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Database: UniProt
Entry: A0A0W1GS71_9SPHN
LinkDB: A0A0W1GS71_9SPHN
Original site: A0A0W1GS71_9SPHN 
ID   A0A0W1GS71_9SPHN        Unreviewed;       902 AA.
AC   A0A0W1GS71;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Glutamine-synthetase adenylyltransferase {ECO:0000313|EMBL:KTE57665.1};
GN   ORFNames=ATE69_02345 {ECO:0000313|EMBL:KTE57665.1};
OS   Sphingopyxis sp. H071.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759078 {ECO:0000313|EMBL:KTE57665.1, ECO:0000313|Proteomes:UP000054127};
RN   [1] {ECO:0000313|EMBL:KTE57665.1, ECO:0000313|Proteomes:UP000054127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H071 {ECO:0000313|EMBL:KTE57665.1,
RC   ECO:0000313|Proteomes:UP000054127};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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:KTE57665.1}.
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DR   EMBL; LNSF01000001; KTE57665.1; -; Genomic_DNA.
DR   RefSeq; WP_058455638.1; NZ_LNSF01000001.1.
DR   AlphaFoldDB; A0A0W1GS71; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000054127; 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   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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:KTE57665.1}; Transferase {ECO:0000313|EMBL:KTE57665.1}.
FT   DOMAIN          44..238
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          269..398
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          508..747
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
SQ   SEQUENCE   902 AA;  96962 MW;  B76BB9317301C560 CRC64;
     MIASDASARR SALDRLTANA PFLARLAELN PDDVARFLGE GADAALAEVA PPPVDDDIMR
     TLRQWRGRMA LLLALGDLSG EHDVGLTTRL LSDFADTACD IALAAAFAER VPGEEPRGIA
     VIALGKLGSH ELNYSSDIDP ILIFDPETMP RRSRDDPGEA AVRIARRMVE ILSARTADGH
     VLRVDLRLRP HPEVTPIVLP ESAAISYYES EALAWEQAAF IRSRASAGDR ALGNRFLAAI
     QPFIWRRSLD FRQLKEIGAM SDRIRDHFSQ GQAFGPGYDL KRGRGGIREI EFFAQVHQLI
     YGGRDPSLRL PATVDALAAL AKAGRVDADV AERLTGHYAL LRRIEHRLQM IEDQQTQCLP
     VQPAALDGVA RLDGEADGAA LLATLQPVVT DVGACYDRLV AERAATSGLP RDEGELAGAV
     MAAGFDPPDA ALRTISEWRG GKLRALRSAA ALEALETALP ELVKALGAAP DPDAALLRFD
     KLVGGLPSAI GFFHLLAAQP ALAKIATRIL WLAPALADAL GARVELIEGL IDKRAFEAPA
     TKAELLAEWA PGLAGLDYER LLDRVRDRVG ERRFAYGVQI IAGSTDPLAI ACGYSELAEA
     ALQVLADATV TEFVAAHGRV PDSELVVLAL GRLGGRALTH ASDLDLIYLF TGDHLAESDG
     PRPLGATTYY NRLAQRVSGA MSVPTAAGKL YDVDTRLRPQ GAQGPLVVTL DSFERYQREE
     AWTWEHMALL RARPVYGSDR AKAAVQRTID ELLAAPRDRA TVAQDAAEMR DKIAAHKPPK
     GPLDIKGGPG GLVDLEFAMQ VTQLATGRCH DPNIGSALAC LRVDGLAPPE ICDAHGLLAR
     MLVMLRLTAP EGEPATAAAR QLVASACGEP GWPQLLAAHD AARQEIADWW ASIRPPQQET
     KP
//
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