ID   A0A1I7DAC2_9MICC        Unreviewed;      1003 AA.
AC   A0A1I7DAC2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:SFU08631.1};
GN   ORFNames=SAMN04487915_11097 {ECO:0000313|EMBL:SFU08631.1};
OS   Arthrobacter sp. ov118.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1761747 {ECO:0000313|EMBL:SFU08631.1, ECO:0000313|Proteomes:UP000199457};
RN   [1] {ECO:0000313|EMBL:SFU08631.1, ECO:0000313|Proteomes:UP000199457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV118 {ECO:0000313|EMBL:SFU08631.1,
RC   ECO:0000313|Proteomes:UP000199457};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FPAY01000010; SFU08631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7DAC2; -.
DR   SMR; A0A1I7DAC2; -.
DR   STRING; 1761747.SAMN04487915_11097; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000199457; 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; 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:SFU08631.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:SFU08631.1}; Transferase {ECO:0000313|EMBL:SFU08631.1}.
FT   DOMAIN          75..326
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          347..492
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          597..835
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          860..1000
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   1003 AA;  109519 MW;  EB94A93A0EF36FE0 CRC64;
     MSLARRLIAA GFSDLDKGER FLAARELEGL DQDALFAGLQ LAANPDTALQ SLVRLIEKHP
     ALRTLAVADP ETSEPLYRVL GASEALGEFL IRHPEHLDAF DVRASPEPLA ADAVALRARL
     LQSVRADPKS VRPVAGLSGQ EAYAALRTAY RRGLVELAIK DLCAADPLDF MPAAGAELAD
     LAGAALEAAL AVSRAETAEK FDAAEVADVG LAVIGMGKCG ARELNYISDV DVIYVIDSGT
     LEDATATTIG TALASGISRA IMSTCREPGL WEVDANLRPE GKSGPLVRTL ASHESYYARW
     AESWEFQALL KARTIAGDTD LGTRYEAAVT PLIWSSAGRE GFVESVRAMR RRVTEHIPAD
     EEQRQIKLGR GGLRDVEFTV QLLQLVHGKS DESLRCRDTT SAIAALSAGG YIGRSDAAEF
     DRDYRYLRLL EHRIQLFQLR RTHLMPETEA SLRSLAKAVL GPFSAERPKP DALMAAWRKT
     KRSVRELHER IFYRPLLNTV ATLSSEEARL TPEAAQGRLA ALGYLDPPGA MRHIEALTAG
     VSRRAALQRQ LLPILLDWLA DGVDPDAGLL AFRRVSEALG TTHWYLGMLR DSTAAAERLC
     HVLANSRLIA DLLEVSPESV AWLGADKELV PLPLETQWLE ITSKMSRHAD PESAMRLIRL
     IRRREILRIA IADSAGLLDQ DQVGGALADT DQAAVLGALR VAETMIAAEQ PLKTHVLVVA
     MGRQGGREIG YGSDADVIYV HRGLPGVPEE EAQAQAAQIV GKLSSLLTQP LKPAILAERV
     LSVDADLRPE GKNGPMVRSL ESFAEYYRRW SLVWEAQALL RARPMAGDDA LAADFMALIN
     PIRYPESLSQ QDTREVRRIK ARVEAERLPR GADPARHLKL GRGGLSDVEW LAQLLQLQHA
     GEHPELRTTS TVEALGAAAA LGLLDEGDAE ILLGAWRLAS RIRSANVIWT GRSSDLLPSS
     RRDLEAVARW CGYGQGNAAA LEEDYLRLSR RARSVFERVF YGQ
//