ID   A0A1X6WT97_9MICO        Unreviewed;      1028 AA.
AC   A0A1X6WT97;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:SLM88219.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:SLM88219.1};
GN   ORFNames=FM110_01370 {ECO:0000313|EMBL:SLM88219.1};
OS   Brachybacterium nesterenkovii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=47847 {ECO:0000313|EMBL:SLM88219.1, ECO:0000313|Proteomes:UP000195981};
RN   [1] {ECO:0000313|EMBL:SLM88219.1, ECO:0000313|Proteomes:UP000195981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP104813 {ECO:0000313|EMBL:SLM88219.1,
RC   ECO:0000313|Proteomes:UP000195981};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FWFG01000013; SLM88219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6WT97; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000195981; Unassembled WGS sequence.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-EC.
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:SLM88219.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:SLM88219.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195981};
KW   Transferase {ECO:0000313|EMBL:SLM88219.1}.
FT   DOMAIN          85..334
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          357..492
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          598..853
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          878..1015
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   REGION          708..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1028 AA;  112262 MW;  EE6576BB837AB379 CRC64;
     MSVEISTGSL ARLGFGRTDR AQRFLADPAL DGLDRAGVEA IGRTADPDEA LIGLLRWAES
     ARQADEAGAA RLLAEVGEEG TAGSRLVTLL GASVALGDFL TRHPDRIVAL EGEADGLDAA
     TAEVRRRLLR AVGADPDAEI PVAAGDGRSG RDALRIAYHE RLVQIAVADL AAPDPTAVQP
     AVSEALADLA DAALDAALAV ARTSVDGHED VRLAVLAMGK TGARELNYIS DVDVIHVAEP
     RPGADGGSVD EEALIATASS LARELARVCS DRTAEGSLWQ VDANLRPEGK DGPLARTLDS
     CRRYYRTWAA SWEFQALLKA RPAAGDRDLG EAFVEMVAPH VWQAAARDGF VEDSRAMRRR
     VIDHIPRGEV ERNLKLGPGG LRDVEFTVQM LQMVHGRGDE SLRVRGTLPA LERLRDGGYI
     GRDHAAELDA SYRFLRAVEH RLQLHRMRRT HVLPTSEGDL RRLARALGLL PDEFPARYEK
     VRRRVRRLHE EIYYRPLLDT ASTLSEDQVR LTPEAAAERL AAIGYRDPKR ALAHIDALTE
     GISRRAAIQR QLLPSLLEWF ADGVDPDLGL LAFRRLSDAV GSAHWYMGLL RDSGVAAQRL
     TRVLSDSRYA GEQLEQIPEA VRWLARDEEL RPLGREALIG EFAAVIRRVD TAEEATEVLR
     RTRRRELLRI AMAHLVHLVR PEEVAAALTD LAEAVLEAGV QVAAHVVATE DGPERPSEQP
     QTTGEDADED QSALERLGID LGVLAMGSFG AAEMGYSSDA DVQFVVADAG AGEATTSVAV
     KVATTLQRIL NAPSSGADMK VSADLRPEGR NGVLVRTIES WSGHYDRSAE TWERQALLRA
     RPIFGSAALR EAMRETMDRH RYPDGGLTAQ QRRDIVRMKA RVESERLPRG TDPSRHLKLG
     RGSMTDVEWT VQLLTMDSAS AHPALRGRTG TLDLLDALVD ADVLPRRSAE DLAAAWRLAW
     ELRGALFLWR GRESAILPLD RIELRAAAQV VLGPDATARQ VEEEYLRVTR HARGIVEAVF
     FGEPGPGA
//