ID N6Y0M4_9RHOO Unreviewed; 344 AA.
AC N6Y0M4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Ferredoxin:oxidoreductase FAD/NAD(P)-binding:oxidoreductase FAD-binding region {ECO:0000313|EMBL:ENO75713.1};
GN ORFNames=C664_16390 {ECO:0000313|EMBL:ENO75713.1};
OS Thauera sp. 63.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=497321 {ECO:0000313|EMBL:ENO75713.1, ECO:0000313|Proteomes:UP000013007};
RN [1] {ECO:0000313|EMBL:ENO75713.1, ECO:0000313|Proteomes:UP000013007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63 {ECO:0000313|EMBL:ENO75713.1,
RC ECO:0000313|Proteomes:UP000013007};
RA Liu B., Shapleigh J.P., Frostegard A.H.;
RT "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL Submitted (SEP-2012) 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:ENO75713.1}.
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DR EMBL; AMXC01000027; ENO75713.1; -; Genomic_DNA.
DR AlphaFoldDB; N6Y0M4; -.
DR eggNOG; COG0543; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR Proteomes; UP000013007; 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; cd06190; T4MO_e_transfer_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; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 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}.
FT DOMAIN 8..100
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 108..207
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 344 AA; 37307 MW; B1B7E302E3961826 CRC64;
MTEGAMSDQA RITNKKDGST FVHNAGDTVL RAALRAGVGM SYECNSGGCG GCKFELIEGE
VDTLWAEAPG LSERDKQRGR HLACQCIPRG DITISAPCAT EYAPPRPPQR QSARLAAVRD
ITHDIREFRF VAAVGANFLP GQYAMLDLPG VNGSRAYSLS NTANASSEWH FQIRRVPHGS
GTKVLFDRLA KGDEVGLDGP YGVAYLRTDS ARDLVCVAGG SGLAPMISIA RGAVEAGMLG
ERMLYFFYGA RTARDVCGED MLASLEGFGD RIRFIPVVSQ PGEGEQWTGA TGYVHAQLEC
VLPQPLSNYE FYFAGPPQMT QALQELLMIG HKVPFGQIHF DRFF
//
