ID A0A0F6RBS7_9GAMM Unreviewed; 960 AA.
AC A0A0F6RBS7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=TQ33_0425 {ECO:0000313|EMBL:AKE51411.1};
OS Kangiella geojedonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC Kangiella.
OX NCBI_TaxID=914150 {ECO:0000313|EMBL:AKE51411.1, ECO:0000313|Proteomes:UP000034071};
RN [1] {ECO:0000313|EMBL:AKE51411.1, ECO:0000313|Proteomes:UP000034071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCS-5 {ECO:0000313|EMBL:AKE51411.1,
RC ECO:0000313|Proteomes:UP000034071};
RA Kim K.M.;
RT "Complete genome sequence of Kangiella geojedonensis strain YCS-5T.";
RL Submitted (FEB-2015) 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; CP010975; AKE51411.1; -; Genomic_DNA.
DR RefSeq; WP_046560605.1; NZ_CP010975.1.
DR AlphaFoldDB; A0A0F6RBS7; -.
DR STRING; 914150.TQ33_0425; -.
DR KEGG; kge:TQ33_0425; -.
DR PATRIC; fig|914150.5.peg.432; -.
DR HOGENOM; CLU_006233_0_1_6; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000034071; 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; 1.20.120.330; 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:AKE51411.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000034071};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:AKE51411.1}.
FT DOMAIN 38..277
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 298..436
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 551..803
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 834..924
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..440
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 453..960
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 960 AA; 109627 MW; 46E3C61C40C1E3DD CRC64;
MRTDFSLPAS LKELADKRYG EWRDALTSEE SFDEDKARLV LASSDYISRW AVKKPEWLLD
AINGVSIEQG LSQLQDTFDL SVSEFDMKQK LRLERHYWSI LIAVNDMFQL ADIKAITFYQ
STLADILIQA AYRWAEHHHH QQYGKPYGAS GDVQQMLILA MGKLGGRELN FSSDIDLIFA
YPEEGETDRQ SKPVENQKFF IRLGQKLISL LSDVTYDGFV YRVDMRLRPY GQSGALVTNF
NALQDYYLEQ GREWERFAMI KARVVNGSDE NKAELEQIIR PFSYRRYIDF SVLESIRQLK
QKIASELLRK NAKGNIKLGE GGIRELEFIV QSLQLIGGGR HPVLQTKNWW HSLDTLQVKE
FIPAQEAKPL KQAYEFLRKL ENAIQIRDEE QTQEVPTDTL EQRQVAAMLG LEGWGEVAES
LSDHQNHVAN FFKGLFHDPH DEDKVDEDCE RVSKWLEGSL DQNAETALQQ KLSISPAMVA
MVNQFRGEFS ERKIGSRGLV RLDQLLPHLL IEAGAQPEPE TTLQRCIELL QGVGRRTAYF
EMLAENLPVL EYLVQLVSRS RWLAKQMSIY PSLLDELLFP SNFGKQLSKA DLASQLRQAL
IRIEADDIEG QLVALGGFKQ SSQFKIAAGD LTGRFDISAV SQQLTDLAEV IVEYLLQFAW
RETVSKFGVP PGCEEGLASG FLVLGYGKLG GDELGYGSDL DLVFLYQGDS QSETSGKNHS
GEKTLELHQF YTRLAQRLVH YLGTRTQQGI MYEVDTRLRP SGRAGMLVSH IDAFKKYQHN
EAWTWEHQAL VRARPIAGDY PLREEYMALR SEILAKPSSP QSESNDLASD VVAMRQKMRD
NLNKSDSKLW DIKQGEGGLV DIEFLVQYWA LSHSAILMEH LSNQELPFNN VDWLQLLAKH
GLISQEVRDQ LIMNYRAFRE VGNHSSLQSQ PQLIPIDELT QERQQVSELW HSTFENVEVQ
//
