(data stored in ACNUC7421 zone)

SWISSPROT: Q75C64_ASHGO

ID   Q75C64_ASHGO            Unreviewed;       633 AA.
AC   Q75C64;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 103.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial {ECO:0000256|RuleBase:RU362051};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051};
GN   ORFNames=AGOS_ACR052W {ECO:0000313|EMBL:AAS51279.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51279.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51279.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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|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|RuleBase:RU362051}.
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DR   EMBL; AE016816; AAS51279.2; -; Genomic_DNA.
DR   RefSeq; NP_983455.2; NM_208808.2.
DR   STRING; 33169.AAS51279; -.
DR   EnsemblFungi; AAS51279; AAS51279; AGOS_ACR052W.
DR   GeneID; 4619580; -.
DR   KEGG; ago:AGOS_ACR052W; -.
DR   HOGENOM; HOG000160475; -.
DR   InParanoid; Q75C64; -.
DR   KO; K00234; -.
DR   OMA; LTCAVQT; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   Gene3D; 3.90.700.10; -; 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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   SUPFAM; SSF46977; SSF46977; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF56425; SSF56425; 1.
DR   TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR   TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75C64.
DR   SWISS-2DPAGE; Q75C64.
KW   Electron transport {ECO:0000256|RuleBase:RU362051};
KW   FAD {ECO:0000256|RuleBase:RU362051};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362051};
KW   Membrane {ECO:0000256|RuleBase:RU362051};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362051};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transit peptide {ECO:0000256|RuleBase:RU362051};
KW   Transport {ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN          47..443
FT                   /note="FAD_binding_2"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          498..633
FT                   /note="Succ_DH_flav_C"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
SQ   SEQUENCE   633 AA;  68772 MW;  C256A6C6AC8119A0 CRC64;
     MLSVTRTAPG VRTRALRLFS SGRAASLAAV GAGAPQAKYH IVDHEYDCVV VGAGGAGLRA
     AFGLAEAGYK TACISKLFPT RSHTVAAQGG INAALGNMHG DDWKWHMYDT VKGSDWLGDQ
     DSIHYMTREA PASIIELENF GMPFSRNDEG RIYQRAFGGQ SKEYGKGGQA YRTCAVADRT
     GHAMLHTLYG QALSHNTHFF VEYFAMDLLT HNGEVVGVIA YNQEDGTVHR FRAHRTVMAT
     GGYGRAYFSC TSAHTCTGDG NAMVSRAGFP LQDLEFVQFH PSGIYGSGCL ITEGARGEGG
     FLLNSEGERF MERYAPTAKD LACRDVVSRA ITMEIREGRG VGPEKDHIHL QLSHLPPSVL
     KERLPGISET AHIFAGVDVT KEPIPVLPTV HYNMGGIPTR WTGEALTIDE ETGEDKVIPG
     LLACGEAACV SVHGANRLGA NSLLDLVVFG RAVAHTVADS LQPGLPHKPL PADLGKESIA
     NLERMRTASG PLTTSQIRLN MQKAMQKDVS VFRTQQTLDE GVHNVSAIDE TLKDVGTSDR
     SMIWNSDLVE TLELQNLLTC AVQTAKSAAE RKESRGAHAR EDFPERNDEE WMKHTLSWQH
     ASGAPVEIKY RNVITTTLDE TECPPVPPTV RAY
//

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