ID G5R5Q8_SALSE Unreviewed; 448 AA.
AC G5R5Q8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:EHC82368.1};
DE Flags: Fragment;
GN ORFNames=LTSESEN_4974 {ECO:0000313|EMBL:EHC82368.1};
OS Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC82368.1, ECO:0000313|Proteomes:UP000005065};
RN [1] {ECO:0000313|EMBL:EHC82368.1, ECO:0000313|Proteomes:UP000005065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-543 {ECO:0000313|EMBL:EHC82368.1,
RC ECO:0000313|Proteomes:UP000005065};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(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:EHC82368.1}.
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DR EMBL; AFCU01001602; EHC82368.1; -; Genomic_DNA.
DR AlphaFoldDB; G5R5Q8; -.
DR PATRIC; fig|913082.3.peg.3864; -.
DR Proteomes; UP000005065; 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; 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; 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; 1.
DR Pfam; PF03710; GlnE; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:EHC82368.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:EHC82368.1}; Transferase {ECO:0000313|EMBL:EHC82368.1}.
FT DOMAIN 55..307
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 327..419
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHC82368.1"
SQ SEQUENCE 448 AA; 50902 MW; C789C8D5FEACED40 CRC64;
RGRQVLDQLM PHLLADVCSR EDAAVTLSRI TPLLAGIVTR TTYLELLSEF PGALKHLIML
CAASPMIASQ LARYPLLLDE LLDPGTLYQP TATDAYRDEL RQYLLRVPEE DEEQQLEALR
QFKQAQLLRI AAADIAGTLP VMKVSDHLTW LAEAMIDAVV QQAWTQMVAR YGQPAHLDER
QGRGFAVVGY GKLGGWELGY SSDLDLIFLH DCPMDVMTNG EREIDGRQFY LRLAQRIMHL
FSTRTSSGIL YEVDARLRPS GAAGMLVTSA DAFADYQQHE AWTWEHQALV RARVVYGDPQ
LTSQFDAVRR TIMTTARDGK TLQTEVREMR EKMRAHLGNK HRDRFDIKAD EGGITDIEFI
AQYLVLRYAH EKPKLTRWSD NVRILELLAQ NGIMDEYEAQ ALTVAYTTLR DELHHLALQE
LPGHVAQTCF SKERALVQAS WRKWLVAV
//
