ID A0A5S9HWS0_NEOKA Unreviewed; 129 AA. AC A0A5S9HWS0; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 14-DEC-2022, entry version 9. DE SubName: Full=Succinate:cytochrome c oxidoreductase subunit 3 {ECO:0000313|EMBL:BBH62867.1}; GN Name=sdh3 {ECO:0000313|EMBL:BBH62867.1}; OS Neopyropia katadae var. hemiphylla. OG Mitochondrion {ECO:0000313|EMBL:BBH62867.1}. OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia. OX NCBI_TaxID=243213 {ECO:0000313|EMBL:BBH62867.1}; RN [1] {ECO:0000313|EMBL:BBH62867.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Omosegawa {ECO:0000313|EMBL:BBH62867.1}, Orikasagawa RC {ECO:0000313|EMBL:BBH62866.1}, and Otowagawa RC {ECO:0000313|EMBL:BBH62868.1}; RA Tamaki M., Fujiyoshi E., Kobayashi M., Iwade S., Kaneko A., Suda M.; RT "DNA analysis of Pyropia katadae in Japan."; RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR000178-1}; CC Note=The heme is bound between the two transmembrane subunits. CC {ECO:0000256|PIRSR:PIRSR000178-1}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the cytochrome b560 family. CC {ECO:0000256|ARBA:ARBA00007244}. 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; LC436590; BBH62866.1; -; Genomic_DNA. DR EMBL; LC436591; BBH62867.1; -; Genomic_DNA. DR EMBL; LC436592; BBH62868.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5S9HWS0; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0045281; C:succinate dehydrogenase complex; IEA:InterPro. DR GO; GO:0009055; F:electron transfer activity; 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:InterPro. DR Gene3D; 1.20.1300.10; -; 1. DR InterPro; IPR034804; SQR/QFR_C/D. DR InterPro; IPR018495; Succ_DH_cyt_bsu_CS. DR InterPro; IPR014314; Succ_DH_cytb556. DR InterPro; IPR000701; SuccDH_FuR_B_TM-su. DR PANTHER; PTHR10978; SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT; 1. DR Pfam; PF01127; Sdh_cyt; 1. DR PIRSF; PIRSF000178; SDH_cyt_b560; 1. DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1. DR TIGRFAMs; TIGR02970; succ_dehyd_cytB; 1. DR PROSITE; PS01000; SDH_CYT_1; 1. DR PROSITE; PS01001; SDH_CYT_2; 1. PE 3: Inferred from homology; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000178-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000178-1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000178-1}; KW Mitochondrion {ECO:0000313|EMBL:BBH62867.1}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 32..52 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 64..86 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 106..127 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT BINDING 85 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:PIRSR000178-1" SQ SEQUENCE 129 AA; 15238 MW; BDF58E5B908687F3 CRC64; MHNINRPISP HLTIYNPQIS ATFSIWHRIS GVVMFILIAS SILILNQVYF SYTPIFLVDI LLNYILSNWI LVSFRLLIST IFLYHISNGL RHFLWDSVRH VNTKKIYKDS NLLLFFVFIV TITQSYIEF //