ID A0A3A9VEE4_9FLAO Unreviewed; 351 AA.
AC A0A3A9VEE4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Flavodoxin reductase {ECO:0000313|EMBL:AXT18559.1};
GN ORFNames=D1817_01360 {ECO:0000313|EMBL:AXT18559.1};
OS Flavobacteriaceae bacterium.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1871037 {ECO:0000313|EMBL:AXT18559.1, ECO:0000313|Proteomes:UP000260281};
RN [1] {ECO:0000313|EMBL:AXT18559.1, ECO:0000313|Proteomes:UP000260281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU392 {ECO:0000313|EMBL:AXT18559.1,
RC ECO:0000313|Proteomes:UP000260281};
RA Song W., Thomas T., Edwards R.;
RT "Complete genome sequences of pooled genomic DNA from 10 marine bacteria
RT using PacBio sequencing.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP031964; AXT18559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9VEE4; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000260281; Chromosome.
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; 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; PR00410; PHEHYDRXLASE.
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:UP000260281}.
FT DOMAIN 2..106
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 261..351
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 351 AA; 39129 MW; 8017AEEAEC3F714A CRC64;
MVHFHKLTIK EIVKETANAV TISFSIPEHL NEVFTFKAGQ YITIKTIING EELRRDYSLC
VDAKSREFKV AVKAVENGTF SMYANNDLKI GDVLEVSEPN GRFIFTPDDL QSRTIVAFAA
GSGITPIMSI IKTLLKQEPS SKFILIYGNK TPKDTIFYNE LLALQSQFEN RLDIHFVFSQ
SNIEGSLFGR IETSTVNYII KNKYKDVVID AFYLCGPEAM TKNVNSILNE NGIENDVIFY
ELFTTPVSDT TENTTISEGK TQITILVDEE ESTFLMSQKD SVLDAALAQK IDAPYSCQGG
ICSSCLARIT EGKATMRQNN ILTENELAEG LVLTCQAHPT TPTIIVDYDD V
//