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Database: UniProt
Entry: W6K389_9MICO
LinkDB: W6K389_9MICO
Original site: W6K389_9MICO 
ID   W6K389_9MICO            Unreviewed;       904 AA.
AC   W6K389;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:CCH72944.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:CCH72944.1};
GN   Name=glnE {ECO:0000313|EMBL:CCH72944.1};
GN   ORFNames=BN11_2140001 {ECO:0000313|EMBL:CCH72944.1};
OS   Tetrasphaera australiensis Ben110.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1193182 {ECO:0000313|EMBL:CCH72944.1, ECO:0000313|Proteomes:UP000035763};
RN   [1] {ECO:0000313|EMBL:CCH72944.1, ECO:0000313|Proteomes:UP000035763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ben110 {ECO:0000313|EMBL:CCH72944.1,
RC   ECO:0000313|Proteomes:UP000035763};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
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:CCH72944.1}.
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DR   EMBL; CAJA01000129; CCH72944.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6K389; -.
DR   STRING; 1193182.BN11_2140001; -.
DR   Proteomes; UP000035763; Unassembled WGS sequence.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-EC.
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; 1.20.120.1510; -; 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; 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:CCH72944.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:CCH72944.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035763};
KW   Transferase {ECO:0000313|EMBL:CCH72944.1}.
FT   DOMAIN          24..231
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          252..392
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          497..733
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          757..896
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   904 AA;  98800 MW;  A5D9BAEE2B3C6943 CRC64;
     MIGASIALGD HLVAHPEHWR SVAEARPRTP EQRVARIVGR VRNPDPGLSP DDALRVYYRR
     GLLGISALDL VAPDPLVKLP DTAAALADLA AAALEGALVI AQSELPDDAA QCRFAVIAMG
     KTGGRELNYI SDVDVIFVAE PADGVSEQDA MAAAARLATR LMTACSAATA HGTLWPVDAA
     LRPEGKAGPL VRTVASHKQY YERWAKTWEF QALLKARPVA GDKEVGAAYL QAMAPMVWQA
     ASRENFVDDV QAMRRRVEAH IPSAEADRQL KLGPGGLRDI EFSVQLLQLV HGRTDERIRS
     GTTLDALAAL AAYGYVGRDD AAQLAAAYRL LRTLEHRIQL LRLRRTHLMP TSPHELRRLG
     RALGHREDPA AAVVAEWKAE AREVRRLHER LFYRPLLGAV ARLGTDDARL TPEAARERLS
     ALGFRDPTGA LRHLEALTEG LSRRAAIQRH LLPVMLGWFA AEADPDGGLL AFRKVSESLD
     SSHWYLRLLR DEPAAAEQLA RTLARSKFAA EVLVAAPEAV QILGEPGGVR PHSRGDIERR
     MRTAAQRKTS LDDAIAAARQ VRRLELFRIA VADLVGDLPQ PDVGRALSDL TAATIEVALQ
     FVIREEEKRA GRPLVTDLLI VGMGRLGGNE LGYASDADVL FVHDPHIGAD EDAAQAQALA
     VVKSMQRVLS VPGPDPAIGL DADLRPEGKN GPLVRSLDSY RAYYDRWALI WEAQALVRAR
     PIAGNAELAA RFEDLIDPIR WHGAGLSAQD LREIRRLKAR MEAERLPRGA DKRTHFKLGT
     GGLSDVEWVV QTLQMEHAHN YPTLRTTSTL PALTAATQAR LISSADSAAL AKAWEFAAHA
     RNASMLYRGK AVESVPTDSR EADGTARIMG LPPGSGQEFG EDYRRITRHA RAVVDRVFYG
     REES
//
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