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Database: UniProt
Entry: A0A2T6BIL0_9RHOB
LinkDB: A0A2T6BIL0_9RHOB
Original site: A0A2T6BIL0_9RHOB 
ID   A0A2T6BIL0_9RHOB        Unreviewed;       924 AA.
AC   A0A2T6BIL0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:PTX55895.1};
GN   ORFNames=C8N43_0543 {ECO:0000313|EMBL:PTX55895.1};
OS   Litoreibacter ponti.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Litoreibacter.
OX   NCBI_TaxID=1510457 {ECO:0000313|EMBL:PTX55895.1, ECO:0000313|Proteomes:UP000243978};
RN   [1] {ECO:0000313|EMBL:PTX55895.1, ECO:0000313|Proteomes:UP000243978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100977 {ECO:0000313|EMBL:PTX55895.1,
RC   ECO:0000313|Proteomes:UP000243978};
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 (APR-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:PTX55895.1}.
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DR   EMBL; QBKS01000001; PTX55895.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6BIL0; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000243978; 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; 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:PTX55895.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:PTX55895.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243978};
KW   Transferase {ECO:0000313|EMBL:PTX55895.1}.
FT   DOMAIN          64..274
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          299..437
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          528..770
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          795..914
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   924 AA;  100392 MW;  13C9CF01C64B84BB CRC64;
     MAFSDRISRS PLIYDETVAA DIRAEFGDVP EPLCALLEAA ASCSGYLAGL MRREAEWVRT
     FATHEADALR DGVWADIAAA EDLKPAFRQA KRRIALLTAL ADLGGLWPLE TVTHCLTELA
     DRCLQVGLSA LVAAQIARGA LPGLKPEDAE TGGGMCVLAM GKMGAYELNY SSDIDLICLF
     DESRFAPDDY TQARATFVKI TRALMGMMSD VTADGYVFRT DLRLRPDASV TPVCIAMEAA
     ERYYESVGRT WERAAFIKAR PCAGDIAAGD AFLQRLAPFI WRKHLDFAAI QDAHDMRLRI
     RSHKGLGGEM ALEGHNMKLG AGGIREIEFF TQTRQLIAGG RDASLRARGT LEGLSCLVDA
     GWIPAEAAQV LAASYVAHRE VEHRLQMIGD AQTHDLPKNS QGFDRLARFM GFAETESFRA
     RVLERLDQVA AVTDEFFAPE ADETGGDVPS ELESAQSYLE RWRSLPALRS ERAVTLFQRV
     FPGVLAQMAR APRPREAMAE FERFLSGLPA GVQVFSLFDA NPKLAALIVE ICATSPALAT
     YLSRNAAVLD AVIGGGFFAP WPGVDALRAE LAEQMRQAPD YEAKLDTARR WQKEWHFRIG
     VHHLQQLLEA GDVAAQYADL AEATVSALMA VVTDEFARKH GPPPGQGALV LAMGSLGVGR
     LSAVSDLDMI VIYEPGDEEI STGPRSLPVR SYYAKLTQAL VTALSAPMAE GRLYEVDLRL
     RPSGQSGPVA TSLASYAGYQ KGEAWVWEHL ALTRARPVFG AAELRARVEE VRVDVLTDGY
     PIEQIKRETQ EMRVRLAEAG RGRGTWDVKG GPGGMQDVEL CSQAIGLMAR SAARGLTEQL
     DTGVDAGLIT TEDAATLAQA HDLYSRVQLA ARLLTAKPLD PDEIGEGGLR LLLRECGCDS
     LDALAARLEN CRKQAAGVVD KALS
//
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