ID A0A0J7ZKX8_STRVR Unreviewed; 312 AA.
AC A0A0J7ZKX8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:KMS76671.1};
GN ORFNames=ACM01_02100 {ECO:0000313|EMBL:KMS76671.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS76671.1, ECO:0000313|Proteomes:UP000037432};
RN [1] {ECO:0000313|EMBL:KMS76671.1, ECO:0000313|Proteomes:UP000037432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS76671.1,
RC ECO:0000313|Proteomes:UP000037432};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUN-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:KMS76671.1}.
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DR EMBL; LFNT01000002; KMS76671.1; -; Genomic_DNA.
DR RefSeq; WP_048579271.1; NZ_LGUR01000117.1.
DR AlphaFoldDB; A0A0J7ZKX8; -.
DR PATRIC; fig|1938.3.peg.12; -.
DR OrthoDB; 502624at2; -.
DR Proteomes; UP000037432; 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}.
FT DOMAIN 1..105
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 227..312
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 312 AA; 33573 MW; 0C3B0C2BE2D3BAAF CRC64;
MTVYEAELVV ARREFAADGV LALTLRHPLG EELPAWEPGA HIDVVLGPEL ERQYSLCGDP
ADRSAWRIAV LREPDGRGGS AHVHEELGQG GKVRVRGPRN HFALRPAPRY RFIAGGIGIT
PILPMLAAAE SAGAEWTLLY GGRTRRSMAF AEELSRYGGD RVTVAPQDET GLLDLASVLD
DVPEGTLVYC CGPGPLLDAV EARCPAGLLH VERFAPKEQE DGTNTEFEVE LAQSGRTLTV
PADVSVLDAV RGAGVEVLFS CTEGTCGTCE TDVLEGTPDH RDSVLTAEEQ ESGETMMICV
SRCRGKRLVL DL
//
