GLNE_VIBCH
ID GLNE_VIBCH Reviewed; 948 AA.
AC Q9KPD4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=VC_2438;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF95580.1; -; Genomic_DNA.
DR PIR; C82077; C82077.
DR RefSeq; NP_232067.1; NC_002505.1.
DR RefSeq; WP_000056837.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KPD4; -.
DR SMR; Q9KPD4; -.
DR STRING; 243277.VC_2438; -.
DR PRIDE; Q9KPD4; -.
DR DNASU; 2612980; -.
DR EnsemblBacteria; AAF95580; AAF95580; VC_2438.
DR GeneID; 57741044; -.
DR KEGG; vch:VC_2438; -.
DR PATRIC; fig|243277.26.peg.2323; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_6; -.
DR OMA; EFMVQYA; -.
DR BioCyc; VCHO:VC2438-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..948
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209281"
FT REGION 1..444
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 452..948
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 948 AA; 109334 MW; 2FD4BF9F4E93433E CRC64;
MSLPSALLPT AELHYQSLIS EHPHIANWPS SVLNQLRYVL GLSQFVAQTL QRDDPLCQVL
PSLLAKPSRE QYYRSELAQW LAECQDEAVA QKRLRQFRNQ EMVYIAWRDF CASWTLEESL
SHLSQLAEAL IFESYQWLYQ RCCLEMGTPC NAQGEAQPML IIGMGKLGGG ELNFSSDIDL
IFTYPENGET QGARRSIANA QFFTRLGQRL IKLLDQSTPD GFCYRVDMRL RPFGDSGPLA
MSYAALEDYY QEQGRDWERY AMIKARVMGR EMYPQYQELR QMLRPFVFRR YIDFSAIQSL
RRMKSMISSE VRRRGLSNNI KLGAGGIREV EFIAQVFQLI RGGREPSLRK RGLLETLDAI
AELELLTREQ VQDLRDAYRF LRRLENLLQA MADKQTQTLP DKEDDQLRLS IAIGLADWPS
LQREVSEHMQ RVHRVFATLI GEEDEEEEHT VARHFHELWD MAHKPEVIEH IIEQDLGLSD
AGEQIRTITQ FKDDLAKRTI GPRGREVLNR LMPKVYQAVF AHPDAEFGLS RVLALLHSIA
TRTTYLELLD EHPAALVQLV RLCTASPMIS EQLARYPILL DELIDPQHLY NPIPLESYQT
ELRDFLARIP EEDMEQQMEG LRQFKQISIL RIAAADIAGV LPVMKVSDHL TYLAEAIVEA
VVSQAWLQVS SKYGEPTHLK HRDGRGFAVV GYGKVGGWEL GYNSDLDIVF MHDCPVEVNT
DGEKSIDGRQ FYLRLAQRII HIFSTRTASG ILYEVDTRLR PSGASGLLVS PTDAFDEYQR
QEAWTWEHQA LVRARMIYGD APLQQAFANT RHQILCLPRE EHKLKQEVVE MRIKMRDHLG
GKKAGRFMLK QDEGGITDIE FLAQYLVLRF SHQQPKLTRW SDNVRIFESL MNHQVMSESQ
ALALTHAYTS MRDQIHRRNL LNQSADVRDS QFVVEREQVI QAWQQWLG
