ID A0A1Z8LAN3_9PROT Unreviewed; 539 AA.
AC A0A1Z8LAN3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN ORFNames=CBB73_02215 {ECO:0000313|EMBL:OUT45861.1};
OS Pelagibacteraceae bacterium TMED13.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=1986627 {ECO:0000313|EMBL:OUT45861.1, ECO:0000313|Proteomes:UP000196466};
RN [1] {ECO:0000313|EMBL:OUT45861.1, ECO:0000313|Proteomes:UP000196466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED13 {ECO:0000313|EMBL:OUT45861.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58359; EC=1.4.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001895};
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:OUT45861.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NHBS01000012; OUT45861.1; -; Genomic_DNA.
DR Proteomes; UP000196466; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR024188; GltB.
DR InterPro; IPR002932; Glu_synthdom.
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 SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 408..438
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 539 AA; 60691 MW; 28DCE90C521DE071 CRC64;
MNEVXWGRYS LLVXTGISTV ALLILSFFFK FLILLTFIXS FLFAXSLWDF FQKKRSILSN
FPLLGRFRFF LESIRPELRQ YYWESDDDEV PYSRNQRSMV YQRSKDIEGV RPFGSLEKMY
REDFVWLNHS ITPSHIKNSE FRIKVGSGKN FYNMSVLNIS GTSFGAISPP AITSLNMAAX
MGNFAHNTGE GSMSSYHEKG GGDTIWQIST GYFGCRDSKG NFSPKKFTIK AKSPQIKMIE
IKIXQGAKPG HGGMLLAPKV TEEIAATRGI EVGKDCISPA RHKEFSTPSQ LLKFVEKLRX
LSGGKPVGIK MCIGHPWELI SIIKTMVLEK KYIDFITVDG AEGGTGAAPA EFTDHLGSPL
KDAIIFVDNX LVGSNLRDRV KIGVSGKIVS AFDIAHMXAX GADWVNMARP FMFSIGCIQC
RSCHTGECPT GIATMXPMRY RAIDXKDRSN RAFNFHKNTI FVLKELLESV GVKHPSELNR
RHIVRRLSES EILLADQIYP RAEKGELLKK GKKTIADPRI NVYWNKVNTK SFNYDTRSI
//
