ID   SDHA_PONAB              Reviewed;         664 AA.
AC   Q5R616;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   13-SEP-2023, entry version 112.
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;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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). Can act as a tumor suppressor.
CC       {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: the
CC       flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome
CC       b560 composed of SDHC and SDHD (By similarity). Interacts with
CC       SDHAF2/SDH5; interaction is required for FAD attachment (By
CC       similarity). Interacts with TRAP1 (By similarity). Interacts with LACC1
CC       (By similarity). {ECO:0000250|UniProtKB:P31040,
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   -!- PTM: Acetylated. Deacetylated by SIRT3. {ECO:0000250|UniProtKB:Q8K2B3}.
CC   -!- PTM: Phosphorylation at Tyr-215 is important for efficient electron
CC       transfer in complex II and the prevention of ROS generation.
CC       {ECO:0000250|UniProtKB:P31040}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
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DR   EMBL; CR860684; CAH92800.1; -; mRNA.
DR   RefSeq; NP_001126633.1; NM_001133161.1.
DR   AlphaFoldDB; Q5R616; -.
DR   SMR; Q5R616; -.
DR   STRING; 9601.ENSPPYP00000017089; -.
DR   GeneID; 100173631; -.
DR   KEGG; pon:100173631; -.
DR   CTD; 6389; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   InParanoid; Q5R616; -.
DR   OrthoDB; 551958at2759; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB.
DR   GO; GO:0006105; P:succinate metabolic process; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Electron transport; FAD; Flavoprotein; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle; Tumor suppressor.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   CHAIN           43..664
FT                   /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT                   subunit, mitochondrial"
FT                   /id="PRO_0000272304"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         68..73
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         91..106
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         275
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         440
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         451
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         456..457
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   MOD_RES         99
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   MOD_RES         167
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         179
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P31040"
FT   MOD_RES         179
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         182
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         215
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P31040"
FT   MOD_RES         250
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         250
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         335
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P31040"
FT   MOD_RES         335
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         480
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         485
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         485
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         498
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         498
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         517
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         538
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         538
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         541
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P31040"
FT   MOD_RES         547
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         547
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         550
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         598
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         608
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P31040"
FT   MOD_RES         615
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         624
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         636
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT   MOD_RES         647
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2B3"
SQ   SEQUENCE   664 AA;  72692 MW;  705C3B8852ADFE21 CRC64;
     MSGVRGLSRL LSARRLALAK AWPTVLQTGA RGFHFTVDGN KRASAKVSDS ISAQYPVVDH
     EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT VAAQGGINAA LGNMEEDNWR
     WHFYDTVKGS DWLGDQDAIH YMTEQAPAAV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF
     GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE
     DGSIHRIRAK NTVVATGGYG RTYFSCTSAH TSTGDGTAMI TRAGLPCQDL EFVQFHPTGI
     YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE
     KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ
     VLRHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IEESCRPGDK
     VPPIKPNAGE ESVMNLDKLR FADGSIRTSE LRLSMQKSMQ NHAAVFRVGS VLQEGCGKIS
     KLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR
     IDEYDYSKPI QGQQKKPFEE HWRKHTLSYV DVSTGKVTLE YRPVIDKTLN EADCATVPPA
     IRSY
//