ID A0A2C1YTU2_9BACI Unreviewed; 524 AA.
AC A0A2C1YTU2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=FMN-binding glutamate synthase family protein {ECO:0000313|EMBL:PGV48331.1};
GN ORFNames=COD92_26830 {ECO:0000313|EMBL:PGV48331.1};
OS Bacillus sp. AFS037270.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV48331.1, ECO:0000313|Proteomes:UP000225442};
RN [1] {ECO:0000313|EMBL:PGV48331.1, ECO:0000313|Proteomes:UP000225442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS037270 {ECO:0000313|EMBL:PGV48331.1,
RC ECO:0000313|Proteomes:UP000225442};
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:PGV48331.1}.
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DR EMBL; NUNF01000070; PGV48331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1YTU2; -.
DR Proteomes; UP000225442; 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 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 120..489
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
SQ SEQUENCE 524 AA; 58363 MW; 9E32D326C2C94E22 CRC64;
MVWTIFIFLL IVFIVGPIAL LLWLHILAKK PQHSIIRAHP YLGWMRYLLE KIGPEFRQYW
FDDDNSGKPF SRTDFLGIVF SAKYRSDLLS FGSKRDFEKQ GFYIANGLFP LLNEELRVDN
QEKVHSMKYK IDNEGLFTRH EQLEKDQTTR WLYHEEETII VGSDRKFPWR LRGPFGASAT
SYGAVGENYI LSTGQGSRMA GGSWINTGEG GVAPEHLESG VDVVAQIGPG LFGFRDDEGN
FSIDEFKCKA QEPNIKAFEL KFGQGAKIRG GHLEGSKVTT KVATIRKVPV GQTINSPNRF
PFLHNALETL EFIKMLQDEG GKPVGIKIVV GYPSSLDEFF EAMNHLKIYP DFITVDGGEG
GTGATYKSMA DTMGLPLYPA LIAVIDKAFQ FGIRNKLRIF ASGKLISADK IAIALAIGAD
AVNSARGFMI ANGCIMALQC HTGKCPTGVT TTDPKYQEAL VPEEKKWRVM NYIINVRHGL
FALAAACGID SPRKFTRDHI VFKDVDGKII KLSELFPIPD SSAE
//
