DHSD_RECAM
ID DHSD_RECAM Reviewed; 120 AA.
AC P80482;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Succinate dehydrogenase membrane anchor subunit;
DE AltName: Full=Succinate dehydrogenase, subunit IV;
GN Name=SDH4;
OS Reclinomonas americana.
OG Mitochondrion.
OC Eukaryota; Discoba; Jakobida; Histionina; Histionidae; Reclinomonas.
OX NCBI_TaxID=48483;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 50394;
RX PubMed=8637872; DOI=10.1073/pnas.93.6.2328;
RA Burger G., Lang B.F., Reith M., Gray M.W.;
RT "Genes encoding the same three subunits of respiratory complex II are
RT present in the mitochondrial DNA of two phylogenetically distant
RT eukaryotes.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:2328-2332(1996).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=The heme is bound between the two transmembrane subunits.
CC {ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC flavoprotein, an iron-sulfur protein, plus two membrane-anchoring
CC proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF007261; AAD11912.1; -; Genomic_DNA.
DR PIR; S78179; S78179.
DR RefSeq; NP_044797.1; NC_001823.1.
DR AlphaFoldDB; P80482; -.
DR SMR; P80482; -.
DR GeneID; 801073; -.
DR UniPathway; UPA00223; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR014312; Succ_DH_anchor.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR Pfam; PF01127; Sdh_cyt; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
DR TIGRFAMs; TIGR02968; succ_dehyd_anc; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Transmembrane; Transmembrane helix;
KW Transport; Tricarboxylic acid cycle.
FT CHAIN 1..120
FT /note="Succinate dehydrogenase membrane anchor subunit"
FT /id="PRO_0000158713"
FT TOPO_DOM 1..17
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..63
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..95
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 76
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with second transmembrane
FT subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
SQ SEQUENCE 120 AA; 14222 MW; 119F6DB10475544E CRC64;
MTEKLLHFIR TKSGSMHWWL QRFLAILLAP IILYLLFDVA IYIGQQSDPT VMMFLNRIFN
HNSIFIFITS VILIWHVRGG MEVIIEDYVH GEKTRIVSIF LIRVIAIEIM EYLYKCSIIF
