ID A0A0F0H372_9ACTN Unreviewed; 351 AA.
AC A0A0F0H372;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Iron-sulfur protein {ECO:0000313|EMBL:KJK49935.1};
GN ORFNames=UK14_14360 {ECO:0000313|EMBL:KJK49935.1};
OS Streptomyces sp. NRRL F-4428.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK49935.1, ECO:0000313|Proteomes:UP000033569};
RN [1] {ECO:0000313|EMBL:KJK49935.1, ECO:0000313|Proteomes:UP000033569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK49935.1,
RC ECO:0000313|Proteomes:UP000033569};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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:KJK49935.1}.
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DR EMBL; JYJI01000107; KJK49935.1; -; Genomic_DNA.
DR RefSeq; WP_045322276.1; NZ_JYJI01000107.1.
DR AlphaFoldDB; A0A0F0H372; -.
DR PATRIC; fig|1609137.3.peg.3212; -.
DR OrthoDB; 502624at2; -.
DR Proteomes; UP000033569; 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:UP000033569};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..351
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039032740"
FT DOMAIN 49..148
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 268..351
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 351 AA; 37473 MW; 9A24175766ADF162 CRC64;
MRRALAVTTA TAVAGAAWAA RRSLNRRIGN SPLWPLPALE VPVSGHSPRR PLRALIVSRV
QPAQDVLELT LESPELPAWT PGAHVDVTLP SGLVRQYSLC GDPADTGRYR IAIRLVEDGR
GGSREAHAQL VEGAELQVRP PRNRFELLPA PSYVFVAGGI GITPILPMLR AATAAGADWT
LLYGGRSLDS MPFLDDLAVY GDRVTVLPED EVGLPDLAPL ARTAPGTLVY CCGPEPMMLA
VTEAAREPAA VHLERFAPSA APAPARAFTV ELRRSGRVVE VGAGESTLAA VRRELPGTPY
SCGQGFCGTC QHRVLAGEVD HRDDLLTDPE RADSMLLCVS RAKGDRLALD L
//
