GLNE_BORPE
ID GLNE_BORPE Reviewed; 941 AA.
AC Q7VYQ0;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
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=BP1260;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE41556.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX640414; CAE41556.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_880032.1; NC_002929.2.
DR RefSeq; WP_050865593.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VYQ0; -.
DR SMR; Q7VYQ0; -.
DR STRING; 257313.BP1260; -.
DR PRIDE; Q7VYQ0; -.
DR KEGG; bpe:BP1260; -.
DR PATRIC; fig|257313.5.peg.1357; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_4; -.
DR Proteomes; UP000002676; 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..941
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209233"
FT REGION 1..431
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 447..941
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
SQ SEQUENCE 941 AA; 104312 MW; 37BAAC62AD66B7F1 CRC64;
MSSAPPFAAA LAWSGHLRRR LDAHPDLAAW LANACAHPVS ANVLAAWQAE LSGPDAPEVL
PVEQCRGMLR KLRERVFLTL IVRDLGGQAD LEEVVGAMTV LADIAVGTAY RSVAAELAAV
HGLPREQSTG DPQEMLIVGM GKLGGRELNV SSDIDLVMLY GDEGETDGPR RISNHEFYGR
LTRRMMPVLS EVDADGQVFR TDLRLRPDGD AGPLAWSLDA LEHYLIGQGR EWERYAWLKA
RLMPAQAFAD SNPDAQARQL ESLRVPFVYR KYFDFDALAA LRALRERIRQ DWQRRALARN
GVDSANNIKL GDGGIREIEF IVQLSQLIRG GRMPALQRRG LLEALHAERA AGLVPEGDAQ
KLEAAYRFLR RTEHALQYRE DEQTHLLPAD PAQRAALAAA LGYEPAAFER TLAEHRAFVS
QTFRNAFRLA GMGEEDDSPA PARTHANGHA MRPHAGALHD IEERLAGQIQ RDFPEHAEDL
LRRTETLLGS HRVRSLPDSS RHRLEALLPA ALTAATQTSA PMDAALRLFD LIETIAQRSA
YLALLAEYPD TLARVARMVA ASPWAAQYLT QHPLLLDSLI DWRTLFEPLD FAQVAHQLAA
DLDACRLPDG EPDIERQMNL MRDVQRQASF QLLAQDLEGE LTVEKLADQL SALADLLLAE
TIRRVWPLVN RRPGAEPHLA VIAYGKLGGK ELGYASDLDL VFLFDDDRED AAELYAKLGR
RMTSWLSTMT SSGRLYEVDL RLRPDGNAGL LAVSLEAFEQ YQRSHAWPWE HQALTRARYA
AGDTEAGARF ERIRADILVM PRDVQALRGE VLGMRDKISA GHPNRSELFD VKHDRGGMVG
VEFVTQYLVL CHAATHRVLV NNLGNIALLR LAGEAGLIPA PLALAAGDAY RTLRRAQHQL
RLKGVDKARV PPGQLAAERA TVCELWQTVL QDGTIAQAEV K
