ID A0A494UTR8_9ACTN Unreviewed; 286 AA.
AC A0A494UTR8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Fe-S-binding domain-containing protein {ECO:0000313|EMBL:AYL38822.1};
GN ORFNames=CNQ36_27530 {ECO:0000313|EMBL:AYL38822.1};
OS Streptomyces fungicidicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68203 {ECO:0000313|EMBL:AYL38822.1, ECO:0000313|Proteomes:UP000282170};
RN [1] {ECO:0000313|EMBL:AYL38822.1, ECO:0000313|Proteomes:UP000282170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TXX3120 {ECO:0000313|EMBL:AYL38822.1,
RC ECO:0000313|Proteomes:UP000282170};
RA Zhang H., Hu S., Xu J., He Z.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP023407; AYL38822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494UTR8; -.
DR KEGG; sfug:CNQ36_27530; -.
DR Proteomes; UP000282170; Chromosome.
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:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR PANTHER; PTHR24960:SF88; PHOTOSYSTEM I IRON-SULFUR CENTER; 1.
DR PANTHER; PTHR24960; PHOTOSYSTEM I IRON-SULFUR CENTER-RELATED; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000282170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 11..89
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 188..216
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 230..286
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 286 AA; 31290 MW; E5F2CABC172EB2B7 CRC64;
MTVTPLGIPR RLLEFTLDGE PVRAPEGSTI LDACRAAGKD VPTLCEGDTL TPKNACRVCV
VEVEGSRTLV PACSRRAEPG MEVRTGTERA RHSRKVVLEL LASSVDLSTT PRVAGWLKEY
EAKPDRFGPD AARVDEEPRV DNDLYVRDYG KCILCYKCVD ACGDQWQNTF AISVAGRGFD
ARIAVEHDAP LTDSACVYCG NCIEVCPTGA LSFKSEFDMR AAGTWDESRQ SETTTVCAYC
GVGCNLTLHV QDNEIVKVTS PHDNPVTHGN LCIKGRFGYQ HVQNRD
//
