ID   C0INP0_9BACT            Unreviewed;       614 AA.
AC   C0INP0;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:ACN58926.1};
GN   ORFNames=AKSOIL_0084 {ECO:0000313|EMBL:ACN58926.1};
OS   uncultured bacterium BLR7.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=506523 {ECO:0000313|EMBL:ACN58926.1};
RN   [1] {ECO:0000313|EMBL:ACN58926.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18843302; DOI=10.1038/ismej.2008.86;
RA   Allen H.K., Moe L.A., Rodbumrer J., Gaarder A., Handelsman J.;
RT   "Functional metagenomics reveals diverse beta-lactamases in a remote
RT   Alaskan soil.";
RL   ISME J. 3:243-251(2009).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; EU408356; ACN58926.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0INP0; -.
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   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          70..595
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  66170 MW;  EEB624864AA81F2C CRC64;
     MARPSGRCRK RRTRRSDGSP GEGRMAEKKT VSRRDLIKTA GAAGAAVAAG GIVAAPASAQ
     TAPNWDREAD IVIIGSGATG MPAAIVAREA GSSVIIVDAN KDIGGHAICS GANIPLGGGT
     SIQKKFGIKD SPDLVYQDLT DWSVVQPNGA PDYRYNDREI IRAFADNCTA TFEFLLSHDV
     TFVNEKPDGR AGSSHGNSVP RQMHVWAGDW PQVQTGRPTD EAVRKSTSNG NGLMRPLEAS
     ARKLGVDILL EHRMTSIHRE QPKGRVTGIA VTNNGRTLNI RAKKAVIVAT GGFTGNVNFR
     RMFDPRLTEE YCGLAGMPWS NQDGSGEIAS MAVGASLWGL TNFSSELGSG LTKAGKIGCQ
     YGYVNLTWMP GSRVFDEAGA SGLRVRDWQN VITVNMLGKR FYDETGEDFT GNQYNQINPY
     TPNNPVNIKN LKYNPNDYLN AAMAGIGDGQ NGGGPIWAIF DADAAAREKW DTKHPWVDEK
     NGFFFSANSI SELAAKIKMK YQRLPMPSAN LEATVARYNS FVDSGTDEDF GKPKPMYKIA
     KGPFYAAWAM PVIHDTRAGL RINAKCQVMD MDGQVIPNFY CGGESAGGFS MHGLARCLTQ
     GYIAGHAAHA EKAI
//