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Database: UniProt
Entry: A0A0Q7SRK6_9BURK
LinkDB: A0A0Q7SRK6_9BURK
Original site: A0A0Q7SRK6_9BURK 
ID   A0A0Q7SRK6_9BURK        Unreviewed;       550 AA.
AC   A0A0Q7SRK6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KQY90290.1};
GN   ORFNames=ASD35_00300 {ECO:0000313|EMBL:KQY90290.1};
OS   Pelomonas sp. Root1444.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY90290.1, ECO:0000313|Proteomes:UP000051648};
RN   [1] {ECO:0000313|Proteomes:UP000051648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1444 {ECO:0000313|Proteomes:UP000051648};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY90290.1, ECO:0000313|Proteomes:UP000051648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1444 {ECO:0000313|EMBL:KQY90290.1,
RC   ECO:0000313|Proteomes:UP000051648};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQY90290.1}.
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DR   EMBL; LMFP01000001; KQY90290.1; -; Genomic_DNA.
DR   RefSeq; WP_056872910.1; NZ_LMFP01000001.1.
DR   AlphaFoldDB; A0A0Q7SRK6; -.
DR   STRING; 1736464.ASD35_00300; -.
DR   OrthoDB; 9795032at2; -.
DR   Proteomes; UP000051648; 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:UP000051648};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          166..482
FT                   /note="Glutamate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01645"
SQ   SEQUENCE   550 AA;  59874 MW;  C62AB699E398D2AD CRC64;
     MLAWPRWTRR INEHFPLRYL TWLLCGLLAL FFAIRWTAGL GDAVLMVVFL ALALLGLRDS
     RQQHHSILRN YPVIGHLRFL LEFIRPEIRQ YFVEGDNDAA PFSRAQRSIV YQRAKGAPDQ
     RPFGTQLDTG ARGYEWINHS LMPTHLTSHD FRITIGAGRA QPYSASVFNI SAMSFGALSA
     NAILALNKGA KLGGFAHDTG EGSISVHHRA NGGDLIWEIG SGYFGCRNDD GSFSVERFQA
     NAADPQVKMI ELKLSQGAKP GHGGVLPGPK VTAEIAAARG VPEGVDCISP ARHSAFSTPV
     EMMQFIQQLR DLSGGKPTGF KLCIGHPWEW FAVAKAMLET GITPDFIVVD GAEGGTGAAP
     LEFTNHVGAP VQEGLLLVHN TLVGLGLRDT IKLGCAGKIT SAFDIVRLMA LGADWCNSAR
     GFMFALGCIQ AQACHTGHCP TGVTTQDALR QRAINVPDKA HRVANFHQGT LKALKELVEA
     AGLCHPQEIT AQHIVHRLDK HEVRLLANLL PFVEPGALLR GEMPHNTFRI YWPLASAHSF
     APQGSIARSP
//
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