ID H2PF44_PONAB Unreviewed; 768 AA.
AC H2PF44;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial {ECO:0000256|ARBA:ARBA00020842, ECO:0000256|RuleBase:RU362051};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU362051};
GN Name=SDHA {ECO:0000313|Ensembl:ENSPPYP00000017115.3};
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 {ECO:0000313|Ensembl:ENSPPYP00000017115.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000017115.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000017115.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00000030,
CC 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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (eukaryal route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004788, ECO:0000256|RuleBase:RU362051}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU362051};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443,
CC ECO:0000256|RuleBase:RU362051}; Matrix side
CC {ECO:0000256|ARBA:ARBA00004443, 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}.
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DR AlphaFoldDB; H2PF44; -.
DR Ensembl; ENSPPYT00000017810.3; ENSPPYP00000017115.3; ENSPPYG00000015298.3.
DR eggNOG; KOG2403; Eukaryota.
DR GeneTree; ENSGT00910000144277; -.
DR HOGENOM; CLU_014312_4_1_1; -.
DR InParanoid; H2PF44; -.
DR OMA; FHPTGIW; -.
DR TreeFam; TF352884; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000001595; Chromosome 5.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
DR GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl.
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 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 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};
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:UP000001595};
KW Transit peptide {ECO:0000256|RuleBase:RU362051};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU362051}.
FT DOMAIN 167..561
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 617..768
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 30..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 444
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-1"
FT MOD_RES 203
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ SEQUENCE 768 AA; 83922 MW; B41148AE1CA0B882 CRC64;
MLVPNTSLEQ GPLYLGRGAR DLGVHPNATV RGSALRRRSA PTQPPPRAWH GAQARCPPLR
PRSTPAWCAG AVSPPTPPAP LDPGVMRRRS LRRDWRDCAA ATTDMSGVRG LSRLLSARRL
ALAKAWPTVL QTGARGFHFT VDGNKRASAK VSDSISAQYP VVDHEFDAVV VGAGGAGLRA
AFGLSEAGFN TACVTKLFPT RSHTVAAQGG INAALGNMEE DNWRWHFYDT VKGSDWLGDQ
DAIHYMTEQA PAAVVELENY GMPFSRTEDG KIYQRAFGGQ SLKFGKGGQA HRCCCVADRT
GHSLLHTLYG RSLRYDTSYF VEYFALDLLM ENGECRGVIA LCIEDGSIHR IRAKNTVVAT
GGYGRTYFSC TSAHTSTGDG TAMITRAGLP CQDLEFVQFH PTGIYGAGCL ITEGCRGEGG
ILINSQGERF MERYAPVAKD LASRDVVSRS MTLEIREGRG CGPEKDHVYL QLHHLPPEQL
ATRLPGISET AMIFAGVDVT KEPIPVLPTV HYNMGGIPTN YKGQVLRHVN GQDQIVPGLY
ACGEAACASV HGANRLGANS LLDLVVFGRA CALSIEESCR PGDKVPPIKP NAGEESVMNL
DKLRFADGSI RTSELRLSMQ KSMQNHAAVF RVGSVLQEGC GKISKLYGDL KHLKTFDRGM
VWNTDLVETL ELQNLMLCAL QTIYGAEARK ESRGAHARED YKVRIDEYDY SKPIQGQQKK
PFEEHWRKHT LSYVDVSTGK VTLEYRPVID KTLNEADCAT VPPAIRSY
//
