ID   A0A1G6U761_9ACTN        Unreviewed;       871 AA.
AC   A0A1G6U761;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:SDD37123.1};
GN   ORFNames=SAMN05216270_103354 {ECO:0000313|EMBL:SDD37123.1};
OS   Glycomyces harbinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Glycomyces.
OX   NCBI_TaxID=58114 {ECO:0000313|EMBL:SDD37123.1, ECO:0000313|Proteomes:UP000198949};
RN   [1] {ECO:0000313|EMBL:SDD37123.1, ECO:0000313|Proteomes:UP000198949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3516 {ECO:0000313|EMBL:SDD37123.1,
RC   ECO:0000313|Proteomes:UP000198949};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNAD01000003; SDD37123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6U761; -.
DR   STRING; 58114.SAMN05216270_103354; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000198949; Unassembled WGS sequence.
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; 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   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:SDD37123.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:SDD37123.1}; Transferase {ECO:0000313|EMBL:SDD37123.1}.
FT   DOMAIN          62..211
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          235..374
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          480..702
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          747..858
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   871 AA;  94972 MW;  C7B5E798931D287F CRC64;
     MADEVESADA DRARLAVVAA SNALGDFLRA HPEFEPALTE DEDAGHARVR EASPFELNAA
     WKANLLRIAA ADLTGATDLK DTSAALSRLA DAVLVRGLEL ARADCPGETR LAVIAMGKTG
     AEELNYVSDV DVVFVAEGNL DLATRQAARM IQILGPATWP VDAGLRPEGR HGALVRTIES
     YEAYLKDWAR TWEFQALLKA RPAAGDLQLG LDWLASVQPF IWGAADRPGV VADIRDMRRK
     VAESVPAAER RFEIKLGPGG LRDIEFAVQL LQLVHGRGDA ALRVRSTLEA LDVLVAGGYL
     ARRDGEDLAD TYVFLRTVEH RVQLQRLLRT HRVPDGGEPL HHLARTLGYT TDEGFLAAWR
     AHATTARRLH EKLLYKPLLD AVTRVPTNEL RLTETEAASR LAVLGFADPA SALTHMKKLT
     EGVSRTATVQ RALLPVVLHE LADSPEPDRG LLAYRQVSDK LGSTPWYLRL LRDGGPAAVR
     LARLLGTSRY FTSLLLHVPQ SLRYLSDNAD LKPRPRETLA MGMLQAAARH GEATAAIGAV
     RAIRRRELIR IAAADLLELL DDQGVGLALS DLTDAVLQAA LDIASRGIAD APPISVIGMG
     RLGGRETGFG SDADVVFLHA GETDAERTAA RKIVEAVRTL LGAPTADPPL VLDLDLRPEG
     KGGAIAPSLA AYRRYYADRA RLWERQALLR ARPVAGDAAL SEAWRMIADE VRYRPGGLSE
     PERVEFRRVK ARVDSERLPR GADPNGHTKL GRGGLVDIEW AAQLLQLEHG EDASLHTTRT
     VPALAAATAA GYLDRADFEA LRDAWEFVSR VRNDMTLARG VPRDDLPRSG PELAALAQTL
     GFGEDTERFL NQYRRLTRLA HDAAHRIVYG D
//