ID Q0K8F8_CUPNH Unreviewed; 121 AA.
AC Q0K8F8;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit {ECO:0000256|ARBA:ARBA00019425};
GN Name=sdhD {ECO:0000313|EMBL:CAJ93713.1};
GN OrderedLocusNames=H16_A2631 {ECO:0000313|EMBL:CAJ93713.1};
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ93713.1, ECO:0000313|Proteomes:UP000008210};
RN [1] {ECO:0000313|EMBL:CAJ93713.1, ECO:0000313|Proteomes:UP000008210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC 337 {ECO:0000313|Proteomes:UP000008210};
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC {ECO:0000256|ARBA:ARBA00004050}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR000169-2};
CC Note=The heme is bound between the two transmembrane subunits.
CC {ECO:0000256|PIRSR:PIRSR000169-2};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000256|ARBA:ARBA00005163}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AM260479; CAJ93713.1; -; Genomic_DNA.
DR RefSeq; WP_010814617.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0K8F8; -.
DR STRING; 381666.H16_A2631; -.
DR GeneID; 57644755; -.
DR KEGG; reh:H16_A2631; -.
DR eggNOG; COG2142; Bacteria.
DR HOGENOM; CLU_151315_2_1_4; -.
DR OrthoDB; 5612767at2; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0005886; C:plasma 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:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd03494; SQR_TypeC_SdhD; 1.
DR Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR014312; Succ_DH_anchor.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR NCBIfam; TIGR02968; succ_dehyd_anc; 1.
DR PANTHER; PTHR38689; SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR SUBUNIT; 1.
DR PANTHER; PTHR38689:SF1; SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR SUBUNIT; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000169; SDH_D; 1.
DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000169-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000169-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000169-2};
KW Oxidoreductase {ECO:0000313|EMBL:CAJ93713.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008210};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 77
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:0000256|PIRSR:PIRSR000169-2"
FT BINDING 89
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000256|PIRSR:PIRSR000169-1"
SQ SEQUENCE 121 AA; 13680 MW; FB18E6A73BCD5244 CRC64;
MANNNIGPKR LVVGAHYGLK DWLAQRVTAV IMVVFTVVLA IAFLLSNGAS YEAWAGLFSN
QWMKIITFLT ILSLLYHAWI GVRDIWMDYV RPMAVRLVLQ VLTILWLVGC AGYAAQILWR
V
//
