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Database: UniProt
Entry: Q63QY4_BURPS
LinkDB: Q63QY4_BURPS
Original site: Q63QY4_BURPS 
ID   Q63QY4_BURPS            Unreviewed;       546 AA.
AC   Q63QY4;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Glutamate synthase {ECO:0000313|EMBL:CAH36900.1};
GN   OrderedLocusNames=BPSL2890 {ECO:0000313|EMBL:CAH36900.1};
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH36900.1, ECO:0000313|Proteomes:UP000000605};
RN   [1] {ECO:0000313|EMBL:CAH36900.1, ECO:0000313|Proteomes:UP000000605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243 {ECO:0000313|EMBL:CAH36900.1,
RC   ECO:0000313|Proteomes:UP000000605};
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA   Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA   Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA   Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA   Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA   Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA   Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009716, ECO:0000256|PIRNR:PIRNR006429}.
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DR   EMBL; BX571965; CAH36900.1; -; Genomic_DNA.
DR   RefSeq; WP_004522103.1; NZ_CP009538.1.
DR   RefSeq; YP_109484.1; NC_006350.1.
DR   AlphaFoldDB; Q63QY4; -.
DR   STRING; 272560.BPSL2890; -.
DR   GeneID; 56528308; -.
DR   KEGG; bps:BPSL2890; -.
DR   PATRIC; fig|272560.51.peg.2401; -.
DR   eggNOG; COG0069; Bacteria.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR   CDD; cd02808; GltS_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR024188; GltB.
DR   InterPro; IPR002932; Glu_synthdom.
DR   InterPro; IPR027283; YerD.
DR   PANTHER; PTHR43819:SF1; ARCHAEAL GLUTAMATE SYNTHASE [NADPH]; 1.
DR   PANTHER; PTHR43819; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR   Pfam; PF01645; Glu_synthase; 1.
DR   PIRSF; PIRSF006429; GOGAT_lg_2; 1.
DR   PIRSF; PIRSF500060; UCP500060; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000605}.
FT   DOMAIN          154..470
FT                   /note="Glutamate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01645"
SQ   SEQUENCE   546 AA;  59752 MW;  220B4B1BBF7D39B0 CRC64;
     MLSRRYLAMW CALALFAAAA VLAARHTISW LWIVPVAALV ALGLYDLNQD RHAILRNYPL
     WGHLRFLFEF IRPEIRQYFV EDDTDEKPFS RAQRSVVYQR AKNVADNRPY GTELDVKAVA
     HEWISHSLAP TKLDGHDFRI RVGATRKQPY DISIFNISAM SFGALSANAI RALNLGAKQG
     GFAHDTGEGS LSKYHREHGG DIIWEIGSGY FGCRRDDGTF DPEKFAKQAR EPQVKMIEVK
     LSQGAKPGHG GVLPAAKITP EIAETRGVPM GKDCVSPAAH SAFSTPRGLL EFVDRLRELS
     GGKPTGFKLC VGHPWEFFGI AKAMLETGIV PDFIVVDGAE GGTGAAPLEF TDHVGVPLQE
     GLLLVHNTLV GIGLREQVKL GASGKIITAF DIARTLAIGA DWVNSARGFM FAVGCIQAQH
     CHTDRCPTGV ATQDPVRQRA LVVPDKADRV YNFHRNTLHA LQELVQAAGL SHPSELRAHH
     IVQRVAPHEV RLMSQLLKYL EPGALLNGGH CGFSLYETWW PLARGDSFSP GEGAYARVGT
     GAPARA
//
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