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Database: UniProt
Entry: A0A395JGS8_9GAMM
LinkDB: A0A395JGS8_9GAMM
Original site: A0A395JGS8_9GAMM 
ID   A0A395JGS8_9GAMM        Unreviewed;       915 AA.
AC   A0A395JGS8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:RBP49116.1};
GN   ORFNames=DFR28_10442 {ECO:0000313|EMBL:RBP49116.1};
OS   Arenicella xantha.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Arenicellales;
OC   Arenicellaceae; Arenicella.
OX   NCBI_TaxID=644221 {ECO:0000313|EMBL:RBP49116.1, ECO:0000313|Proteomes:UP000253083};
RN   [1] {ECO:0000313|EMBL:RBP49116.1, ECO:0000313|Proteomes:UP000253083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24032 {ECO:0000313|EMBL:RBP49116.1,
RC   ECO:0000313|Proteomes:UP000253083};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-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:RBP49116.1}.
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DR   EMBL; QNRT01000004; RBP49116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395JGS8; -.
DR   InParanoid; A0A395JGS8; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000253083; 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; 1.
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   Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:RBP49116.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:RBP49116.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253083};
KW   Transferase {ECO:0000313|EMBL:RBP49116.1}.
FT   DOMAIN          38..246
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          291..418
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          557..738
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   COILED          730..757
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   915 AA;  104429 MW;  7C16ACBC9BC0D9BC CRC64;
     MTDADSLILA SPYLNRLQSR VSVDVSATQD GLIAGLKQIR ERLNTLSQDD PDVSEQVLLQ
     AKIDYSFLWA NLELQQFGTA AQRGKLWTEF ADCTIEFALR LAWQIVARKE KSVAAKVVEY
     EGRVPGLVVL GMGKLGGCDL NVSSDVDLVA YFDPDVLPVP DVVGKSYVCH RVLQALTRLL
     SQNEQTDFVW RVDWRLRPNA SATTLAMSTK AARDYYFYRA SPWHRLALMK ARVVAGDRTL
     GSRFLAELSP FIWRQNLDYR ALDELAEIKQ RINLEHPGLR TQRQWREPIG EEIAGFNVKL
     GSGGIREVEF VANALQLVWG GRMHSLRQPN TVKALSALAD EQRLDRNDAN NLIESYQTLR
     RIENAIQLLG NQQSHQIPSE PVRQQQLLTL LGIAEWNQLV SQINPARRWV NDYFSELFAE
     QSSSHQEPII WPEGLSAQAD EIVEAWENGY YLYGVSNQVR HRLVPLTRGI ASFLNENSEP
     NNQTASEIIV RLHDFFRSLP SGEQYFRLLA ESPALLRSIV PPLLYSPPMV SLLRQSPHII
     DCYVQEDWRY PDPFDGDYVL QAEGYEEQLE RMRRFVNEYL YQLYLSFLQG AITVPDFQEA
     LTRLAEQSIE LAVQSVTQNM GLTESPVSII GMGKVAMRRM SPMSDLDLIF VFDQSAADID
     SASRFVSRLQ TAISTPMREG ILYELDTRLR PSGRSGAPTV SIESFANHHR QRAHTWEHIA
     LVPSRVVVGN HQAEKRIENI KLEMINAERS HDQLLRDALK MWTRIADHRI GDTPMQNLNS
     KLRTGGLMQA EYLASCMILI NGHDKQFTNG SFDAMLAECL TESGLEELPE VLQFWRIQQL
     WERLLGKTDQ PLSSLRDVYF SRLLEHSEVG SMDELLAKKK RYSELIESSL NDLFAGLKMT
     RKEIDDWHEQ QVIWK
//
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