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SDHX_YEAST
ID   SDHX_YEAST              Reviewed;         634 AA.
AC   P47052; D6VWD9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 186.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial;
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE   AltName: Full=Flavoprotein subunit of complex II;
DE            Short=FP;
DE   AltName: Full=SDH1b;
DE   Flags: Precursor;
GN   OrderedLocusNames=YJL045W; ORFNames=J1194;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=9730279;
RX   DOI=10.1002/(sici)1097-0061(199808)14:11<1001::aid-yea304>3.0.co;2-k;
RA   Colby G., Ishii Y., Tzagoloff A.;
RT   "Suppression of sdh1 mutations by the SDH1b gene of Saccharomyces
RT   cerevisiae.";
RL   Yeast 14:1001-1006(1998).
CC   -!- FUNCTION: Probable minor catalytic subunit of succinate dehydrogenase
CC       (SDH) that is involved in complex II of the mitochondrial electron
CC       transport chain and is responsible for transferring electrons from
CC       succinate to ubiquinone (coenzyme Q). Probably forms a catalytic dimer
CC       with SDH2. Electrons flow from succinate to the FAD bound to the
CC       catalytic subunit, and sequentially through the iron-sulfur clusters
CC       bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4.
CC       {ECO:0000269|PubMed:9730279}.
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:Q00711}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q00711}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q00711}; Matrix side
CC       {ECO:0000250|UniProtKB:Q00711}.
CC   -!- MISCELLANEOUS: In vitro, can complement a SDH1 disruption and leads to
CC       less than 15% of wild-type SDH reductase activity probably due to its
CC       lower expression level (compared to SDH1).
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
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DR   EMBL; Z49320; CAA89336.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08755.1; -; Genomic_DNA.
DR   PIR; S56817; S56817.
DR   RefSeq; NP_012490.1; NM_001181478.1.
DR   AlphaFoldDB; P47052; -.
DR   SMR; P47052; -.
DR   BioGRID; 33713; 264.
DR   DIP; DIP-4262N; -.
DR   IntAct; P47052; 3.
DR   MINT; P47052; -.
DR   STRING; 4932.YJL045W; -.
DR   iPTMnet; P47052; -.
DR   MaxQB; P47052; -.
DR   PaxDb; P47052; -.
DR   PRIDE; P47052; -.
DR   EnsemblFungi; YJL045W_mRNA; YJL045W; YJL045W.
DR   GeneID; 853405; -.
DR   KEGG; sce:YJL045W; -.
DR   SGD; S000003581; YJL045W.
DR   VEuPathDB; FungiDB:YJL045W; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   GeneTree; ENSGT00910000144277; -.
DR   HOGENOM; CLU_014312_6_1_1; -.
DR   InParanoid; P47052; -.
DR   OMA; HWEWHMF; -.
DR   BioCyc; YEAST:YJL045W-MON; -.
DR   UniPathway; UPA00223; UER01006.
DR   PRO; PR:P47052; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47052; protein.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
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; IMP:SGD.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0045333; P:cellular respiration; IMP:SGD.
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   3: Inferred from homology;
KW   Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW   Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..634
FT                   /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT                   subunit 2, mitochondrial"
FT                   /id="PRO_0000010343"
FT   ACT_SITE        325
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         53..58
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         76..91
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         260
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         392
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         427
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         438
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         443..444
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   MOD_RES         84
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
SQ   SEQUENCE   634 AA;  69382 MW;  F00CD157AB9BF9C5 CRC64;
     MLSLKKGITK SYILQRTFTS SSVVRQIGEV KSESKPPAKY HIIDHEYDCV VVGAGGAGLR
     AAFGLAEAGY KTACLSKLFP TRSHTVAAQG GINAALGNMH PDDWKSHMYD TVKGSDWLGD
     QDAIHYMTRE APKSVIELEH YGMPFSRTED GRIYQRAFGG QSKDFGKGGQ AYRTCAVADR
     TGHAMLHTLY GQALKNNTHF FIEYFAMDLL THNGEVVGVI AYNQEDGTIH RFRAHKTVIA
     TGGYGRAYFS CTSAHTCTGD GNAMVSRAGF PLEDLEFVQF HPSGIYGSGC LITEGARGEG
     GFLLNSEGER FMERYAPTAK DLASRDVVSR AITMEIRAGR GVGKNKDHIL LQLSHLPPEV
     LKERLPGISE TAAVFAGVDV TQEPIPVLPT VHYNMGGIPT KWTGEALTID EETGEDKVIP
     GLMACGEAAC VSVHGANRLG ANSLLDLVVF GRAVANTIAD TLQPGLPHKP LASNIGHESI
     ANLDKVRNAR GSLKTSQIRL NMQRTMQKDV SVFRTQDTLD EGVRNITEVD KTFEDVHVSD
     KSMIWNSDLV ETLELQNLLT CATQTAVSAS KRKESRGAHA REDYAKRDDV NWRKHTLSWQ
     KGTSTPVKIK YRNVIAHTLD ENECAPVPPA VRSY
 
 
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