ID I1XEQ8_METNJ Unreviewed; 947 AA.
AC I1XEQ8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 OrderedLocusNames=Q7A_16 {ECO:0000313|EMBL:AFI82877.1};
GN ORFNames=CDW43_00080 {ECO:0000313|EMBL:AUZ85931.1};
OS Methylophaga nitratireducenticrescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI82877.1, ECO:0000313|Proteomes:UP000009144};
RN [1] {ECO:0000313|EMBL:AFI82877.1, ECO:0000313|Proteomes:UP000009144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI82877.1,
RC ECO:0000313|Proteomes:UP000009144};
RX PubMed=22815445; DOI=10.1128/JB.00726-12;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT sp. strain JAM7.";
RL J. Bacteriol. 194:4126-4127(2012).
RN [2] {ECO:0000313|EMBL:AFI82877.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI82877.1};
RX PubMed=23148104; DOI=10.1099/ijs.0.044545-0;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Methylophaga nitratireducenticrescens sp. nov. and Methylophaga frappieri
RT sp. nov., isolated from the biofilm of the methanol-fed denitrification
RT system treating the seawater at the Montreal Biodome.";
RL Int. J. Syst. Evol. Microbiol. 63:2216-2222(2013).
RN [3] {ECO:0000313|EMBL:AFI82877.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI82877.1};
RA Villeneuve C., Villemur R.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AUZ85931.1, ECO:0000313|Proteomes:UP000238402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP59 {ECO:0000313|EMBL:AUZ85931.1,
RC ECO:0000313|Proteomes:UP000238402};
RA Villemur R.;
RT "The sequence of the genome of Methylophaga nitratireducenticrescens GP59
RT and its two plasmids.";
RL Submitted (JUN-2017) 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; CP003390; AFI82877.1; -; Genomic_DNA.
DR EMBL; CP021973; AUZ85931.1; -; Genomic_DNA.
DR AlphaFoldDB; I1XEQ8; -.
DR STRING; 754476.Q7A_16; -.
DR KEGG; mej:Q7A_16; -.
DR PATRIC; fig|754476.3.peg.15; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_6; -.
DR Proteomes; UP000009144; Chromosome.
DR Proteomes; UP000238402; 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: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};
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:AFI82877.1}.
FT DOMAIN 40..282
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 305..443
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 554..807
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 825..912
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 1..447
FT /note="Adenylyl removase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT REGION 457..947
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
SQ SEQUENCE 947 AA; 107604 MW; 858AF83D8BD3866B CRC64;
MIVHFEMANE AKMTISPPLL TEQWLSILQD KQYLLDAAPE VLTASEYVLN QGDRQPQRLR
ELVESGDLEI VYAEDGYQQR LQTRLAKVND EATLHQQLRI FRHREMVRII WRDLSGWADL
TETVRELTAL ADCCVRQALN KLYHWQTELL GTPTNNAGDP QHLIVLGMGK MGAGELNLSS
DIDLIFTYPD EGETQGARKS LTNEEFFTRL GRKLIQALDN VTVDGFVFRV DMRLRPFGDS
GSLVASFDAM EDYYQTQGRE WERYAMIKAR PVTGSEQDKK AVNELLRPFV YRRYLDYGMF
DSLREMKSMI ARQLHLKGME NNIKLGAGGI REIEFIGQVF QLIYGGRDRP LQQRPILTIL
DLLAERKLLS GYAVTALKNA YIFLRRTEHR IQAWADQQTH LLPKDNVAQM RLARSMGFGS
WDEFATTLNE HRQQVHEHFA QLLTAPQADN EATETIALLT SSEEEIFAYL KKWGYHEPEQ
SQQTIEKLLN LHVVKNLSHT GLGRLKKLLP LLVQAAAGTD DPDTCLNRMI PLLESIMRRS
AYMSLLVENT LALSQLVKLC AASPLISHQL ARYPVLLDEL LDPRSLYEVP GREQQKALLN
QFLSVAEDTD LEQQMNLLRE FRQIATLHVA AADVTEVLPL MRVGDQLSEL AEILLERVLL
LAWQHLIVRH GLPPAADKDD MLECGFSVIA YGKLGGLELG YGSDLDLVFV FNDALKGMTD
GNKPVDLMVF YTRLAQRMIH LLNTVTSGGV LYEVDMRLRP RGNSGLLVSP ISGFADYQQS
EAWTWEHQAL VRARCVAGDK KLAGQFSHIR QQVLCKSRTE SELAKEVSEM RHKMRQQLDK
SSVGKFDLKQ GVGGITDIEF MVQYAVLAWS ANLPDLMVYT DNIRILDALV ATGKLSEQEG
TMLADAYRYY RSEANHCVLQ EQPAVVPEAK VVDFQQQVNA IWQRWLG
//
