ID A0A0T5NTS1_9RHOB Unreviewed; 445 AA.
AC A0A0T5NTS1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KRS12118.1};
GN ORFNames=XM53_12795 {ECO:0000313|EMBL:KRS12118.1};
OS Roseovarius atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS12118.1, ECO:0000313|Proteomes:UP000051295};
RN [1] {ECO:0000313|EMBL:KRS12118.1, ECO:0000313|Proteomes:UP000051295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R12B {ECO:0000313|EMBL:KRS12118.1,
RC ECO:0000313|Proteomes:UP000051295};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius sp.R12b.";
RL Submitted (APR-2015) 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:KRS12118.1}.
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DR EMBL; LAXJ01000012; KRS12118.1; -; Genomic_DNA.
DR RefSeq; WP_057793912.1; NZ_LAXJ01000012.1.
DR AlphaFoldDB; A0A0T5NTS1; -.
DR STRING; 1641875.XM53_12795; -.
DR PATRIC; fig|1641875.4.peg.353; -.
DR OrthoDB; 9795032at2; -.
DR Proteomes; UP000051295; Unassembled WGS sequence.
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; IPR043578; GltB_archl_type.
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; 2.
DR PIRSF; PIRSF500061; GOGAT_lg2_archl; 1.
DR PIRSF; PIRSF006429; GOGAT_lg_2; 1.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
FT DOMAIN 78..335
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
FT DOMAIN 359..407
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
FT REGION 114..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 47435 MW; 704A9E3AF1D3E931 CRC64;
MSDNQKSAPR TLPRYSNTFT PDVNAEIRRA AATGIYDIRG GGAKRKVPHF DDLVFLGASM
SRYPLEGYRE RCDTNVVLGT RYAKKPIELK IPITIAGMSF GALSAQAKEA LGRGASMAGT
STTTGDGGMT PEERGQSKTL VYQYLPSRYG MNPVDLRKAD AIEVVVGQGA KPGGGGMLLG
QKISDRVAEM RTLPKGIDQR SACRHPDWTG PDDLEIKILE LREITGWEKP IYVKVGAARP
FFDTTLAVKA GADVVVIDGM QGGTAATQDV FIEHVGIPTL ACIREAVAAL QELGMHRKVQ
LIVSGGIRTG ADVAKALALG ADAVSIGTAA MVAIGDNDPK WEAEYNALGS TAGAYDDWHE
GRDPAGISTQ DPELSKRLDP VEAGRRLNNY LQVLTLEAQT LARACGKNHV HNLEPEDLQA
LTVEAAAMAR VPLAGTSWIP GQGGM
//
