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Database: UniProt
Entry: A0A0S4IZL1_BODSA
LinkDB: A0A0S4IZL1_BODSA
Original site: A0A0S4IZL1_BODSA 
ID   A0A0S4IZL1_BODSA        Unreviewed;      1200 AA.
AC   A0A0S4IZL1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=NADH-dependent fumarate reductase, putative {ECO:0000313|EMBL:CUG28369.1};
GN   ORFNames=BSAL_76915 {ECO:0000313|EMBL:CUG28369.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG28369.1, ECO:0000313|Proteomes:UP000051952};
RN   [1] {ECO:0000313|Proteomes:UP000051952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) 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; CYKH01000732; CUG28369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4IZL1; -.
DR   VEuPathDB; TriTrypDB:BSAL_76915; -.
DR   OMA; NWRYVRD; -.
DR   OrthoDB; 169293at2759; -.
DR   Proteomes; UP000051952; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd06183; cyt_b5_reduct_like; 1.
DR   Gene3D; 3.10.520.10; ApbE-like domains; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR024932; ApbE.
DR   InterPro; IPR003374; ApbE-like_sf.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF02424; ApbE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   SUPFAM; SSF143631; ApbE-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT   DOMAIN          942..1047
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   1200 AA;  130611 MW;  1BFC1BF65A352BBA CRC64;
     MADSRTSASV VIVDPVKAAE ERDRLARAQL NDTNPGAKPM FVASGVEHTV PFTVKVVFPD
     GIAKEKIEAD VSGVLRDVFG LVDKHLNNFN PASEISIVNQ LPAHIIHQMS PALAAVVHCS
     LSVFANARGH FDIACGPAAN FAKTFLQQPS NAGKDYQSDP QFVELLAISS LSGGFKFHDG
     DHTLEKRDAR AYLDLGGVSK GYGVDAVIER LAVLGYQDTF FDWGGDCRGS GRNALGEKWA
     VAVLRPPPMK DLLPVQDKSR VSNLKPDAPL IRVCHLDNEA LATSGDYENL FQGNDGQLYS
     TQWSTSTKRF LTPSQKHISQ ATVKCFTAMY ADALATATLH MHFFAPVRMI MDHWRWKRNA
     VTDYTMFVRD GERVSKMQEL SKESVEMRQK RISDTLPARV VIVGGGLAGL CAAIEAASCG
     AQVILLEKST RLGGNSAKAT SGINGWGSRT QAKQGVIDGD KFFERDTYLS GLGGTCDPGL
     VKLLSVKSGE AIHWLSSFGI PLTVLSQLGG HSRKRCHRAP DLKDGTKKKK SGEAIHWLSS
     FGIPLTVLSQ LGGHSRKRCH RAPDLKDGTP VPIGYTIMKT LEAYIRSQLS RQVTIMTESA
     VTSLIRQIIP LPDNTQRIKV LGVTFRPKNA EEDVTVYSDA VILATGGFSN DQTTGSLMRE
     FAPHLFGQPT TNGPFATGDG VKMARSIGAQ LIDMDKVQLH PTGFVDPKDP ANPTKFLGPE
     ALRGSGGILI NAFGERFVNE LDLRSVVSAA INEQNTEYPN SNGCKVAFCV LNAEAAKLFG
     INALQFYWKK QGLFSFVDDT DQLAKLIGCP LDTLRATLAA YQHTSSAKTA PCPTTGKRVF
     PCVIGNEGPY YVAVITPSIH YTMGGCLISP AAEVQSEFIT TSIFGSRRPI QGLFGAGEVT
     AGVHGENRLG GNSLLECVVF GRIAGDRAAT ILQKKPHALS QDQWSPLILR EIREGADFGQ
     GSRILRFNLP GATQNSGLKL GQFVAIRGEW DGQHLVGYYS PITLPDDHGV IGILVRVDKG
     TLKDWLTAMR PGDAIEMRAC GGLAIDRIPS LRQLQFRKEP IHKITMIAGG TGVAPMIQII
     RAALKRPYID RMQSLDLIYA AEDYSELTYR TIFEKYQNEH RDRFHLTLVL NNPPPRWTGG
     VGFVDKGILS TYVPAPSKDL LIVICGPPMM QRVTKSTLIS MGHVARHVRT VDEDSGPSKL
//
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