ID   A0A1C4WTR3_9ACTN        Unreviewed;      1006 AA.
AC   A0A1C4WTR3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:SCE99554.1};
GN   ORFNames=GA0070612_2826 {ECO:0000313|EMBL:SCE99554.1};
OS   Micromonospora chokoriensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=356851 {ECO:0000313|EMBL:SCE99554.1, ECO:0000313|Proteomes:UP000198224};
RN   [1] {ECO:0000313|EMBL:SCE99554.1, ECO:0000313|Proteomes:UP000198224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45160 {ECO:0000313|EMBL:SCE99554.1,
RC   ECO:0000313|Proteomes:UP000198224};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT607409; SCE99554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4WTR3; -.
DR   eggNOG; COG1391; Bacteria.
DR   Proteomes; UP000198224; Chromosome i.
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; 3.
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:SCE99554.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:SCE99554.1}; Transferase {ECO:0000313|EMBL:SCE99554.1}.
FT   DOMAIN          103..313
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          351..483
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          589..667
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          688..842
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          865..1000
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1006 AA;  108116 MW;  3B981C410A91C429 CRC64;
     MSRPTRAPGR LARYGFGTAE GDGGARAADL LGPDGLRLWR PEEQEPTDEP AGELLAALSR
     AADPDLALRQ LHRIVEAERR ATEGSAESPL IAELHADPGL RRRLIAVLGA SSALGDHLVA
     NPEHCLTLRT APDGLAPIAE GRLEPTDGGN PTAALRSAYR LALLRIAAAD LTGGRGLEQT
     MAALSALADA TLAAAYEIAV TELADGTERP RLAVVAMGKC GGGELNYVSD VDVIFVAAED
     ADLPAATLVA TRLISICGMV AWPVDAALRP EGNRGPLVRT LASHLAYYRR WARTWEFQAL
     LKARPAAGDL PLAQEWIDQL APLVWRAAER PEAVEDVRSM RRRIIDNIPP KELEREIKRG
     PGGLRDIEFA VQLLQLVHGR GDETLREPGT IPALRALVAG GYVGRADGEA LLRGYRFLRS
     VEHRLQLQGL RRTHTVPTEP GALRWLAAAL GFTAAPGRSA VESFRAEWVT HATEVRRLHA
     KLLYRPLLES VARVPADGLR LTPEAARHRL EILGFADPAG ALRHLQALTG GVSRTAAIQR
     TLLPVLLSEF ADAPEPDRGL LNYRKVSDKL GSTPWYLRLL RDGGPVARRL ARVLSLSRYV
     ADLLARDPEA LRLLAEENEL APRSREVLRE GFLAAAARHT DPVEATSAVR ALRRRELVRV
     ACADVLCRAG SLAPSPTRPD GTSRPAPGLS DITQVGTALA DVTDATLAAA LRAAQASQPA
     PEGLRFAVIG MGRLGGYESN YLSDADVLFV YDPPAGVGDS AASAAAHAIA EELRRLLGVP
     APDPPLGVDA DLRPEGRQGP LVRSLAAYAA YYARWSRVWE SQALLRARFV CGDAGLGAEF
     EAMIDPVRYP AEGLTREQVV EIRRIKARVE NERLPRGADP ATNTKLGRGA LADVEWAVQL
     VQLRHAGANP ALRGTRTLDA LAAAERAGLI DPADAAEMAA GWSLAAQVRN ALMLVRGRAG
     DQLPRHGVEL AGVVRLLGRD DPGEFLDEYL RVGRRSRAAT ERVLNA
//