ID A0A0M9ZM92_9ACTN Unreviewed; 315 AA.
AC A0A0M9ZM92;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:KOV64018.1};
GN ORFNames=ADK64_17900 {ECO:0000313|EMBL:KOV64018.1};
OS Streptomyces sp. MMG1121.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV64018.1, ECO:0000313|Proteomes:UP000037687};
RN [1] {ECO:0000313|Proteomes:UP000037687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1121 {ECO:0000313|Proteomes:UP000037687};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KOV64018.1}.
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DR EMBL; LGDV01000187; KOV64018.1; -; Genomic_DNA.
DR RefSeq; WP_053660065.1; NZ_LGDV01000187.1.
DR AlphaFoldDB; A0A0M9ZM92; -.
DR STRING; 1415544.ADK64_17900; -.
DR PATRIC; fig|1415544.3.peg.3844; -.
DR OrthoDB; 502624at2; -.
DR Proteomes; UP000037687; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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 CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000037687}.
FT DOMAIN 6..107
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 230..315
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 315 AA; 33528 MW; CFD92B1E9693CB79 CRC64;
MSTTEDPQMD LLVRRMTWEA EGVLSVELTH PDGKPLPVWA PGAHLDLHVG GYVRQYSLCG
DPEDTGVYRL GILNEPSSRG GSRHVHTTLR PGQTVRVAGP RNHFPLDRAA SYVFIAGGVG
ITPILAMARQ AQRDGIPFRL VHGGRSRASM AFGGELAALD GGEVTLVPQD EQGHIDLARA
LDGLPSDTLV YCCGPEPLLK AVEEAVPEGQ LRIERFAAPV VERHGDDSAF EVECRTSGVT
LNVGGGTSVL EAAENAGLTV SSSCREGICG SCETRVLAGT PDHRDFLLSE AEHATGGTMM
ICVSRCASDR LVLDL
//
