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Database: UniProt
Entry: A0A3P1WI68_9ACTN
LinkDB: A0A3P1WI68_9ACTN
Original site: A0A3P1WI68_9ACTN 
ID   A0A3P1WI68_9ACTN        Unreviewed;       960 AA.
AC   A0A3P1WI68;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase {ECO:0000313|EMBL:RRD46011.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:RRD46011.1};
DE            EC=2.7.7.89 {ECO:0000313|EMBL:RRD46011.1};
GN   ORFNames=EII42_09215 {ECO:0000313|EMBL:RRD46011.1};
OS   Tessaracoccus sp. OH4464_COT-324.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=2491059 {ECO:0000313|EMBL:RRD46011.1, ECO:0000313|Proteomes:UP000274803};
RN   [1] {ECO:0000313|EMBL:RRD46011.1, ECO:0000313|Proteomes:UP000274803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH4464_COT-324 {ECO:0000313|EMBL:RRD46011.1,
RC   ECO:0000313|Proteomes:UP000274803};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-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:RRD46011.1}.
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DR   EMBL; RQYZ01000016; RRD46011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P1WI68; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000274803; Unassembled WGS sequence.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047388; F:[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase activity; IEA:UniProtKB-EC.
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:RRD46011.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274803};
KW   Transferase {ECO:0000313|EMBL:RRD46011.1}.
FT   DOMAIN          75..309
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          333..461
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          569..793
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          830..948
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   960 AA;  104795 MW;  E1C6C07AB4A7F689 CRC64;
     MGRIQSSSAE FARRGFESAT AAARIWDAWP AEQRAMVDLA LFGRVGDRFQ ALETLDRLRA
     TDRFEAIAAD PGWLERVLRV AGASSVLAAG LRTSPETVQL LAEEPRERDE RAWAAFFQAR
     VPVVDGECHR HPDELRSANR AALTLIAARD LAADDPTEIV EGVARELSHV ADCVLETSLA
     LARAETPGWQ AARLAIVALG KAGGQELNYL SDVDVLYIAE PTEGADPDEA AAIANRVAAA
     QARICSAHTK AGTIWSVDAS LRPEGKAGPL VRSLASCRRY YDQWAENWEF QALLKARPAA
     GDLGLGEAFI DLVSPLVWRS GERPGFLPEM RAMRERVIAH IPDKQAETEI KLSEGGLRDT
     EFSVQLLQLV HGRADDRIRD RGTLPALRSL VSCGYIGRSD GSQLAQHYRF QRVLEHRAQL
     VNLRRTHVVP DDDRLAQFAR AGLDDARARW RTSRRDVRRL RQRIFFSPLL DTVVSLPADT
     LLSPDAVKER MRALGFNDPR TALGHMQALT AGTSRAAEIL RQLMPAMLEW IALGPNPDFG
     LLAFRQLCET LGESPWFLRG LRDEGYMATR LAKVASTSRF TVDLLKRAPD TVGLLASDEA
     LTPRSAAELG VAMGRSAARH ADLARALDSA RAFRRSELCR VALRDVLGGV DIVECGRALS
     ALASATVQTA LDIARRAVDA PELGIIALGR WGGEEMSYAS DLDCIFVVAD DAGPAGLAAA
     TELVRELARI LKQPGVEGIT LDADLRPEGK GGPQVRTVSS YRKYYERWGA VWEAQMLLRA
     RHGAGSAELV QAVLDDIDPV RYPERLTDDA VREIRRLKSR MERERIPAGV DPSRHLKLGP
     GGLSDIEWTI QLIQLAHAHR HPELRTTSTL GALAAARALG LVAPGDADAL SAAWRHASTV
     RDAIMLVRGR PSDALPTNTR ELAAVAALLG HDAPVAELGE NTRRHARLAG AVVGRLFWGE
//
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