ID   A0A248VE74_9BURK        Unreviewed;       536 AA.
AC   A0A248VE74;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=FMN-binding glutamate synthase family protein {ECO:0000313|EMBL:ASV97190.1};
GN   ORFNames=CJU94_02805 {ECO:0000313|EMBL:ASV97190.1};
OS   Paraburkholderia aromaticivorans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2026199 {ECO:0000313|EMBL:ASV97190.1, ECO:0000313|Proteomes:UP000215158};
RN   [1] {ECO:0000313|Proteomes:UP000215158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BN5 {ECO:0000313|Proteomes:UP000215158};
RA   Lee Y.;
RT   "Identification and genetic characteristics of simultaneous BTEX- and
RT   naphthalene-degrading Paraburkholderia sp. BN5 isolated from petroleum-
RT   contaminated soil.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009716, ECO:0000256|PIRNR:PIRNR006429}.
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DR   EMBL; CP022989; ASV97190.1; -; Genomic_DNA.
DR   RefSeq; WP_007179306.1; NZ_CP022989.1.
DR   AlphaFoldDB; A0A248VE74; -.
DR   KEGG; parb:CJU94_02805; -.
DR   OrthoDB; 9795032at2; -.
DR   Proteomes; UP000215158; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..536
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012038109"
FT   TRANSMEM        30..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          154..470
FT                   /note="Glutamate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01645"
SQ   SEQUENCE   536 AA;  59251 MW;  594C8B7473222AD7 CRC64;
     MFSRRYLAMW CAAALFAVCA AFAATHHISW FWIIVPLALV ALGLFDLTQQ RHAILRNYPL
     WGHFRFLFEF IRPEIRQYFV EGDTDEKPFS RAQRSIVYQR AKNDVDSRPY GTELDVKAVA
     HEWISHSLAP TRLDSHDFRI VVGPDRAQPY SMSIFNVSAM SFGSLSANAI MALNLGAKKG
     NFAHDTGEGS MSKYHREHGG DIIWEIASGY FGCRNEDGTF SAEKFAKQAA EPQVKMIEVK
     LSQGAKPGHG GVLPAAKITP EIAETRGVPM GRDCISPATH SEFSTPRGLL EFVDRLRTLS
     GGKPTGFKLC IGHPWEFFGI AKAMLETGIL PDFIVVDGAE GGTGAAPLEF TDHVGVPLQE
     GLLLVHNTLV GIGLRQRIRI GASGKMITAF DITKTLAIGA DWVNAARGFM FAVGCIQAQT
     CHTGRCPTGV ATQDPVRQRA LVVPDKADRV FNFHHNTLHA LKEIIQAAGL KHPAELRAHH
     IVRRVSSHEV QLMSELLKYL DPNDLLNGNY RYSLFEKYWP VAQSDSFSPK VELAAT
//