ID W0QBM4_9PAST Unreviewed; 963 AA.
AC W0QBM4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=X808_14340 {ECO:0000313|EMBL:AHG75956.1};
OS Mannheimia varigena USDA-ARS-USMARC-1296.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=1433287 {ECO:0000313|EMBL:AHG75956.1, ECO:0000313|Proteomes:UP000066995};
RN [1] {ECO:0000313|EMBL:AHG75956.1, ECO:0000313|Proteomes:UP000066995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-1296 {ECO:0000313|EMBL:AHG75956.1,
RC ECO:0000313|Proteomes:UP000066995};
RA Harhay G.P., Clawson M.L., Murray R.W., Lubbers B.V., Heaton M.P.,
RA Chitko-Mckown C.G., Harhay D.M., Smith T.P.L.;
RT "Annotation of the Mannheimia varigena USDA-ARS-USMARC-1296 complete
RT genome.";
RL Submitted (DEC-2013) 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; CP006943; AHG75956.1; -; Genomic_DNA.
DR RefSeq; WP_025217659.1; NZ_CP006943.1.
DR AlphaFoldDB; W0QBM4; -.
DR STRING; 1433287.X808_14340; -.
DR KEGG; mvi:X808_14340; -.
DR PATRIC; fig|1433287.3.peg.1435; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_6; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000066995; 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:AHG75956.1};
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:AHG75956.1}.
FT DOMAIN 25..267
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 292..448
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 573..824
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 845..939
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..453
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 466..963
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 963 AA; 111483 MW; DA7F8D44A51C4D05 CRC64;
MLTTLISQSQ FTLPADLQNS EQIQPLVVAM AMSNLVTQTL QKQPDLFAEW KNNLPTTNEC
GNYLSRLNEL LVTVENEEQL SRELRLFRHR ELSRLSFLQS NKLATVEFVF QRLSDLAESL
ILAARDWLFK RCCEEYGTPM NSLGEQQELL ILGMGKLGGG ELNFSSDIDL IFTYPDTGET
EGGRKPIENS KFFIRLGQRL IKALDDITAD GFVYRTDMRL RPFGDSGALV FSFAAMEDYY
QEQGRDWERY AMIKAKILGE ESQNINHRYL KQMLRPFVYR RYLDFSAIQS LREMKQKISR
EVVRRNLTDN IKLGAGGIRE VEFIVQTFQM IRGGRDKILQ ERSLLKVLPR LSDLNLLTQA
QVEKLHNAYI FYRQVENVLQ AIDDKQTQTL PTDPEDQARL IFACQCYWQQ ELNSETVIFI
EHQFNDWAGF LAVLNGYQNE VRHIFNELIG EEESEDEASP LNEKLAEWKD ILNYTISLED
LSAVLKNYPQ VAESDYETIF HHFSTTFQDW VKRPIGVRGR EVLRNLMPKI ADSIFEREDY
LLLLPRLLNI VDKITTRTTY LELMVEREQI LPQLLTLCSK SVMIAEQIAR YPMLLDELMR
YNGLTEVLEL GQYQSALQDY LIRIPEEDEE TLIDGLRQFK QTQILRIAAS DILGVLPVMK
ISDHLTYLAE AIINAVVHMA WKQVSQRFGT PEHLESDEKG FAVIGYGKLG GIELGYNSDL
DLVFLHNAPE NSQTIGGKKE ISSHQFYLKL AQKINSIFNL NTSAGVLYEV DMRLRPSGEA
GLLVSTFNAY EHYQKNEAWT WETQALVRAR CVFGAEHLRQ EFERIRQSTL ALPRTSSQLR
QEICEMREKM YQHLSSHSQD QFNIKTDQGG ITDIEFIAQY LVLAHSNENP QMAVWSDNVR
IFDSAVECGI LSLPESEQLK HCYTSLRNKI HHLNLLRKES MVEATEFVKE REFVRRMWQS
LLN
//
