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Database: UniProt
Entry: Q1R6C0_ECOUT
LinkDB: Q1R6C0_ECOUT
Original site: Q1R6C0_ECOUT 
ID   Q1R6C0_ECOUT            Unreviewed;       472 AA.
AC   Q1R6C0;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Glutamate synthase small subunit {ECO:0000313|EMBL:ABE09094.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:ABE09094.1};
GN   Name=gltD {ECO:0000313|EMBL:ABE09094.1};
GN   OrderedLocusNames=UTI89_C3650 {ECO:0000313|EMBL:ABE09094.1};
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE09094.1, ECO:0000313|Proteomes:UP000001952};
RN   [1] {ECO:0000313|EMBL:ABE09094.1, ECO:0000313|Proteomes:UP000001952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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DR   EMBL; CP000243; ABE09094.1; -; Genomic_DNA.
DR   RefSeq; WP_000081665.1; NZ_CP064825.1.
DR   AlphaFoldDB; Q1R6C0; -.
DR   KEGG; eci:UTI89_C3650; -.
DR   HOGENOM; CLU_000422_3_3_6; -.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR006006; GltD-like.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   NCBIfam; TIGR01318; gltD_gamma_fam; 1.
DR   PANTHER; PTHR42783; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR42783:SF3; 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; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:ABE09094.1}.
FT   DOMAIN          38..69
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   472 AA;  51987 MW;  8F03A92CDFA36E9F CRC64;
     MSQNVYQFID LQRVDPPKKP LKIRKIEFVE IYEPFSEGQA KAQADRCLSC GNPYCEWKCP
     VHNYIPNWLK LANEGRIFEA AELSHQTNTL PEVCGRVCPQ DRLCEGSCTL NDEFGAVTIG
     NIERYINDKA FEMGWRPDMS GVKQTGKKVA IIGAGPAGLA CADVLTRNGV KAVVFDRHPE
     IGGLLTFGIP AFKLEKEVMT RRREIFTGMG IEFKLNTEVG RDVQLDDLLS DYDAVFLGVG
     TYQSMRGGLE NEDADGVYAA LPFLIANTKQ LMGFGETNDE PFVSMEGKRV VVLGGGDTAM
     DCVRTSVRQG AKHVTCAYRR DEENMPGSRR EVKNAREEGV EFKFNIQPLG IEVNGNGKVS
     GVKMVRTEMG EPDAKGRRRA EIVAGSEHIV PADAVIMAFG FRPHNMEWLA KHSVELDSQG
     RIIAPEGSDN AFQTSNPKIF AGGDIVRGSD LVVTAIAEGR KAADGIMNWL EV
//
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