ID   A0A1C4XFP6_MICEC        Unreviewed;       640 AA.
AC   A0A1C4XFP6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Succinate dehydrogenase / fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:SCF07265.1};
GN   ORFNames=GA0070618_3012 {ECO:0000313|EMBL:SCF07265.1};
OS   Micromonospora echinospora (Micromonospora purpurea).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1877 {ECO:0000313|EMBL:SCF07265.1, ECO:0000313|Proteomes:UP000198253};
RN   [1] {ECO:0000313|EMBL:SCF07265.1, ECO:0000313|Proteomes:UP000198253}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43816 {ECO:0000313|EMBL:SCF07265.1,
RC   ECO:0000313|Proteomes:UP000198253};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR630664-51};
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DR   EMBL; LT607413; SCF07265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4XFP6; -.
DR   InParanoid; A0A1C4XFP6; -.
DR   OrthoDB; 9805351at2; -.
DR   Proteomes; UP000198253; Chromosome i.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal 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; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|PIRSR:PIRSR630664-51};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR630664-
KW   51}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          11..432
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          488..600
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        323
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   BINDING         16..21
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         39..54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         229
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         389
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         416
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         426
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         431..432
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
SQ   SEQUENCE   640 AA;  70378 MW;  17B9C1647B9B1D05 CRC64;
     MTTRIERHHY DVVVIGAGGA GLRAAIEARL AGKKTAIISK SLFGKAHTVM AEGGAAAAMG
     NVNSRDNWQV HFRDTMRGGK FLNNFRMAEL HAKESPQRIW ELETYGALFD RTKDGKISQR
     NFGGHEYPRL AHVGDRTGLE LIRTLQQKIV SLQQEDKKEF GSYDARIKVF AETTITELLL
     DGDRVAGAFG YYRESGEFVL FEAPAVVLAT GGVGRSYKVT SNSWEYTGDG HALALRAGAT
     LINMEFLQFH PTGMVWPVSV KGILVTESVR GDGGVLKNSE GKRFMFDYVP DVFRKQYADN
     EAEADRWYKD PDNNRRPPEL LPRDEVARAI NSEVKAGRGT PAGGVYLDIA SRLPAEEIRR
     RLPSMYHQFK ELADVDITKE PMEVGPTCHY VMGGVEVDPD SGAASGNVRG LFAAGEVSGG
     MHGSNRLGGN SLSDLLVFGK RAGGHAATYA DQLPSRPKVS VDAVEAAVET ALAPLQRDTG
     ENPYTLQQDL QAVMGDLVGI IRREGELADA LVRLAELRER VAKVSAAGGR RYNPGWHLAL
     DLRNMLVVSE CTAKAALERQ ESRGGHTRED FPKMDPTWRR VNLVCSLDGD TVRLEHKPLP
     KMRAELISLF DRAELAKYLT DEELADFDAL VADAHAEEAK
//