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Database: UniProt
Entry: A0A091FL97_CORBR
LinkDB: A0A091FL97_CORBR
Original site: A0A091FL97_CORBR 
ID   A0A091FL97_CORBR        Unreviewed;       643 AA.
AC   A0A091FL97;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU362051};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU362051};
DE   Flags: Fragment;
GN   ORFNames=N302_14450 {ECO:0000313|EMBL:KFO62090.1};
OS   Corvus brachyrhynchos (American crow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO62090.1, ECO:0000313|Proteomes:UP000052976};
RN   [1] {ECO:0000313|EMBL:KFO62090.1, ECO:0000313|Proteomes:UP000052976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO62090.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000030,
CC         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|ARBA:ARBA00004788}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004443}; Matrix side
CC       {ECO:0000256|ARBA:ARBA00004443}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040,
CC       ECO:0000256|RuleBase:RU362051}.
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DR   EMBL; KK719225; KFO62090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091FL97; -.
DR   STRING; 85066.A0A091FL97; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000052976; 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   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:UP000052976};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN          42..436
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          491..643
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        319
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   MOD_RES         78
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO62090.1"
FT   NON_TER         643
FT                   /evidence="ECO:0000313|EMBL:KFO62090.1"
SQ   SEQUENCE   643 AA;  70514 MW;  66135524B5F924E9 CRC64;
     WPAACQAPAR NLHFTVYGKK NASTKVSDSI STQYPVVDHE FDAVVVGAGG AGLRAAFGLS
     EAGFNTACVT KLFPTRSHTV AAQGGINAAL GNMEDDNWRW HFYDTVKGSD WLGDQDAIHY
     MTEQAPAAVI ELENYGMPFS RTEEGKIYQR AFGGQSLQFG KGGQAHRCCC VADRTGHSLL
     HTLYGRSLRY DTSYFVEYFA LDLLMENGEC RGVIALCIED GTIHRFRAKN TVIATGGYGR
     TYFSCTSAHT STGDGTAMVT RAGLPCQDLE FVQFHPTGIY GAGCLITEGC RGEGGILINS
     QGERFMERYA PVAKDLASRD VVSRSMTIEI REGRGCGPEK DHVYLQLHHL PPQQLATRLP
     GISETAMIFA GVDVTKEPIP VLPTVHYNMG GIPTNYKGQV ITHVNGEDKV VPGLYACGEA
     ASASVHGANR LGANSLLDLV VFGRACALTI ANTCKPGEPV PPIKPNAGEE SVANLDKLRF
     ADGSIRTSEA RLNMQKAMQN HAAVFRTGSV LQEGCEKLSQ IYGDLAHLKT FDRGIVWNTD
     LVETLELQNL MLCALQTIYA AEARKESRGA HAREDYKLRV DEFDYSKPLQ GQQRKPFEEH
     WRKHTLSYVD IPTGKVTLKY RPVIDRTLNE QDCQTVPPAI RSY
//
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