ID A0A1F2ZTS3_9PROT Unreviewed; 345 AA.
AC A0A1F2ZTS3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OFW97291.1};
GN ORFNames=A3D94_19015 {ECO:0000313|EMBL:OFW97291.1};
OS Alphaproteobacteria bacterium RIFCSPHIGHO2_12_FULL_66_14.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1797225 {ECO:0000313|EMBL:OFW97291.1, ECO:0000313|Proteomes:UP000176194};
RN [1] {ECO:0000313|EMBL:OFW97291.1, ECO:0000313|Proteomes:UP000176194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFW97291.1}.
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DR EMBL; MEMN01000223; OFW97291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2ZTS3; -.
DR STRING; 1797225.A3D94_19015; -.
DR Proteomes; UP000176194; 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; cd06187; O2ase_reductase_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 3..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 100..199
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 345 AA; 37522 MW; A8FEB9BA1DD00D37 CRC64;
MSFKVRIAQA DRTIDVPTGA TILETALDAG ISYPFGCQSG NCGACKSHLV KGEVTMEGYS
EFALSDEEKE RGLILACRAV PWEECEVAWL EEDDLVVHPR RVLACKVVGL DDATHDIKRV
RLEIVSGGPF DFSAGQFASV TFDGCPPRDY SMANVPGDPI LEFHIRRTVG GATSLHVAGK
LKVGDSVRVE GPFGASYLRE THRGPIIAVA GGSGMAPIKA IVERAVQKSL PQHIYLYFGV
RTERDLYLHD HFKALADRYK NLHFIPVLSE GDGMTRRCGL VHDAVAADFD EVDGCKAYLA
GPPVMVEAAT KLLERRGMRR IDVHADAFYT AAEMASAAKK TGAQQ
//
