ID   A0A2G1XVD7_9GAMM        Unreviewed;       926 AA.
AC   A0A2G1XVD7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase {ECO:0000313|EMBL:PHQ55165.1};
DE   Flags: Fragment;
GN   ORFNames=COA29_05490 {ECO:0000313|EMBL:PHQ55165.1};
OS   Porticoccus sp.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae; Porticoccus.
OX   NCBI_TaxID=2024853 {ECO:0000313|EMBL:PHQ55165.1, ECO:0000313|Proteomes:UP000226842};
RN   [1] {ECO:0000313|Proteomes:UP000226842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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:PHQ55165.1}.
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DR   EMBL; NVQM01000077; PHQ55165.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G1XVD7; -.
DR   Proteomes; UP000226842; 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; 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   HAMAP; MF_00802; GlnE; 1.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000313|EMBL:PHQ55165.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:PHQ55165.1}; Transferase {ECO:0000313|EMBL:PHQ55165.1}.
FT   DOMAIN          5..249
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          273..410
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          531..781
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          816..898
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PHQ55165.1"
SQ   SEQUENCE   926 AA;  104456 MW;  4649791DAEED64F6 CRC64;
     TLARQLPLVW ACSEYVAAAC AGQPTLFQQL VESGDLEASY SDTALKEHLA LWLSDVTSED
     RLLKVLRQFR TREMVRIIWR DLTRSAELEE TTADMSRLAE ACLQGALDFL YPRACAEWGT
     PVDESGEPQQ LVILGMGKLG ACELNVSSDI DLIFAYPEAG ETRGGRRSLS NQEFFIRLGQ
     WLIKALDTPT VDGFVFRVDM RLRPYGQSGA LVLNFDAMEE YYQTQGRDWE RYAMIKARVV
     AGDRAAGSRL MAMLRPFTYR KYLDFSAFES LRGMKAMINR EVQRKGLVSD VKRGAGGIRE
     VEFVAQAFQI IRGGRDRRFQ TPPLKEVLEL LGQEGLLPLE DTERLYRGYR FLRNVEHVLQ
     GWQDKQTQLL PADELGRCRV AYLMGCSSWD QFLLQLDEFR QFIHQLFEDV VAEQHQGDGG
     DDAPEEHPLA EQVWQAIDGD ELMPDELATM GYDLPEKAAE MINTLRGSRS VQSMANDTRG
     RLDKLMPQLI SICGQRDNAT ETLGRVLKLV EAVARRSAYL LLLKENPAAL QSTVKLFSGS
     SWVADQLVRY PALLDELLDS RTLFSLPEKS TLEDELHQQL LRVPTDDLES QMEVLRYFQQ
     SHSLRVAACE LEEILPLMKV SDYLTWLAEA ILSHVLQLAW NQLVERHGYP KTAEGETAGF
     LIVGYGKLGG IELGHGSDLD LVFLHDADAA AATDGVHPLD SATFFARLGQ RIVHILTAKT
     SSGDLYEVDM RLRPSGSSGM LVSSLTAFEK YQLGEAWTWE HQALVRARPV AGPEKLVRAF
     AEIRQRVLVL PRQRDKLVAD VLEMRGRMKK HLASGKADQD RVFHLKHDPG GIVDIEFMVQ
     FAVLAWSHDI PDLTRWSDNI RILECLEESG VLSVEDVDIL TSAYKNYRSA GHRLQLQQAE
     LVVSAAEFAV QRQQVAALWH RLLGEE
//