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Database: UniProt
Entry: K2JHW4_9RHOB
LinkDB: K2JHW4_9RHOB
Original site: K2JHW4_9RHOB 
ID   K2JHW4_9RHOB            Unreviewed;       505 AA.
AC   K2JHW4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Ferredoxin-dependent glutamate synthase {ECO:0000313|EMBL:EKE74758.1};
GN   ORFNames=B30_03500 {ECO:0000313|EMBL:EKE74758.1};
OS   Celeribacter baekdonensis B30.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE74758.1, ECO:0000313|Proteomes:UP000006762};
RN   [1] {ECO:0000313|EMBL:EKE74758.1, ECO:0000313|Proteomes:UP000006762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B30 {ECO:0000313|EMBL:EKE74758.1,
RC   ECO:0000313|Proteomes:UP000006762};
RA   Wang W.;
RT   "Celeribacter baekdonensis B30 Genome Sequencing.";
RL   Submitted (SEP-2012) 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:EKE74758.1}.
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DR   EMBL; AMRK01000001; EKE74758.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2JHW4; -.
DR   STRING; 1208323.B30_03500; -.
DR   PATRIC; fig|1208323.3.peg.717; -.
DR   eggNOG; COG0069; Bacteria.
DR   Proteomes; UP000006762; 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   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.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006762};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          138..464
FT                   /note="Glutamate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01645"
SQ   SEQUENCE   505 AA;  55351 MW;  F39103E74B45881D CRC64;
     MTVWHWTMGA LQVLALIFVL AIGFMALAAL ALYVLDKRQT RDAILRNYPV IGHFRHLFSS
     LGEFFRQYFF AMDREEMPFN RAQRDWIYRA SDGKGNTVAF GSTRSLSIPG TPIFMNAPFP
     PLDDQFTSTD PMVIGPHCRV PYTAKSIFNI SGMSYGAISK PAVLALSKGA KEAGIWLNTG
     EGGLSPFHLE GGADLVYQIG TAKYGIRDDA GNLDDDKLRA MAAHETVRMF EIKLSQGAKP
     GKGGILPAAK ITPEIAQIRG LKPGEDGISP NRHREVDDFG DLLDFIDHIR EVTGKPVGFK
     FVVGSSRPWA EFFEMIVERG PESAPDFITI DGGEGGTGAA PMPLIDLVGM PIKEALIRIV
     DLRDKYGLHD RIRIVAAGKL VNPADIAWAI CAGADFVASA RGFMFSLGCI QALKCNKNTC
     PTGITTHDPH LQGGLVVNDK YKKVAAYAKA STYELEMIAH SVGVLEPRQM RRRHVRIVQA
     DGTSIPLDRI VPSFDAERYN TPTQL
//
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