ID   A0A3M0CIA8_9PROT        Unreviewed;       990 AA.
AC   A0A3M0CIA8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:RMB08565.1};
GN   ORFNames=BXY39_1200 {ECO:0000313|EMBL:RMB08565.1};
OS   Eilatimonas milleporae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC   Kordiimonadaceae; Eilatimonas.
OX   NCBI_TaxID=911205 {ECO:0000313|EMBL:RMB08565.1, ECO:0000313|Proteomes:UP000271227};
RN   [1] {ECO:0000313|EMBL:RMB08565.1, ECO:0000313|Proteomes:UP000271227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25217 {ECO:0000313|EMBL:RMB08565.1,
RC   ECO:0000313|Proteomes:UP000271227};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RMB08565.1}.
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DR   EMBL; REFR01000010; RMB08565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0CIA8; -.
DR   InParanoid; A0A3M0CIA8; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000271227; 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:RMB08565.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:RMB08565.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271227};
KW   Transferase {ECO:0000313|EMBL:RMB08565.1}.
FT   DOMAIN          44..289
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          324..452
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          560..797
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          830..920
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   990 AA;  108670 MW;  CFD8045FED3C557F CRC64;
     MALSSRPHIP PHDSRKADEI WAHLQEFAGA HILPPTARAL SDTLFGNSPY LARLAQQMPE
     FACEVLRGQR PALMQAILRD MESIRPKEES RAQLAGYLRR KKAETALVLA AEDVGGTASL
     EDITHGLSAF ADAAVQLGLA HLVAERRAKG EIGTPDGTPD MVDPTYDDPS GYFILALGKH
     GGRELNYSSD IDLVALYDPA RVRYDGRKTA GDAMIRLTQD LIALLDQRTA DGYVFRVDLR
     LRPDPGATPV AISTHAAESY YQSSALNWER SAMIKARFIA GDRQAAAEYL DHLGSWIWRR
     TIDFAALADI SALKDQVHSH FGQTDKTFAG YDVKLGPGGI REIEFFAQIN QLLHGGRRPA
     LRSRETLVTL QTLVTEGLLP ETTARDLTAA YYFLRMLEHR LQMIADEQTH RLPEDRNGLD
     HVAGFAGFTD AGALESALGH HTRIVRSHFD DLMPDSANSG AEPAFSPDAL EATLRDLGFE
     DPAGSAERIA IWRRGRYRAL KTQRARELLD CCLAPLTEAL SMTAAPSAAL VRFDSWLGQL
     PSGVQIFSLF QANPNLFRLV ARIMGLAPAL AETLAKQPGL WDTVLDPEFF APIEDETVLE
     TRLSTMFERA ADYQDMLDAV RHFVGEHRFR IGVHMLEGLA DVRECGTALA RVADVALKLL
     IPRVEDSFTE KFGRIRGGGL AVLAMGKYGG RELTHTSDLD LVFLYHVPLA DPSSAAIQSD
     GPKPLGPSQY YSRLVQQVVT AITALTPAGR LFEVDTRLRP SGAQGPLVVT LKTFADYYRS
     AAWMWEHMAL TRARLILAPD SMAGPLNNTI LSVLTCQHDG PALLLAVADM RAKLAENTRA
     SQDWAVKHGR GGLVDIEFIC QYLMLRDGEN TRALFTPSIS DCLKGLAQHG ILARDTAEAL
     DKAYWLQSNI QAILRLSFGE TIPGTDSDLP PGLREILCHA TGLKTFDDLK QALSRSQGIV
     YSIFQQLITV PAGDLQTPHS DGQPTNGENT
//