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Database: UniProt
Entry: A0A068YIP3_9BURK
LinkDB: A0A068YIP3_9BURK
Original site: A0A068YIP3_9BURK 
ID   A0A068YIP3_9BURK        Unreviewed;       121 AA.
AC   A0A068YIP3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit {ECO:0000256|ARBA:ARBA00019425};
OS   Polaromonas sp. CG9_12.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1504672 {ECO:0000313|EMBL:CDS50080.1, ECO:0000313|Proteomes:UP000043372};
RN   [1] {ECO:0000313|EMBL:CDS50080.1, ECO:0000313|Proteomes:UP000043372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Smith H.J., Foreman C.M., Ramaraj T.;
RT   "Draft Genome Sequence of a Metabolically Diverse Antarctic Supraglacial
RT   Stream Organism, Polaromonas sp. Strain CG9_12, Determined Using Pacific
RT   Biosciences Single-Molecule Real-Time Sequencing Technology.";
RL   Genome Announc. 2:1-2(2014).
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; CCJP01000005; CDS50080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068YIP3; -.
DR   STRING; 1504672.gene:199030562; -.
DR   eggNOG; COG2142; Bacteria.
DR   OrthoDB; 5612767at2; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000043372; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000043372};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..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;  13842 MW;  7C2BDD9535D61FF3 CRC64;
     MSVNYGSKRI VVGAHYGTRD WLSQRITAAL MAIFTILLLG QVIFSKGPIG YDQWAGIFSP
     QWMKVLTFAV IIALLQHVWV GMRDIWMDYI KPVGLRLLLQ VFTIFWLVAC AGWGVQVLWR
     L
//
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