ID A2SHT6_METPP Unreviewed; 120 AA. AC A2SHT6; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 91. DE RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit {ECO:0000256|ARBA:ARBA00019425}; GN OrderedLocusNames=Mpe_A2169 {ECO:0000313|EMBL:ABM95125.1}; OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Sphaerotilaceae; Methylibium. OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM95125.1, ECO:0000313|Proteomes:UP000000366}; RN [1] {ECO:0000313|EMBL:ABM95125.1, ECO:0000313|Proteomes:UP000000366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1 RC {ECO:0000313|Proteomes:UP000000366}; RX PubMed=17158667; DOI=10.1128/JB.01259-06; RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., RA Hristova K.R.; RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta- RT proteobacterium Methylibium petroleiphilum PM1."; RL J. Bacteriol. 189:1931-1945(2007). 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}. 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; CP000555; ABM95125.1; -; Genomic_DNA. DR RefSeq; WP_011829762.1; NC_008825.1. DR AlphaFoldDB; A2SHT6; -. DR STRING; 420662.Mpe_A2169; -. DR KEGG; mpt:Mpe_A2169; -. DR eggNOG; COG2142; Bacteria. DR HOGENOM; CLU_151315_2_1_4; -. DR UniPathway; UPA00223; -. DR Proteomes; UP000000366; Chromosome. 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:ABM95125.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000366}; 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..44 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 64..84 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 96..118 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" 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:0000256|PIRSR:PIRSR000169-2" FT BINDING 88 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /evidence="ECO:0000256|PIRSR:PIRSR000169-1" SQ SEQUENCE 120 AA; 13666 MW; 1D3D3EAAAA78AE3C CRC64; MTQNYGSKRI VVGAHYGLRD WLSQRVTAAL MAIFTIVLIA QVLFGAPMGY ERWAGIFSSQ WMKVLTFVVI VSLAWHAWVG VRDIWMDYVK PVGVRLLLQV LTISWLVGCA GWAIQVLWRL //