ID Q9JZP9_NEIMB Unreviewed; 113 AA. AC Q9JZP9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 02-SEP-2026, entry version 117. DE RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit {ECO:0000256|ARBA:ARBA00019425}; GN Name=sdhD {ECO:0000313|EMBL:AAF41355.1}; GN OrderedLocusNames=NMB0949 {ECO:0000313|EMBL:AAF41355.1}; OS Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41355.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41355.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-335 / MC58 {ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., RA Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., RA White O., Fleischmann R.D., Dougherty B.A., Mason T., Ciecko A., RA Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., RA Utterback T.R., Khouri H., Qin H., Vamathevan J., Gill J., Scarlato V., RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., RA Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). 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}. 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; AE002098; AAF41355.1; -; Genomic_DNA. DR PIR; E81138; E81138. DR RefSeq; WP_002223854.1; NC_003112.2. DR AlphaFoldDB; Q9JZP9; -. DR FunCoup; Q9JZP9; 102. DR STRING; 122586.NMB0949; -. DR PaxDb; 122586-NMB0949; -. DR KEGG; nme:NMB0949; -. DR PATRIC; fig|122586.8.peg.1205; -. DR HOGENOM; CLU_151315_2_1_4; -. DR InParanoid; Q9JZP9; -. DR OrthoDB; 5612767at2; -. DR UniPathway; UPA00223; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central. DR GO; GO:0017004; P:cytochrome complex assembly; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR CDD; cd03494; SQR_TypeC_SdhD; 1. DR FunFam; 1.20.1300.10:FF:000012; Succinate dehydrogenase hydrophobic membrane anchor subunit; 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 Electron transport {ECO:0000256|ARBA:ARBA00022982}; 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:UP000000425}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}. FT TRANSMEM 21..38 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 58..78 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 90..112 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT BINDING 70 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 82 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /evidence="ECO:0000256|PIRSR:PIRSR000169-1" SQ SEQUENCE 113 AA; 13149 MW; C1C7C48D584176CD CRC64; MVERKLTGAH YGLRDWVMQR ATAVIMLIYT VALLVVLFSL PKEYSAWQAF FSQTWVKVFT QVSFIAVFLH AWVGIRDLWM DYIKPFGVRL FLQVATIVWL VGCLVYSVKV IWG //