ID F4TKG5_ECOLX Unreviewed; 644 AA.
AC F4TKG5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative oxidoreductase, Fe-S subunit {ECO:0000313|EMBL:EGI19842.1};
GN ORFNames=ECJG_01220 {ECO:0000313|EMBL:EGI19842.1};
OS Escherichia coli M718.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=656419 {ECO:0000313|EMBL:EGI19842.1, ECO:0000313|Proteomes:UP000002790};
RN [1] {ECO:0000313|EMBL:EGI19842.1, ECO:0000313|Proteomes:UP000002790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M718 {ECO:0000313|EMBL:EGI19842.1,
RC ECO:0000313|Proteomes:UP000002790};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli M718.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL884130; EGI19842.1; -; Genomic_DNA.
DR AlphaFoldDB; F4TKG5; -.
DR HOGENOM; CLU_000422_3_3_6; -.
DR Proteomes; UP000002790; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd10554; HycB_like; 1.
DR Gene3D; 3.30.70.20; -; 2.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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:SF1; OXIDOREDUCTASE AEGA-RELATED; 1.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 8..37
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 83..112
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 644 AA; 69650 MW; B1ABF3A8A64076E3 CRC64;
MKGMQMNKFI AAEAAECIGC HACEIACAVA HNQENWPLSH SDFRPRIHVV GKGQAANPVA
CHHCNNAPCV TACPVNALTF QSDSVQLDEQ KCIGCKRCAI ACPFGVVEMV DTIAQKCDLC
NQRSSGTQAC IEVCPTQALR LMDDKGLQQI KVARQRKTAA GKASSDAQPS RSAALLPVNS
RKGADKISAS ERKTHFGEIY CGLDPLQATY ESDRCVYCAE KANCNWHCPL HNAIPDYIRL
VQEGNIIEAA ELCHQTSSLP EICGRVCPQD RLCEGACTLK DHSGAVTIGN LERYITDTAL
AMGWRPDVSK VVPRSEKVAV IGAGPAGLGC ADILARAGVQ VDVFDRHPEI GGMLTFGIPP
FKLDKTVLSQ RREIFTAMGI DFHLNCEIGR DITFSDLTSE YDAVFIGVGT YGMMRADLPH
EDAPGVIQAL PFLTAHTRQL MGLPESEEYP LTDVEGKRVV VLGGGDTTMD CLRTSIRLNA
ASVTCAYRRD EVSMPGSRKE VVNAREEGVE FQFNVQPQYI ACDEDGRLTA VGLIRTAMGE
PGPDGRRRPR PVAGSEFELP ADVLIMAFGF QAHAMPWLQG SGIKLDKWGL IQTGDVGYLP
TQTHLKKVFA GGDAVHGADL VVTAMAAGRQ AARDMLTLFD TKAS
//