ID A0A0V1AFV3_9BILA Unreviewed; 955 AA.
AC A0A0V1AFV3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 Name=sdha-1 {ECO:0000313|EMBL:KRY23718.1};
GN ORFNames=T12_16634 {ECO:0000313|EMBL:KRY23718.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY23718.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY23718.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY23718.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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|RuleBase:RU362051};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
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:KRY23718.1}.
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DR EMBL; JYDQ01000002; KRY23718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1AFV3; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000054783; 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:0004609; F:phosphatidylserine decarboxylase activity; IEA:InterPro.
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:0008654; P:phospholipid biosynthetic process; 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; IPR003817; PS_Dcarbxylase.
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; PF02666; PS_Dcarbxylase; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
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}; Lyase {ECO:0000256|ARBA:ARBA00023239};
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:UP000054783};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051};
KW Ubiquinone {ECO:0000313|EMBL:KRY23718.1}.
FT DOMAIN 52..447
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 502..643
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 329
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-1"
FT MOD_RES 88
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
FT NON_TER 955
FT /evidence="ECO:0000313|EMBL:KRY23718.1"
SQ SEQUENCE 955 AA; 106843 MW; 0F47F2B7F85034FC CRC64;
MKISEIGKMM SKLSSVNVNL LKRCLFFNPQ AYSSYESRRF ASGYEIVDHT YDAVIVGAGG
AGLRAAMGLV EAGFKTAVLT KLFPTRSHTV AAQGGVNAAL GNMEPDDWRW HFYDTVKGSD
WLGDQDAIHY MCREAPRAVL ELENYGMPFS RTKEGKIYQR AFGGQSLDYG RGGQAHRTCC
VADRTGHSML HTLYGRTLAY DCKYFIEYLA LDLLMNKNRC VGVIAWNLED GKLHRFHSNN
TILATGGYGR AYFSCTSAHT CTGDGTAMVS RAGLPNADME FVQFHPTGIY GAGCLITEGV
RGEGGYLINS KGERFMERYA PNAKDLASRD VVSRAMAIEI REGRGVGAQK DHIYLQLHHL
PTNLIHDRLP GIAETAHIFA GVDCTKEPIP VLPTVHYNMG GIPTNHTAQV LTFKPGSGDQ
IIQGLYAAGE TAAHSVHGAN RLGANSLLDL VIFGRACALT IAKTCKPGEK FPDLPANAGE
RSVANLDKLR QANGTITVAD LRLKMQKTMQ EHASVFRTGE VLQEGCKKME GIYKELENVK
LSDRGLIWNT DLVEAIELQN LMLNAVQTIN CAEARKESRG AHAREDFKQR IDEFDYSKPL
DGQTKLPFEK HWRKHSMVWM DEVTGRTRIE YRPVVDKTLD KAEVDWVQPK VSPADGVVQW
CGKISDGVLS QIKGITYHIN DFFGQVEVPG VDFEDLKTNK KGMRHGSLSD LSYGPGYDTE
KGRKMGDFRL GSSVVLIFEA PADFHFSVSS GQRIKYGEML GDINSQAYNL ESSDVRTRKL
HLQSQAHRTV YAAYYAQFEE YRREEMNEQR PSSFAAKSKQ KISSKNANDI LNHWLQINRP
DLYAFSMLRK QLIQLEYDVN KWPVSLRLNH QQQSGVLKFI FFEINVTDVD IVHLWKLKQQ
FTTHNKFINF RTSPSFPSQG DVSTIAGSWA PFTGAVDPRP YESSLKAQCT RKIHI
//
