ID C0BL19_9BACT Unreviewed; 359 AA.
AC C0BL19;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:EEG43789.1};
GN ORFNames=Flav3CDRAFT_1267 {ECO:0000313|EMBL:EEG43789.1};
OS Flavobacteria bacterium MS024-3C.
OC Bacteria; Bacteroidota; Flavobacteriia.
OX NCBI_TaxID=487797 {ECO:0000313|EMBL:EEG43789.1, ECO:0000313|Proteomes:UP000003631};
RN [1] {ECO:0000313|EMBL:EEG43789.1, ECO:0000313|Proteomes:UP000003631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS024-3C {ECO:0000313|EMBL:EEG43789.1,
RC ECO:0000313|Proteomes:UP000003631};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Woyke T., Xie G., Copeland A., Gonzalez J., Han C., Kiss H., Saw J.,
RA Senin P., Chatterji S., Cheng J.-F., Eisen J.A., Sieracki M.E.,
RA Stepanauskas R.;
RT "Assembling the metagenome, one cell at a time.";
RL Submitted (AUG-2008) 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:EEG43789.1}.
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DR EMBL; ABVW01000001; EEG43789.1; -; Genomic_DNA.
DR AlphaFoldDB; C0BL19; -.
DR STRING; 487797.Flav3CDRAFT_1267; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000003631; 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; cd06214; PA_degradation_oxidoreductase_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; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00371; FPNCR.
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:UP000003631}.
FT DOMAIN 2..110
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 269..359
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 359 AA; 38183 MW; 91FDDA5AE2D6C239 CRC64;
MTHFYPLNVS QVDNLTTQSV AISFEIPADL QSNFAFKAGQ YITIKHTIHG KEVRRAYSIS
SAPVVSGPQN SVTVGIKEVA GGAFSPYANR YIQKGDILEV MPPQGRFLYE PTTAAVHHLG
VAAGSGITPI LSIAKSVLAS GPEHSFTLIY GNKSPQDVMF SNEIEALQTA YPTQFKVQWV
YSQAKEDQAL FGRIDTAAIN YVLKNTDTAP FDGAYLCGPE GMIKTATETL EKAGLSKDHI
HYELFTVATE STSDSGEAAS GGALAVGKIA VEVTVDGETA SLEMDAKTIL LDAIIKADID
APYSCQGGVC SSCICKVTKG SATMIKNQIL TDSEIADGLV LSCQAMVTST EIAVDFDDV
//
