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Database: UniProt
Entry: A0A117V2B1_9SPHN
LinkDB: A0A117V2B1_9SPHN
Original site: A0A117V2B1_9SPHN 
ID   A0A117V2B1_9SPHN        Unreviewed;       477 AA.
AC   A0A117V2B1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KUR76520.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:KUR76520.1};
GN   Name=gltD {ECO:0000313|EMBL:KUR76520.1};
GN   ORFNames=AQZ50_13160 {ECO:0000313|EMBL:KUR76520.1};
OS   Novosphingobium sp. Fuku2-ISO-50.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR76520.1, ECO:0000313|Proteomes:UP000056630};
RN   [1] {ECO:0000313|EMBL:KUR76520.1, ECO:0000313|Proteomes:UP000056630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR76520.1,
RC   ECO:0000313|Proteomes:UP000056630};
RA   Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA   Glaeser S.;
RT   "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM 27930), a
RT   Novosphingobium acidiphilum related species isolated from a surface water
RT   sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:KUR76520.1}.
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DR   EMBL; LLZR01000018; KUR76520.1; -; Genomic_DNA.
DR   RefSeq; WP_067746933.1; NZ_KQ954294.1.
DR   AlphaFoldDB; A0A117V2B1; -.
DR   STRING; 1739114.AQZ50_13160; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000056630; Unassembled WGS sequence.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR006005; Glut_synth_ssu1.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR   PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KUR76520.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000056630}.
FT   DOMAIN          26..130
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          145..458
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   477 AA;  52398 MW;  03C21AAE1AEC5388 CRC64;
     MGKPTGFLET DRHDRGYDAP AERLKHYREF IVPHDDATLR GQAARCMNCG IPYCHNGCPV
     NNQIPDWNHL VYEADWRDAL DNLHSTNNFP EFTGRICPAP CEAACTLNIV DQPVTIKSIE
     CAIVDKGWRE GWIEPQVPAK KSGRSVAVVG SGPAGLACAQ QLARAGHSVT VFEKSDRVGG
     LLRYGIPDFK MEKHLINRRM VQMMAEGVEF RTSVEVGVTV SMASLRENFD VVVMAGGSED
     PRPLLIPGFE LPGVRFAMEF LTQQNKRNAG DDEIRAAPRG SLLATGKHVV VVGGGDTGSD
     CVGTSNRQGA LSVTQLEIMP RPPEKEDKAL TWPDWPLKLR TSSSHEEGVE REFAVLTKRV
     TGETEVTGLE CVRVEWVGGK MQEVPGSEFT LKADLILLAM GFVGPRKQGL IEQSGVDLDP
     RGNVRATMQD YKTSVENVFS CGDMRRGQSL VVWAIREGRQ CARAVDEALM GVSELPR
//
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