ID A0A0P7VE44_9SPHN Unreviewed; 914 AA.
AC A0A0P7VE44;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glutamate-ammonia-ligase adenylyltransferase GlnE {ECO:0000313|EMBL:KPP84440.1};
GN Name=glnE {ECO:0000313|EMBL:KPP84440.1};
GN ORFNames=HLUCCO15_13910 {ECO:0000313|EMBL:KPP84440.1};
OS Erythrobacteraceae bacterium HL-111.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae.
OX NCBI_TaxID=1666908 {ECO:0000313|EMBL:KPP84440.1, ECO:0000313|Proteomes:UP000050295};
RN [1] {ECO:0000313|EMBL:KPP84440.1, ECO:0000313|Proteomes:UP000050295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-111 {ECO:0000313|EMBL:KPP84440.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPP84440.1}.
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DR EMBL; LJSW01000050; KPP84440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7VE44; -.
DR PATRIC; fig|1666908.3.peg.2703; -.
DR Proteomes; UP000050295; 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; 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; 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 Ligase {ECO:0000313|EMBL:KPP84440.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:KPP84440.1}; Transferase {ECO:0000313|EMBL:KPP84440.1}.
FT DOMAIN 20..236
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 274..390
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 507..748
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT REGION 407..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 97994 MW; 0D1D0439BC7F918D CRC64;
MADRPDWTGA LERARAHAPF LERALDRQGE LAELLAAGAG EAALEWAKAR GREGAIESAL
RRERLGLAAA LAIGDLAGAF PLARVVRELT GFADRALDRA IRAAVRERTG KETAAGFVAL
ALGKQGAGEL NYSSDIDPIL LFDPARLPRR ERDDPGEAAQ RYARRIVRLL SETTAEGYVV
RVDLRLRPAS EISPPAVPIA SALAHYQGQA LAWERAAFVR ARPAAGDIAL GEEFLAATRP
FVWRRHLDFG AIAEIRRLTK RIREDHDGPP RPGPGFDVKR GRGGIREIEF YAQTLQLIHG
GRDPSLRVRG TREALDALAA AGHVGAGDAR TLGDGYDRLR VIEHRLQMVH DRQTHSLPES
AAALDAVAQL DGLADGAALV AELGELTART GAIYDALIRE DAPAAPAVPA RAPAPSPVPS
ASAAPERSAR AAALAERMAG WRDGRYQSLR SPQALAAFDA IAPVLAEAFL DADDPERALV
RWESVLDRAS SAINLFHLLK ARPGLLDRLI SALTLAPTLA DELARRPELL DILLDREARA
LPHAVEAIMG RIMAAAARED YEALLDAIRV VTGEVRFALG VELVEGRADP LAVAASLSRT
AEAALRLAHE GAAAEFARAH GRMAGGELLV LGLGRLGGGA LTHASDLDIV YLFTGDFAAR
SDGPRPLGAT HYFNRLASRV SAALSVPTAE GALYEIDTRL RPQGAQGPLA VSCDAFAKYQ
REAAWTWEHM ALARARVLAG SDAARKQVEA LIEDVLFRPR DPGDLRESVL EMRDAMARHK
QPGGTLDVKL LRGGLVDFEF LVHYLQLRGG RALAEAHPLA FSADLGRAIP ALVGAGLLPQ
GFREDYDLMT RLLVAGRLLA PGGSEPPPLA ARALAQACRQ EDYAGLLRAL GEARQRVAAT
WRAILGQDIL STPS
//