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
//