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
//