SDHA_DANRE
ID SDHA_DANRE Reviewed; 661 AA.
AC Q7ZVF3; Q1LV99;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE AltName: Full=Flavoprotein subunit of complex II;
DE Short=Fp;
DE Flags: Precursor;
GN Name=sdha; ORFNames=si:dkeyp-84f11.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) 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:0000250|UniProtKB:P31040}.
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:0000250|UniProtKB:P31040};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q0QF01};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (eukaryal route): step 1/1.
CC {ECO:0000250|UniProtKB:P31040}.
CC -!- SUBUNIT: Component of complex II composed of four subunits: a
CC flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
CC composed of a large and a small subunit.
CC {ECO:0000250|UniProtKB:Q0QF01}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q0QF01}; Matrix side
CC {ECO:0000250|UniProtKB:Q0QF01}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; BX890617; CAK11468.1; -; Genomic_DNA.
DR EMBL; BC045885; AAH45885.1; -; mRNA.
DR RefSeq; NP_957204.1; NM_200910.1.
DR AlphaFoldDB; Q7ZVF3; -.
DR SMR; Q7ZVF3; -.
DR STRING; 7955.ENSDARP00000018027; -.
DR PaxDb; Q7ZVF3; -.
DR PRIDE; Q7ZVF3; -.
DR Ensembl; ENSDART00000015559; ENSDARP00000018027; ENSDARG00000016721.
DR GeneID; 393884; -.
DR KEGG; dre:393884; -.
DR CTD; 6389; -.
DR ZFIN; ZDB-GENE-040426-874; sdha.
DR eggNOG; KOG2403; Eukaryota.
DR GeneTree; ENSGT00910000144277; -.
DR HOGENOM; CLU_014312_6_1_1; -.
DR InParanoid; Q7ZVF3; -.
DR OMA; DPIPIQP; -.
DR OrthoDB; 606981at2759; -.
DR PhylomeDB; Q7ZVF3; -.
DR TreeFam; TF300763; -.
DR Reactome; R-DRE-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER01006.
DR PRO; PR:Q7ZVF3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000016721; Expressed in muscle tissue and 43 other tissues.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
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; ISS:UniProtKB.
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; 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 PANTHER; PTHR11632; PTHR11632; 1.
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 2: Evidence at transcript level;
KW Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT CHAIN 41..661
FT /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT subunit, mitochondrial"
FT /id="PRO_0000344985"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 65..70
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 88..103
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 437
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 453..454
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT MOD_RES 96
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT CONFLICT 18
FT /note="C -> S (in Ref. 2; AAH45885)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="D -> N (in Ref. 2; AAH45885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 72078 MW; 636BF993BE55D19B CRC64;
MAAVCAASRV LGTKILSCKS LPAVCQANRQ LHFSIYGKRG DAKISDGVSN QYPVVDHEFD
AVVVGAGGAG LRAAFGLSEA GFNTACVTKL FPTRSHTVAA QGGINAALGN MEQDDWRWHF
YDTVKGSDWL GDQDAIHYMT EQAPAAVVEL ENFGMPFSRT DDGKIYQRAF GGQSLKFGKG
GQAHRCCCVA DRTGHSLLHT LYGRSLRYDT SYFVEYFALD LLMEDGECKG VIALCMEDGS
IHRFRAKNTV IATGGYGRTF FSCTSAHTST GDGNAMVTRA GLPCQDLEFV QFHPTGIYGA
GCLITEGCRG EGGILINSEG ERFMERYAPN AKDLASRDVV SRSMTIEIRE GRGVGPDKDH
VHLQLHHLPP QQLAARLPGI SETAMIFAGV DVTKEPIPVL PTVHYNMGGI PTNYKGQVIT
YKDGQDHVVP GLYACGEAGC ASVHGANRLG ANSLLDLVVF GRACALTIAE IDTPGEKLSP
LKPNAGEASV ANLDKMRYAN GSTRTSEIRL NMQKTMQSHA AVFRTGDVLK EGCVKMESVY
KSMDDIKTFD RGIVWNTDLV ETLELQNLML NAVQTIVSAE ARKESRGAHA REDFKDRVDE
YDYSKPLQGQ VKKPFEQHWR KHTLSYVDPE TGKVTLEYRP VIDSSLDAED CAAIPPAIRS
Y
