GLNE_BIFLS
ID GLNE_BIFLS Reviewed; 1076 AA.
AC B7GRV5; E8MKK4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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};
GN OrderedLocusNames=Blon_1452, BLIJ_1498;
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=391904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
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; CP001095; ACJ52535.1; -; Genomic_DNA.
DR EMBL; AP010889; BAJ69081.1; -; Genomic_DNA.
DR RefSeq; WP_012577774.1; NZ_JDTT01000019.1.
DR AlphaFoldDB; B7GRV5; -.
DR SMR; B7GRV5; -.
DR PRIDE; B7GRV5; -.
DR EnsemblBacteria; ACJ52535; ACJ52535; Blon_1452.
DR KEGG; bln:Blon_1452; -.
DR KEGG; blon:BLIJ_1498; -.
DR PATRIC; fig|391904.8.peg.1511; -.
DR HOGENOM; CLU_006233_1_0_11; -.
DR OMA; EFMVQYA; -.
DR Proteomes; UP000001360; 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; Transferase.
FT CHAIN 1..1076
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_1000148541"
FT REGION 1..521
FT /note="Adenylyl removase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 524..1076
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00802"
FT REGION 1041..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 119998 MW; 7283EB111BFC7999 CRC64;
MESSMFKPSS MDLIRAGLQD LDRARALFGQ LKADAIADGR CAELLGVLAH ACDPDVALGN
FVDIVNAMQS SRRDLDRVIP DAGALRRLIT VLGASDAMGK FMRFRPELVE AASVGSADSH
LFNRAQRRAR LLMAVGADPD DQAMPVASKD LAEAATALRA GYRRQLAAII AQDVMAEDPI
RIQPTISSEL SDLADAALEG ALAIARHETE GNEHVRFTII GMGKLGAQEL NYVSDVDLIY
VVEPADKDVD HQTLIRVGTK MGTMLQRVCQ SVIMGVAEQP LWQIDGGLRP EGKDGALVRV
LSSHKNYYEQ WAENWEFQAL LKARPVAGDP DLGQAYMDMS RPFVWSASKR KNFVYDCQKM
RKRVEDLIPA PLKDREIKLG RGGLRDVEFT VQMLQLVHGR TDESLRTSNT LDSLQRLSEG
GYVSRKQAVR MSQDYRFERV MEHRQQIWSL KRTHLFPDLG RASVGGLEKK RDIDVDELNQ
NQELRRLARA FGLHPEELVD KYDDTRREVR HLHLDIYYRP MLPVNAQMEN DQIVLSVEAA
QERFESIGFG DPDAAIRHVQ ALTAGVGRAA KINRIILPAV LQWLGEGQNP DMGLLNWRKL
EENFGTESGY LGFLRDSTSA AQRLCHILSN SRFLGDALNK SVESISWLGD DGNLQARTRE
ALDVQTGSAL ERFGSNINEF ATSMRAMRRH EIERIGLSWM SGVISDSDSL KAMTDVYDAI
IDASLTWAVR HQIAAFGVET APAGITVIAM GRYGGREVNF SSDADAILIY RPADDADDGQ
ANAFAKKVVE DLRNILQGPT TLEPKIELDL DLRPEGKNGP LVRSYASCEE YYESWASTWE
RQALLRARYA AGDAELARDF LINIADPLRY PTAELTEAEL QNIRKLKARM EAERLPRGVR
RERHLKLGKG GLSDVEWTVQ LMQLQHAGDI KDLRVNGTLE ALDVLEAKKL ISAIDAIQLR
KTWTLCTAAR NGNYLWSGRA NQADILPDDI YSLGGIAVYL GYGAHRGQHF ENDLLAVMRK
CRDVCQRLFY GQTEGEATAA ATATASAATP QPQTAPRPRM HVIAPRLERN RRRAQR
