ID A0A2K8KET8_9RHOB Unreviewed; 938 AA.
AC A0A2K8KET8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamine-synthetase adenylyltransferase {ECO:0000313|EMBL:ATX67942.1};
GN ORFNames=BG454_15225 {ECO:0000313|EMBL:ATX67942.1};
OS Rhodobaca barguzinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobaca.
OX NCBI_TaxID=441209 {ECO:0000313|EMBL:ATX67942.1, ECO:0000313|Proteomes:UP000228948};
RN [1] {ECO:0000313|EMBL:ATX67942.1, ECO:0000313|Proteomes:UP000228948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alga05 {ECO:0000313|Proteomes:UP000228948};
RA Kopejtka K., Tomasch J.M., Bunk B., Koblizek M.;
RT "Revised Sequence and Annotation of the Rhodobaca barguzinensis strain
RT alga05 Genome.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP024899; ATX67942.1; -; Genomic_DNA.
DR RefSeq; WP_071482271.1; NZ_SODJ01000001.1.
DR AlphaFoldDB; A0A2K8KET8; -.
DR STRING; 441209.GCA_001870665_02830; -.
DR KEGG; rbg:BG454_15225; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000228948; Chromosome.
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; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ATX67942.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000228948};
KW Transferase {ECO:0000313|EMBL:ATX67942.1}.
FT DOMAIN 43..275
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 297..438
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 527..766
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 790..917
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 938 AA; 102223 MW; 2CD73710504A5FAB CRC64;
MTFGSLTRLP LPYDAESGRS ARDSFPELSG ELSDLVAGAA GCSPYLRTLM SRERDWLADA
LGRDPAATVS DELAALDGVP LSNLSARLRQ AKRRVALLAA LADLGGVWTL DQVTGALSDL
ADRATHVALT ALVADEIARK KLPAATPEDA ATGAGMVVLA MGKMGARELN YSSDIDLICL
FDESRYSADD YHDARASFIR VTRKLCGLLS DHTDEGYVFR TDLRLRPDPS VTPVCLSMEA
AERYYESLGR TWERAAYIKA RPCAGDLAAG ARFLETLRPF VWRKHLDFAA IQDAHDMRLK
IKAHKGLGGA LALEGHDIKL GQGGIREIEF FTQTRQLIAG GRDPDLRSPR TVEGLAALAA
KGWIPHDVAE KLTAHYIEHR EIEHRLQMVQ DAQTQKLPSS PQEFDRIARF VGEAQTNAFR
SRLESRLKDV AELTEGFFAP DSGVEAEPDL SEAAQDMIAG WHSYAALRSN RAQEIFKRMR
PTILTKLHDA ADPEAALVQF DRFLSGLPAG VQLFSLFEAN PQLIDLIVDI CATSPRLAAY
LSRNAAVFDA VIGGGFFAQW PGTPELHRQL ADRLAQIDDY ERQLDAARIW AREWHFRVGV
HHLRGLIDAF EAGAEYASLA EAVLTALWPV VVADFSAKHG PPPGQGAAVL GMGSLGAGRL
NAVSDLDLIV IYDADTSETS QGRRPLDARS YYARLTKAFL TALTAPTAEG RLYEVDMRLR
PSGRQGPVAT SITAFENYQR NEAWTWEHLA LTRARRVAGS VALGDRIETL RRALLAEKST
GPTVCKDVAD MRARLAEAKP AHGIWDAKSG PGRLMDIELV AQFCALRAGH PARRVEAQLR
AGVKAGILDA AAETQLLRAY RLCWTLQATG RLLADRISDI DQLGPGGQKF ILASAGSPST
EALATRLQDC CAQAQHLIAS TLANDGPCKD KTDHDASQ
//