:MF_00802};
DE EC=2.7.7.42 {ECO:0000255|HAMAP-Rule:MF_00802};
DE AltName: Full=Adenylyl transferase {ECO:0000255|HAMAP-Rule:MF_00802};
DE Short=AT {ECO:0000255|HAMAP-Rule:MF_00802};
DE Short=AT-C {ECO:0000255|HAMAP-Rule:MF_00802};
GN Name=glnE {ECO:0000255|HAMAP-Rule:MF_00802}; OrderedLocusNames=HCH_01044;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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:0000255|HAMAP-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:0000255|HAMAP-
CC 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:0000255|HAMAP-
CC Rule:MF_00802};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00802};
CC -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000255|HAMAP-
CC Rule:MF_00802}.
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DR EMBL; CP000155; ABC27926.1; -; Genomic_DNA.
DR RefSeq; WP_011395001.1; NC_007645.1.
DR AlphaFoldDB; Q2SN48; -.
DR SMR; Q2SN48; -.
DR STRING; 349521.HCH_01044; -.
DR PRIDE; Q2SN48; -.
DR EnsemblBacteria; ABC27926; ABC27926; HCH_01044.
DR KEGG; hch:HCH_01044; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_6; -.
DR OMA; EFMVQYA; -.
DR OrthoDB; 427701at2; -.
DR Proteomes; UP000000238; 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; 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 Gene3D; 3.30.460.10; -; 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; PTHR30621; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 2.
DR Pfam; PF03710; GlnE; 2.
DR SUPFAM; SSF81301; SSF81301; 2.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..963
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_1000133906"
FT REGION 1..451
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 461..963
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 963 AA; 109664 MW; 3A6E3E86D9B9328C CRC64;
MAAPSELQLY PSVIHPAIQK YWDEFCELPA ETLSAFSSYY PDILRAFAVS DFLALNILRE
PELVLSFLQS SQHQKECQLV DFRAPLAEEL SGALKEDDLL RILRLFRRRM MFRIIWRDLV
CLVDYQVTTR EVSWLAETCI DEALSWIYRD MSQQFGEPHS TAGVKQQLVV LAMGKLGANE
LNVSSDIDLI FTFPERGETQ GGNRSLDNQA FFTRLGQRLI QALDNTTADG FVFRVDMRLR
PYGQSGALAL SFAAMEAYYQ EQGRDWERYA MIKARAVAGD IDAGEELLTS LKPFVYRKYI
DFGAVQALRA MKEMIEREVQ RKGQDGNIKV GRGGIREIEF IVQVFQLMRG GRDVRLQQRN
LLSTLECLED EGLLPVAAAA ELREAYIFLR NLEHAIQGLE DKQTQEIPKD EEGRERVAVA
MGFPGWGACR VQLDKYRDCV SEHFADIIAE RREAPLERPD TIEWKALWAG RLAQDEAQDL
LLRSGCDQAQ EIYEAVTQLR QSSRVQHMQL QGKERLDEFM PNLLQSLAQS RASHETCRRL
LALVEAVLRR SAYLALLNEN PGALTELIRL FAESAWIARQ IVTTPLLLDE LLHSGSLYTP
PDTTALRDEL RQQMLRIPND DLEEQMEALR YFKKAHVLRV AASDLRETLP LMKVSDYLTF
IAETIIEQVV DEAWETMVKK YGEPGYEDAA LNDMRFAVIG YGKLGGIEMS YGSDLDLVFL
HGASGDLSTS GETSIANQVF FTRLGQRIIH LLTTKTASGD IYEVDMRLRP SGNSGLLVSS
VSAFQQYQEK SAWTWEHQAL VRSRAVAGCP GIRAEFEKVR KDILTQHRDP AKLRTEVMDM
REKMHASLGT KPDSSGSPPY FDLKHDRGGI VDIEFMVQYA ALRWANEYPQ IVVWSDNIRI
LEALGDAGVF SQEDADKLCD IYRLLRAHGH RLALQNLPAR IQTDELLEER RWVVAFWEKV
FAE
