GLNE_PHOPR
ID GLNE_PHOPR Reviewed; 957 AA.
AC Q6LUZ6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=PBPRA0448;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(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; CR378664; CAG18879.1; -; Genomic_DNA.
DR RefSeq; WP_011217235.1; NC_006370.1.
DR AlphaFoldDB; Q6LUZ6; -.
DR SMR; Q6LUZ6; -.
DR STRING; 298386.PBPRA0448; -.
DR EnsemblBacteria; CAG18879; CAG18879; PBPRA0448.
DR KEGG; ppr:PBPRA0448; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_6; -.
DR OMA; EFMVQYA; -.
DR OrthoDB; 427701at2; -.
DR Proteomes; UP000000593; Chromosome 1.
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..957
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209265"
FT REGION 1..449
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 457..957
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 957 AA; 108957 MW; E64E8633A48F3D98 CRC64;
MTQHLERPEL LSIAATKALD KLQQAHPELL AQWPTERQNE LETVIGLSDF IASSLVCDGQ
LLLWLSEHLD DKEHAEQYRQ QLETKLATTA DDVGLMRQLR AFRRQEMVWI AWRDFTNKST
LEQSLAHLSQ LAEALIMEAY QWLYNQCCKE WGTPTNSAGE AQPMLVLGMG KLGGGELNFS
SDIDLIFTYP ENGDTVGGRR SMANAQFFTR LGQRLIKALD QPTYDGFCYR VDMRLRPFGD
SGPLVMSYAA LEDYYQEQGR DWERYAMIKA RVMGRESFTQ YQELRQMLRP FVFRRYIDFS
AIQALRRMKS MISSEVRRRG LSNNIKLGAG GIREVEFIAQ SFQLIRGGRE PSLRGRGLLE
TLAAMKQLAL LPEKQIEHLE QGYCFLRKLE NLLQAIDDKQ TQTLPDKPLD QIRLAFAMGY
ADWQSLFEAI ELHMSAVHLV FDDIIGTDED DAGCSVSEQY NEMWTMAKDE DVLLNIMAEL
EAPDSANQVS TILGMKAELS KRTLGPRGRE VLTRLMPEVL SRIVPRPDAS AVLARVTKLI
VRVATRTTYL ELLGEHPAAL GQLIRLCAAS PMVAEQLTQY PILLDELLDP QHLYNPTPLD
QYGDELREYL ARIPEEDMEQ QMEAIRQYKQ AQLLRIAAAD IAGALPLMAV SDHLTYLAEA
IITAVVNQAW LQMAEKYGEP THLVDRNGKG FGVIGYGKVG GWELGYGSDL DVVFLHDCPA
DIYTNGKKEI DGRQFYLRLA QRIVHLFSTR TSSGVLYEID VRLRPSGASG LLVSTVESFD
EYQQKEAWTW EHQALVRARM IYGDVPLFDA FSDVRKRILT QPRDTQSLQV DVVSMRHKMR
VHLGSKKNGM FGLKQDKGGI TDIEFLAQYL VLQHSHTEPY LTRWSDNVRI FDTMAECEVL
SLSQASALKQ AYCVMRDDIH RLNLLGLPVY VDESQFVTER ETVQQIWQEY LVPSSDE
