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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//