ID   A0A1J6XEM6_9MICO        Unreviewed;       992 AA.
AC   A0A1J6XEM6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Bifunctional glutamine-synthetase adenylyltransferase/deadenyltransferase {ECO:0000313|EMBL:OIU88202.1};
GN   ORFNames=BFN01_05525 {ECO:0000313|EMBL:OIU88202.1};
OS   Microbacterium sp. AR7-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1891970 {ECO:0000313|EMBL:OIU88202.1, ECO:0000313|Proteomes:UP000183831};
RN   [1] {ECO:0000313|EMBL:OIU88202.1, ECO:0000313|Proteomes:UP000183831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR7-10 {ECO:0000313|EMBL:OIU88202.1,
RC   ECO:0000313|Proteomes:UP000183831};
RA   Pei D., Jiang J., Chen H., Li K., Yu W., Ma Y., Xu J.;
RT   "The draft genome of Microbacterium sp. AR7-10 isolated from the wild
RT   caught mosquito Anopheles.";
RL   Submitted (SEP-2016) 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:OIU88202.1}.
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DR   EMBL; MJIR01000037; OIU88202.1; -; Genomic_DNA.
DR   RefSeq; WP_071641833.1; NZ_MJIR01000037.1.
DR   AlphaFoldDB; A0A1J6XEM6; -.
DR   STRING; 1891970.BFN01_05525; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000183831; 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; 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:OIU88202.1}; Transferase {ECO:0000313|EMBL:OIU88202.1}.
FT   DOMAIN          84..326
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          350..487
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          595..825
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          864..989
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   992 AA;  108753 MW;  07D2AE9925D0DA98 CRC64;
     MARPDASISL SALARLGFVE LTSASADLTE LSELTGLERA QLADGMVAAD PDAAVRGLVG
     VARRDAAQVA AVLSDPVARE AAWRLFGASR ALGMFFERHP ERLHPDLLLR THLPDAAELT
     ARMLGAVEAD DGFARADDPV TALRVEYRSC LSEIAAVDLA SESATLAIAG VSAALADAAG
     AALEAGLAVA RAVVDRSGRA GTHDEIAATR LAIIGMGKAG ARELNYLSDV DVIFVAGTAD
     ESVVSEARAI DIATRLARET MTALSGVEIE PPLWEVDAAL RPEGKQGALV RSLASHLAYY
     DRWAKSWEFQ ALLKARPLAG DTRLGADYIT AVQPKVWTSA ERSDFVESVQ RMRERVTDHI
     PADDVPYQIK LGPGGLRDIE FTVQLLQLVH GLSDEGIRTR GTLESLDALV EGGYIGRAEA
     SAFGEQYRIL RLLEHRLQLH DLTRTHLMPR DDEGMRRLAR ATALADSASG LQQIWDEVRR
     AVRDQHVRLF YRPLLSAVAS LPAEERTLST AQAGSRLAAI GFRDPAGALR HIAALTSGLS
     RKATIQRHLM PVMLRWFADG TDPDYGLVAF RRISERLGDT HWFLRMLRDS SGAAERLTRL
     LSSSRYVGEL MEWIPESVAW LDTPAALRPR GGAALDEEAR AIQTRHATTK AALRAVRALR
     RRELLRTAMG AVLEQVGVDE MARALTEITE ATIQAALRAV RREVVPPEDD AMDFSIIAMG
     RFGGAELGFG SDADVLFIYD PNGVDPQRAQ QHAARIVAGL REHLADQRVP LELDADLRPE
     GRNGPIVRTI EAYTQYYRRW SLSWEAQALL RARGIAGSVK LITRFTALAD SIRYPEAVSL
     QDVREIKRIK ARVEGERLPQ GADPRRHLKL GPGTLSDVEW MVQVLQLQHG HRVPDLRTTS
     TLQALDAAVL ADLLPADDAE RLREAWVLAS RLRSAMTLLT GQTKDVLPAD IRELDGVGRL
     LGYPDRAATV LEEDYLRVTR RARRVFEKQF YG
//