Entry
Name
[glutamine synthetase] adenylyltransferase;
glutamine-synthetase adenylyltransferase;
ATP:glutamine synthetase adenylyltransferase;
adenosine triphosphate:glutamine synthetase adenylyltransferase;
ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase;
ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase;
[glutamate---ammonia-ligase] adenylyltransferase
Class
Transferases;
Transferring phosphorus-containing groups;
Nucleotidyltransferases
BRITE hierarchy
Sysname
ATP:[glutamine synthetase]-L-tyrosine adenylyltransferase
Reaction(IUBMB)
ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine [RN:
R03473 ]
Reaction(KEGG)
Substrate
ATP [CPD:
C00002 ];
[glutamine synthetase]-L-tyrosine [CPD:
C01281 ]
Product
diphosphate [CPD:
C00013 ];
[glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine [CPD:
C01299 ]
Comment
This bacterial enzyme adenylates a tyrosine residue of EC
6.3.1.2 , glutamine synthetase. The enzyme is bifunctional, and also catalyses a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC
2.7.7.89 , [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase) [7,8]. The two activities are present on separate domains.
History
EC 2.7.7.42 created 1972, modified 2016
Orthology
K00982 [glutamine synthetase] adenylyltransferase / [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase
Genes
ECOO : ECRM13514_3948(glnE)
ECOH : ECRM13516_3816(glnE)
ECW : EcE24377A_3516(glnE)
EDJ : ECDH1ME8569_2950(glnE)
ECOI : ECOPMV1_03370(glnE)
REE : electrica_00628(glnE)
RTG : NCTC13098_00882(glnE)
CLAP : NCTC11466_03964(glnE)
KIE : NCTC12125_04561(glnE)
METY : MRY16398_07260(glnE)
PSHI : SAMEA2665130_0469(glnE)
YPG : YpAngola_A0293(glnE)
YPI : YpsIP31758_0563(glnE)
SMW : SMWW4_v1c42140(glnE)
SFJ : SAMEA4384070_4253(glnE)
SOF : NCTC11214_02396(glnE)
PAQU : DMB82_0004415(glnE)
DIC : Dpoa569_000769(glnE)
PHEI : NCTC12003_03128(glnE)
PRJ : NCTC6933_03231(glnE)
LRI : NCTC12151_02787(glnE)
HIC : NTHIC486_00973(glnE)
HPIT : NCTC13334_01978(glnE)
HHZ : NCTC10839_01022(glnE)
HAEG : NCTC8502_01997(glnE)
PDAG : 4362423_00509(glnE)
ADP : NCTC12871_01556(glnE)
ALIG : NCTC10568_00333(glnE)
ASEG : NCTC10977_01737(glnE)
AVT : NCTC3438_01181(glnE)
RPNE : NCTC8284_02912(glnE_1)
PAET : NCTC13378_01174(glnE)
XFU : XFF4834R_chr05450(glnE)
XPH : XppCFBP6546_09010(glnE)
XHD : LMG31886_06400(glnE)
LLZ : LYB30171_00528(glnE)
VAU : VANGNB10_cI2202c(glnE)
VPL : SA104470976_00388(glnE)
PAEB : NCGM1900_5766(glnE)
PVD : CFBP1590__4819(glnE)
PPRC : PFLCHA0_c05190(glnE)
PMUD : NCTC8068_00468(glnE)
PFW : PF1751_v1c04350(glnE)
PPUU : PputUW4_00396(glnE)
PTRT : HU722_0003215(glnE)
PTW : TUM18999_55620(glnE)
PTAE : NCTC10697_04127(glnE)
MSHE : MAALD49_07630(glnE)
PSYC : DABAL43B_1660(glnE)
MCAT : MC25239_01113(glnE)
MCUN : NCTC10297_01182(glnE)
SCAA : TUM17387_31800(glnE)
SALH : HMF8227_02395(glnE)
LLG : 44548918_02074(glnE)
LJR : NCTC11533_00828(glnE)
LCJ : NCTC11976_01365(glnE)
LWA : SAMEA4504053_1001(glnE)
LSS : NCTC12082_02908(glnE)
LADL : NCTC12735_01202(glnE)
MISZ : MishRS11D_19570(glnE)
TIB : THMIRHAM_06190(glnE)
TSE : THMIRHAS_07170(glnE)
TZO : THMIRHAT_17920(glnE)
TWN : L2Y54_05255(glnE) L2Y54_05275(glnE)
TFRI : Thiofri_05004(glnE)
TNI : TVNIR_0502(glnE_[H])
GAI : IMCC3135_06850(glnE)
THIC : TspCOW1_20830(glnE)
ALCA : ASALC70_02802(glnE)
AEL : NCTC12917_03614(glnE)
CHJ : NCTC10426_01563(glnE)
CDIZ : CEDIAZO_00910(glnE)
NMQ : NMBM04240196_0236(glnE)
NMZ : NMBNZ0533_0233(glnE)
NMX : NMA510612_0033(glnE)
NWE : SAMEA3174300_1389(glnE)
NZO : SAMEA4504057_0536(glnE)
NCI : NCTC10296_00147(glnE)
NCZ : NCTC10294_01435(glnE)
NANI : NCTC12227_01835(glnE)
ECOR : SAMEA4412678_1174(glnE)
BMV : BMASAVP1_A0491(glnE)
BML : BMA10229_A1108(glnE)
BPM : BURPS1710b_3331(glnE)
BPL : BURPS1106A_3320(glnE)
BUE : BRPE67_ACDS03720(glnE)
PLG : NCTC10937_00690(glnE)
LMIR : NCTC12852_00951(glnE)
BUO : BRPE64_ACDS03950(glnE)
BTRM : SAMEA390648704070(glnE)
AXX : ERS451415_01942(glnE)
LIM : L103DPR2_00293(glnE)
LIH : L63ED372_03019(glnE)
URU : DSM104443_02862(glnE)
UPL : DSM104440_02561(glnE)
FPHO : SHINM1_002030(glnE)
RBS : RHODOSMS8_00539(glnE)
SMEL : SM2011_c02368(glnE)
SFD : USDA257_c07580(glnE)
SAME : SAMCFNEI73_Ch1097(glnE)
AGR : AGROH133_04917(glnE)
AVV : RvVAT039_26370(glnE)
AVF : RvVAR031_13600(glnE)
REC : RHECIAT_CH0001391(glnE)
REL : REMIM1_CH01300(glnE)
REP : IE4803_CH01338(glnE)
REI : IE4771_CH01383(glnE)
RGA : RGR602_CH01216(glnE)
RPHA : AMC79_CH01346(glnE)
NEN : NCHU2750_08610(glnE)
BIO : BR141012304_12026(glnE)
VGO : GJW-30_1_03760(glnE)
BHS : BM1374165_00458(glnE)
BTX : BM1374166_00662(glnE)
BEZ : NCTC12898_00380(glnE)
MAQU : Maq22A_c08470(glnE)
MTUN : MTUNDRAET4_0249(glnE)
FIL : BN1229_v1_2480(glnE)
FIY : BN1229_v1_3435(glnE)
BRN : D1F64_07830 D1F64_07845
BVY : NCTC9239_02494(glnE)
TSV : DSM104635_02423(glnE)
RLI : RLO149_c016390(glnE)
PHP : PhaeoP97_02000(glnE)
PPIC : PhaeoP14_01811(glnE)
SINL : DSM14862_01257(glnE)
SPSE : SULPSESMR1_01255(glnE)
RMM : ROSMUCSMR3_00421(glnE)
AHT : ANTHELSMS3_03483(glnE)
LALG : LentiSH36_01806(glnE)
LVS : LOKVESSMR4R_01671(glnE)
SPHD : HY78_04615 HY78_04620
RDI : CMV14_21320 CMV14_21325
SBIN : SBA_ch1_16330(glnE)
SFLA : SPHFLASMR4Y_01881(glnE)
PMAS : NCF86_13435(glnE) NCF86_16140(glnE)
HFL : PUV54_02590 PUV54_02885
GBN : GEOBRER4_35500(glnE)
PCA : Pcar_1363 Pcar_2171(glnE)
PEF : A7E78_11355 A7E78_14280
MBO : BQ2027_MB2245C(glnE)
MMAE : MMARE11_31950(glnE)
MBAI : MB901379_02982(glnE)
MHEK : JMUB5695_02118(glnE)
MKY : IWGMT90018_24570(glnE)
MPHL : MPHLCCUG_03358(glnE)
MTHN : 4412656_01812(glnE)
MAUU : NCTC10437_03476(glnE)
MFLV : NCTC10271_01963(glnE)
MSAL : DSM43276_01717(glnE)
MTER : 4434518_01594(glnE)
CDIP : ERS451417_01680(glnE)
CUN : Cul210932_1653(glnE)
CUQ : Cul210931_1538(glnE)
CUJ : CUL131002_1576c(glnE)
CMIN : NCTC10288_00748(glnE)
CRL : NCTC7448_00071(glnE)
CCYS : SAMEA4530656_0650(glnE)
NFR : ERS450000_02492(glnE)
NAD : NCTC11293_02615(glnE)
NWL : NWFMUON74_49770(glnE)
NSPU : IFM12276_45780(glnE)
RCR : NCTC10994_04236(glnE)
TPUL : TPB0596_17830(glnE)
TSD : MTP03_30970 MTP03_30980
SAMB : SAM23877_2322(glnE)
SLE : sle_49240(sle_49240)
SGM : GCM10017557_59740(glnE)
STUI : GCM10017668_18820(glnE)
SXT : KPP03845_102476(glnE)
SANT : QR300_01310 QR300_30725
MLV : CVS47_01459(glnE_1) CVS47_01480(glnE_2)
MSUW : GCM10025863_07730(glnE)
AMAU : DSM26151_14180(glnE)
AMAV : GCM10025877_32450(glnE)
MALK : MalAC0309_1576(glnE)
PSEV : USB125703_01706(glnE)
AAGI : NCTC2676_1_01108(glnE)
GCR : GcLGCM259_1825(glnE)
RDN : HMPREF0733_11692(glnE)
DCO : SAMEA4475696_1843(glnE)
PAK : HMPREF0675_3734(glnE)
CGRN : 4412665_00962(glnE)
PAUS : NCTC13651_00708(glnE)
NAQU : ENKNEFLB_02604(glnE)
MSAG : GCM10017556_08470(glnE)
ACTR : Asp14428_26930(glnE)
MCU : HMPREF0573_11590(glnE)
AIR : NCTC12972_00724(glnE)
ASLA : NCTC11923_02052(glnE)
AVC : NCTC10951_00631(glnE)
ACAP : MANAM107_24540(glnE)
BBV : HMPREF9228_0894(glnE)
GVG : HMPREF0421_20747(glnE)
GVA : HMPREF0424_0930(glnE)
GVH : HMPREF9231_0817(glnE)
LCRE : Pla8534_31240(glnE)
NDE : NIDE1376 NIDE1377(glnEb)
NMV : NITMOv2_1289 NITMOv2_1290(glnEb)
NIO : NITINOP_1785 NITINOP_1786(glnEb)
NJA : NSJP_2430 NSJP_2431(glnEb)
NKF : Nkreftii_000992 Nkreftii_000993
» show all
Taxonomy
Reference
Authors
Ebner E, Wolf D, Gancedo C, Elsasser S, Holzer H.
Title
ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties.
Journal
Reference
Authors
Kingdon HS, Shapiro BM, Stadtman ER.
Title
Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase.
Journal
Reference
Authors
Mecke D, Wulff K, Liess K, Holzer H.
Title
Characterization of a glutamine synthetase inactivating enzyme from Escherichia coli.
Journal
Reference
4
Authors
Mecke, D., Wulff, K. and Holzer, H.
Title
Metabolit-induzierte Inaktivierung von Glutaminsynthetase aus Escherichia coli im zellfreien System.
Journal
Biochim Biophys Acta 128:559-567 (1966)
Reference
Authors
Shapiro BM, Stadtman ER.
Title
5'-adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli.
Journal
J Biol Chem 243:3769-71 (1968)
Reference
Authors
Wolf D, Ebner E, Hinze H.
Title
Inactivation, stabilization and some properties of ATP: glutamine synthetase adenylyltransferase from Escherichia coli B.
Journal
Reference
Authors
Jaggi R, van Heeswijk WC, Westerhoff HV, Ollis DL, Vasudevan SG
Title
The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction.
Journal
Reference
Authors
Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL
Title
Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.7.7.42
ExPASy - ENZYME nomenclature database: 2.7.7.42