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Database: UniProt
Entry: F3FPU6_PSESX
LinkDB: F3FPU6_PSESX
Original site: F3FPU6_PSESX 
ID   F3FPU6_PSESX            Unreviewed;       614 AA.
AC   F3FPU6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Bifunctional glutamine-synthetase adenylyltransferase/deadenyltransferase {ECO:0000313|EMBL:EGH32238.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:EGH32238.1};
GN   ORFNames=PSYJA_26075 {ECO:0000313|EMBL:EGH32238.1};
OS   Pseudomonas syringae pv. japonica str. M301072.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH32238.1, ECO:0000313|Proteomes:UP000004471};
RN   [1] {ECO:0000313|EMBL:EGH32238.1, ECO:0000313|Proteomes:UP000004471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
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:EGH32238.1}.
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DR   EMBL; AEAH01001178; EGH32238.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3FPU6; -.
DR   PATRIC; fig|629262.5.peg.4343; -.
DR   HOGENOM; CLU_037743_0_0_6; -.
DR   Proteomes; UP000004471; 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   CDD; cd05401; NT_GlnE_GlnD_like; 1.
DR   Gene3D; 1.20.120.1510; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
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; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
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:EGH32238.1}; Transferase {ECO:0000313|EMBL:EGH32238.1}.
FT   DOMAIN          2..84
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          209..462
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          504..582
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   614 AA;  68864 MW;  694C21705B98C832 CRC64;
     MLKTLEGQGY LPSAVTEELR EGYEFLRYTE HAIQAIADRQ TQMLPDNEQD QARVALIMGF
     ADWAAFHERL MYWRGRVAWH FRQVIADPDA DPDDEQDEDD EVVVGRRMAA TVEESQDEEA
     AGRQLLQAGF VDAERALKHL ANLRSSPNLR SMQRLSRERL DAFIPRLLAQ AVEHEKPDLV
     LERVLPLVEA VARRSAYLVL LTENPDALRQ LLTLCAASPW IAEQIARFPL LLDELLNEGR
     LFNPPLAPEL AAELRERLIR IPEDDLEQQM EALRHFKLAH SLRVAASEIS GSLPLMKVSD
     YLTWLAEAIL DQVLALAWRY SVARHGTPLR PDGTLCDPGF VIVGYGKVGG IELGHGSDLD
     LVFIHDGDLE AETDGAKPID TAQFFTRLGQ RVIHLLTTQT NSGQLYDVDM RLRPSGASGL
     LVSSLGAFAR YQANEAWTWE HQALVRARVM TGSRDVGEQF EKVRADVLGR ERDLDKLRAE
     VSEMRAKMRD NLGTRATAAG RAANAFEAAV PFDLKQDAGG IVDIEFMVQY AALAWSREHP
     ALLQYTDNIR ILEGLEEAGL LPDTDAGLLR EAYKAYRSAA HRQALQKQAG VVSGDQFHAQ
     RREVMRIWTQ MGLS
//
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