ID A0A2B2CDU5_9BACI Unreviewed; 521 AA.
AC A0A2B2CDU5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=FMN-binding glutamate synthase family protein {ECO:0000313|EMBL:PFP30499.1};
GN ORFNames=COJ96_04600 {ECO:0000313|EMBL:PFP30499.1};
OS Bacillus sp. AFS073361.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP30499.1, ECO:0000313|Proteomes:UP000223997};
RN [1] {ECO:0000313|EMBL:PFP30499.1, ECO:0000313|Proteomes:UP000223997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS073361 {ECO:0000313|EMBL:PFP30499.1,
RC ECO:0000313|Proteomes:UP000223997};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) 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:PFP30499.1}.
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DR EMBL; NUZU01000007; PFP30499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B2CDU5; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000223997; 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; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR PANTHER; PTHR43819:SF1; 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:UP000223997};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..489
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
SQ SEQUENCE 521 AA; 57962 MW; 055F9BD166CE02F9 CRC64;
MVWTIFIFLL IVFIIGPIAL LIWLHILAKK PQHSIIRAHP YLGWMRYLLE KIGPEFRQYW
FDDDNSGKPF SRTDFLGIVF SAKYRSDLLS FGSKRDFDNP GYYIANGLFP LLNEELRVDN
QEKVHSMKYK IDHEGLFTRH EQLEKDQTTR WLYHEEETII VGGDRKFPWR LSGPFGVSAT
SYGAVGENYI LSTGRGSYLA GGSWINTGEG GVAPEHLESG VDVVAQIGPG IFGFRDDEGN
FSLDEFKCKA KEPNIKAFEL KFGQGAKIRG GHLEGSKVST KVATIRKVPV GKTINSPNRF
PFLHNALETL EFIKMLQEEG GKPIGIKIVV GHPSSLNELF ESMNHLKIYP DFITVDGGEG
GTGATYKSMA DTMGLPLYPA LIAVVDKAHQ FGVRKKLKIF ASGKLISADK IAIALAIGAD
AVNSARGFMI ANGCIMALQC HTGKCPTGVT TTDPKYQEAL VPEEKKWRVM NYIINVRQGL
FALAAACGID SPCKFTREHI VFKDVDGRIK KLSELFPMID S
//