ID   I3TSS2_TISMK            Unreviewed;       452 AA.
AC   I3TSS2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Putative fumarate reductase/succinate dehydrogenase flavoprotein {ECO:0000313|EMBL:AFK55810.1};
GN   Name=ifcA {ECO:0000313|EMBL:AFK55810.1};
GN   OrderedLocusNames=TMO_a0407 {ECO:0000313|EMBL:AFK55810.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM1 {ECO:0000313|EMBL:AFK55810.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK55810.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK55810.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM1 {ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP003237; AFK55810.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3TSS2; -.
DR   KEGG; tmo:TMO_a0407; -.
DR   PATRIC; fig|1110502.3.peg.4056; -.
DR   HOGENOM; CLU_011398_4_3_5; -.
DR   Proteomes; UP000005258; Plasmid pTM1.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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; PF00890; FAD_binding_2; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Plasmid {ECO:0000313|EMBL:AFK55810.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258}.
FT   DOMAIN          8..434
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   452 AA;  46710 MW;  73671DCFBDC90C39 CRC64;
     MEAGTLPVVV VGAGAAGLTA ALAVRDAGAP VVVLERDAVP AGNTALTLGM LPGAGTRFQR
     AAGIEDDAAL FLADILAKAK GRTDHDLARA ITAASGPAVE WLADRHGVAF ELLDDILYPG
     HSRHRYHVPP DRTGTAFMAD LLAAASRAGV QLVTEAIVEA PETDADGRVT GVVWRDDAGR
     RHHTACRALV LASGGYGADP EAVARYIPEM AGAVHGGHHG SRGDALVWGE RLGAALVDPG
     SYQGHCVADG PNLPVTWALI IRGGFQVGSD GRRFSNEMSG YSEQAHAVAA QPGGVAWTIY
     DRRCEEPALT FRDYHRVLES GVVTTGETVD DLARACGLPV GALAETLAEV EAVTRGHAPD
     RFGRVFDGTP PLQPPFRAVR VRAALFHTQG GLAIDTRARV LDRAGRPLPG LFAAGGAARG
     LSGPAAWGYL GGNGLLTAVV PGRFAGTAAA AC
//