ID A0A0W1RSK8_9GAMM Unreviewed; 545 AA.
AC A0A0W1RSK8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KTG16586.1};
GN ORFNames=AUR63_00520 {ECO:0000313|EMBL:KTG16586.1};
OS Guyparkeria sp. XI15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Thioalkalibacteraceae; Guyparkeria.
OX NCBI_TaxID=1766620 {ECO:0000313|EMBL:KTG16586.1, ECO:0000313|Proteomes:UP000053033};
RN [1] {ECO:0000313|Proteomes:UP000053033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XI15 {ECO:0000313|Proteomes:UP000053033};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloferax marisrubri sp. nov., isolated from the Discovery deep brine-
RT seawater interface in the Red Sea.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716, ECO:0000256|PIRNR:PIRNR006429}.
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:KTG16586.1}.
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DR EMBL; LOPX01000014; KTG16586.1; -; Genomic_DNA.
DR RefSeq; WP_058574808.1; NZ_LOPX01000014.1.
DR AlphaFoldDB; A0A0W1RSK8; -.
DR STRING; 1766620.AUR63_00520; -.
DR Proteomes; UP000053033; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053033};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..21
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 152..470
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
SQ SEQUENCE 545 AA; 60351 MW; 6FAF548BBEF95C83 CRC64;
MHRRFLVIAA VSLAVIVGLG LWWPPLWWLL LPALPLIGLG LYDMRQSRHS LRRNFPLVAR
GRWLVERMRP FIRQYLLESD TDGTPISRMF RSVVYQRAKQ QSETIPYGTR VDTYRLGYEW
LGQSMAAIDV EEIDPDLRVT IGGPQCRQPY SASVLNISAM SYGSLSPTAI QALNRGAQLG
GFSHNTGEGG LSPHHLEHGG DLVWQIGTGY FGCRDDRGRF CAETFREKAV RPVVKMIELK
ISQGAKPGHG GILPAEKNTA EIAAIRDVPA GTRINSPPAH TTFDSPLGLI DFIERLRELS
DGKPVGIKLA IGRKSEFLAL GKAMVERGIY PDFITVDGGE GGTGAAPIEY TNSVGMPLRE
AVAFVDDSLT GFGIRQHIRV IASGKIFTGF HLVKNLALGA DLCNSARGMM LALGCVQSLT
CNTNRCPTGV ATQNPDLYRG LVVPDKAERV HYFHEGTLAA TAELLSSAGL RHPEELNRTH
LYRRVSPEAI RRYDEIFPYV KKGCFLGDDP PERYALELRE ARADNFLPET CFTEIRESQQ
PVERD
//
