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Entry: A0A1C7N6F5_9FUNG
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ID   A0A1C7N6F5_9FUNG        Unreviewed;       657 AA.
AC   A0A1C7N6F5;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial {ECO:0000256|RuleBase:RU362051};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051};
GN   Name=sdh1 {ECO:0000313|EMBL:OBZ84735.1};
GN   ORFNames=A0J61_07214 {ECO:0000313|EMBL:OBZ84735.1};
OS   Choanephora cucurbitarum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC   Choanephora.
OX   NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ84735.1, ECO:0000313|Proteomes:UP000093000};
RN   [1] {ECO:0000313|EMBL:OBZ84735.1, ECO:0000313|Proteomes:UP000093000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ84735.1,
RC   ECO:0000313|Proteomes:UP000093000};
RA   Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT   "Choanephora cucurbitarum.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH)
CC       that is involved in complex II of the mitochondrial electron transport
CC       chain and is responsible for transferring electrons from succinate to
CC       ubiquinone (coenzyme Q). {ECO:0000256|RuleBase:RU362051}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC         Evidence={ECO:0000256|RuleBase:RU362051};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362051};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (eukaryal route): step 1/1.
CC       {ECO:0000256|RuleBase:RU362051}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU362051}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU362051}; Matrix side
CC       {ECO:0000256|RuleBase:RU362051}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040,
CC       ECO:0000256|RuleBase:RU362051}.
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:OBZ84735.1}.
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DR   EMBL; LUGH01000476; OBZ84735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C7N6F5; -.
DR   SMR; A0A1C7N6F5; -.
DR   STRING; 101091.A0A1C7N6F5; -.
DR   InParanoid; A0A1C7N6F5; -.
DR   OrthoDB; 551958at2759; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000093000; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; 4.10.80.40; succinate dehydrogenase protein 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; IPR003952; FRD_SDH_FAD_BS.
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   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   NCBIfam; TIGR01816; sdhA_forward; 1.
DR   NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
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.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU362051};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR611281-4};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362051};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362051};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362051};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093000};
KW   Transit peptide {ECO:0000256|RuleBase:RU362051};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051};
KW   Ubiquinone {ECO:0000313|EMBL:OBZ84735.1}.
FT   DOMAIN          72..467
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          522..657
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   MOD_RES         108
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ   SEQUENCE   657 AA;  71701 MW;  46C3DF3F9A2D40B7 CRC64;
     MLKFLQSSSN KALRTTRNLL NLCLDSNAGR MTSRGFHHAK PAMQVMANNP LRAKEANGPI
     ASQYPVIDHE YDAVVVGAGG AGLRAAFGLA EAGLNTACIT KLFPTRSHTV AAQGGINAAL
     GNMTEDDWRW HMYDTVKGSD WLGDQDAIHY MCREAPSTVI ELENYGVPFS RTPEGKIYQR
     AFGGQSLKYG KGGQAYRCAA VADRTGHAIL HTLYGQSLRH NTNYFIEYFA LDLIMEDGEC
     KGVIALNMED GTIHRFRSHK TVLATGGYGR AYFSCTSAHT CTGDGNAMVA RAGLPLQDLE
     FVQFHPTGIY GSGCLITEGS RGEGGYLVNS AGERFMERYA PTAKDLASRD VVSRAMTMEI
     KAGRGVGAEK DHIFLQLHHL PPSVLHERLP GISETAAIFA GVDVTKEPIP VLPTVHYNMG
     GIPTRYTGEV IKVNEKGEDE VVPGLYAAGE AACVSVHGAN RLGANSLLDI VVFGRAVAHH
     IAETLEPNTP LKPFAADAGA KTLANLDQLR NATGPKRTSE IRLNMQKVMQ SDAAVFRTQE
     TLDEGVVKID KVWNSFKDVG VTDRGMIWNT DLVETLELQN LLTCASQTMH SAAVRKESRG
     AHARDDFTER DDENWMKHTL SYQNQETGEV TLSYRSVTDT TLDEAECKPV PPFARVY
//
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