ID X2K1V4_AGGAC Unreviewed; 977 AA.
AC X2K1V4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00802};
DE AltName: Full=ATP:glutamine synthetase adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE AltName: Full=ATase {ECO:0000256|HAMAP-Rule:MF_00802};
DE Includes:
DE RecName: Full=Glutamine synthetase adenylyl-L-tyrosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_00802};
DE EC=2.7.7.89 {ECO:0000256|HAMAP-Rule:MF_00802};
DE AltName: Full=Adenylyl removase {ECO:0000256|HAMAP-Rule:MF_00802};
DE Short=AR {ECO:0000256|HAMAP-Rule:MF_00802};
DE Short=AT-N {ECO:0000256|HAMAP-Rule:MF_00802};
DE Includes:
DE RecName: Full=Glutamine synthetase adenylyl transferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE EC=2.7.7.42 {ECO:0000256|HAMAP-Rule:MF_00802};
DE AltName: Full=Adenylyl transferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE Short=AT {ECO:0000256|HAMAP-Rule:MF_00802};
DE Short=AT-C {ECO:0000256|HAMAP-Rule:MF_00802};
GN Name=glnE {ECO:0000256|HAMAP-Rule:MF_00802};
GN ORFNames=CF65_01857 {ECO:0000313|EMBL:AHN72110.1};
OS Aggregatibacter actinomycetemcomitans HK1651.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=272556 {ECO:0000313|EMBL:AHN72110.1, ECO:0000313|Proteomes:UP000019758};
RN [1] {ECO:0000313|EMBL:AHN72110.1, ECO:0000313|Proteomes:UP000019758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK1651 {ECO:0000313|EMBL:AHN72110.1,
RC ECO:0000313|Proteomes:UP000019758};
RA Gillaspy A.F., Griffin J., Najar F., Hinkle J., Lewis L.A.,
RA McLaughlin R.E., Hartman K., Nydick C., Gipson M., Conway B., Vaughn J.,
RA Thompson C., Gipson J., Maddera L., Carson M., Kenton S., Lai H., Roe B.A.,
RA Orvis J., Zaitshik J., Griffin J., Scott E., Dyer D.W.;
RT "Genome sequencing and closure of the periodontal pathogen, Aggregatibacter
RT actinomycetemcomitans.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-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:0000256|HAMAP-
CC 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:0000256|HAMAP-
CC Rule:MF_00802};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00802};
CC -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000256|HAMAP-
CC Rule:MF_00802}.
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DR EMBL; CP007502; AHN72110.1; -; Genomic_DNA.
DR RefSeq; WP_025298333.1; NZ_CP007502.1.
DR AlphaFoldDB; X2K1V4; -.
DR SMR; X2K1V4; -.
DR KEGG; aah:CF65_01857; -.
DR PATRIC; fig|272556.10.peg.1273; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_6; -.
DR Proteomes; UP000019758; 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 activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR Gene3D; 1.20.120.1510; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR Gene3D; 1.10.4050.10; Glutamine synthase adenylyltransferase GlnE; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 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:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME; 1.
DR PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 2.
DR Pfam; PF03710; GlnE; 2.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00802}; Ligase {ECO:0000313|EMBL:AHN72110.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00802};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00802};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00802};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00802};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:AHN72110.1}.
FT DOMAIN 46..290
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 314..469
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 586..838
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 859..950
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..474
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 481..977
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 977 AA; 112463 MW; D23C2A08EADC0559 CRC64;
MSFVASFSDK LNSLAEMLIQ SFPEQFDSAL FAQIRQQKDD PASHIGQIAV AVAMSDFVVE
VWQKQPHFLA KCWQNPPHFD DCDHYAERLD AVLQKVQTEE EFYRSLRQFR AREMVKLSFC
QSLNLATVEQ IFIRLSQLAE SLIIGARDWL YVRACEEMGT PMDAQGNAQQ LYILGMGKLG
GFELNFSSDI DLIFTYPSQG ETVGARRNID NAKFFTRLGQ RLINALDQYT ADGFVYRTDM
RLRPFGDSGA LALSFNAMEQ YYQDQGRDWE RYAMIKRRIL GAQTTDPNVT VLQNLLRPFV
YRRYIDFSVI QALRDMKQKI EREVRRRNLT DNIKLGAGGI REVEFIVQVF QLIRGGREAA
LQQPELLSLL PELTKLHLIS DEQETQLRHA YLFLRRAENV LQAIKDQQTQ QLPDNESDRQ
RLIFACAEFT QWNAQRKSVN IRYPIHDWSG FLDVLHDHQR KVRSVFQSLI GDEQEENTSE
NEWEDFLETD FDEQELLGIL QQNGVPETEQ DVVLDRLLQF RNELPRYAIG VRGRAVLNRL
MPNVLQQVLY TPHCPILLPR ILTIIEKILT RTTYLELLAE NPQALTQLIE LCAQSKFIAE
QVARHPILLD ELLDQKSLRN PPHFTEYASE LQQYLLRLPQ GDEEQFIDGL RQFKHAALLR
IAAADILGVL PVMKVSDHLT YLAEAIIGAV VNLAWQQIAV RFGVPEHLAE GQKNFLVVGY
GKLGGIELGY KSDLDLVFLY DPATNSQTVG GKKVIDSNQF YLRLAQKIVS IFSMNTSAGI
LYDVDMRLRP SGDAGLLGCS FAAFENYQLN EAWTWEKQAL VRSRAVFGEP KLREEFDAIR
RKVLAAPRDL AKLKQDVCEM RKKMYQHLTQ QTENQFNIKT DSGGITDIEF IAQYLVLAHS
PQQPALTRWS DNVRIFDIMV KYGVISETDG ERLKQCYVDL RNRTHHLNLL GLPSVVNASE
FHAERAFVRE IWARLFY
//
