ID   V9VQY1_9RHOB            Unreviewed;       934 AA.
AC   V9VQY1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Glutamate-ammonia ligase adenylyltransferase {ECO:0000313|EMBL:AHD01161.1};
GN   ORFNames=METH_11115 {ECO:0000313|EMBL:AHD01161.1};
OS   Leisingera methylohalidivorans DSM 14336.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Leisingera.
OX   NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD01161.1, ECO:0000313|Proteomes:UP000018780};
RN   [1] {ECO:0000313|EMBL:AHD01161.1, ECO:0000313|Proteomes:UP000018780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD01161.1,
RC   ECO:0000313|Proteomes:UP000018780};
RG   DOE Joint Genome Institute;
RA   Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP006773; AHD01161.1; -; Genomic_DNA.
DR   RefSeq; WP_024090465.1; NC_023135.1.
DR   AlphaFoldDB; V9VQY1; -.
DR   STRING; 999552.METH_11115; -.
DR   KEGG; lmd:METH_11115; -.
DR   PATRIC; fig|999552.6.peg.2218; -.
DR   HOGENOM; CLU_006233_0_0_5; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000018780; Chromosome.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000313|EMBL:AHD01161.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:AHD01161.1}; Transferase {ECO:0000313|EMBL:AHD01161.1}.
FT   DOMAIN          32..274
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          297..437
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          528..770
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          807..922
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   934 AA;  101106 MW;  A444B8F243965A3E CRC64;
     MTTALNITRM PRPFDPDLGA ETRALVPELT GAMADLVAGA CGSSPYLMEL TAREAAWLPQ
     ALQDPETALA AVFADCRALE GNGLKPGLRQ AKRRLALLTA LCDLSGGWSL EQVTGALTDF
     GALCADVAIK SEIAALIRRR KLPGLTEDDV ETAGGLTILA MGKMGAHELN YSSDIDLICL
     FDETRFDPDD FYEARQGMVR ATKNMCAALS DRTGDGYVFR TDLRLRPDPA VTPVCLAMEA
     AERYYESLGR TWERAAYIKA RPCAGDIAAG ERFLTTLRPF IWRRHLDFAA IQDAHDIRLR
     IRENKGTGGA LHVPGHDMKL GRGGIREIEF FTQTRQLIAG GRDESLRLRG TVEGLAALAD
     KGWVPPGTAE ILSAHYRAHR EVEHRIQMVH DAQTHQMPKS EDGIARIASL MDRDPAELTA
     EIRDRLTEVH ELTEGFFSPG GTPGAPAAAE NTAELDGAII ARWPTYPALR SSRGARIFER
     LKPELLSRVA KTAKPAETLV ALDGFLSGLP AGVQLFSLFG ANPQLIDLLV DIAGTSRELA
     SFLSRNSGVF DAVIGGSFFD PWPGAEQLRA ELKNRLVQED DYEARLDATR RWCKEWHFRI
     GVHHLRGLID GHQAGVQYAE LAEVVIAGIA PDVVAQFSRK HGPPPGRGAA VLAMGSLGAG
     QINSQSDLDM IVIYDPGGAD MSEGKRPLAT RPYYARLTQA LVTALSAPMA QGKLYEVDMR
     LRPSGNQGPV AVSLAGFTSY QQNEAWVWEH LALTRARVVA GDAALAAEIE TFRAGFLAEP
     RDLAMVLQQV AQMRARLAAA KTPAGVWDAK NGAGRMMDIE LLSQAGALTS VSVARDVASG
     LLGAVAAGWL NDADAEYLTA SYRLFWSVQS AARLLSGKAI EAGTIGEGGA QFLCRTTGYA
     RLDALEQELL ARYERCAALI AEALEREQAD EGQH
//