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Database: UniProt
Entry: Q2J2N3_RHOP2
LinkDB: Q2J2N3_RHOP2
Original site: Q2J2N3_RHOP2 
ID   Q2J2N3_RHOP2            Unreviewed;       543 AA.
AC   Q2J2N3;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Ferredoxin-dependent glutamate synthase {ECO:0000313|EMBL:ABD05277.1};
GN   OrderedLocusNames=RPB_0566 {ECO:0000313|EMBL:ABD05277.1};
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD05277.1, ECO:0000313|Proteomes:UP000008809};
RN   [1] {ECO:0000313|EMBL:ABD05277.1, ECO:0000313|Proteomes:UP000008809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2 {ECO:0000313|EMBL:ABD05277.1,
RC   ECO:0000313|Proteomes:UP000008809};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-2006) 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; CP000250; ABD05277.1; -; Genomic_DNA.
DR   RefSeq; WP_011439467.1; NC_007778.1.
DR   AlphaFoldDB; Q2J2N3; -.
DR   STRING; 316058.RPB_0566; -.
DR   KEGG; rpb:RPB_0566; -.
DR   eggNOG; COG0069; Bacteria.
DR   HOGENOM; CLU_026563_1_0_5; -.
DR   OrthoDB; 9795032at2; -.
DR   Proteomes; UP000008809; Chromosome.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          166..483
FT                   /note="Glutamate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01645"
SQ   SEQUENCE   543 AA;  59620 MW;  8643896466988F7A CRC64;
     METILLPFSP RYIALTICAV LAALFAAIAI VDYDTKLFGV LLTLALVFGA LTLLGVRDLF
     QKNHAVLRNY PISAHLRFLL EEIRPEMRQY FFESEKDGKP FSRDTRALIY QRAKMVLDKR
     PFGTQKDVYE QGYEWMHHSV APRPHAEERF RITIGGPDCA RPYSASVFNI SAMSFGALSP
     NAIRALNAGA KKGGFAHDTG EGGVSPYHRE NGGDLIWEIG SGYFGCRTRD GQFDPEAFAR
     LATDDQIKMV ELKISQGAKP GHGGVLPAAK VSEEISRIRG VAMDEDCISP PYHKAFSTPI
     EMLRFVAEMR RLSGGKPAGF KLCIGHPWEF LAICKAMLAT GITPDFIVVD GKEGGTGAAP
     LEFMDHLGMP MRDGVSFVHN ALIGVGLRDR IRIGAAGKIA TAFDMARAMA LGADWCNSGR
     GFMFALGCIQ SLSCHTDRCP TGVTTQEPSR YRALVVPDKI ERVYNYHRAT LHALAELIAA
     AGLDHPQDIR PIHFSQRSSS SEVVSLAQLY PTLRPGELLD GTDDPRFKHA WAMARAETFA
     AAV
//
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