ID A0A173HIG6_9PSED Unreviewed; 325 AA. AC A0A173HIG6; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 14-DEC-2022, entry version 28. DE RecName: Full=Cbb3-type cytochrome c oxidase subunit {ECO:0000256|PIRNR:PIRNR000006}; GN ORFNames=AA098_19470 {ECO:0000313|EMBL:ANI35563.1}; OS Pseudomonas sp. JY-Q. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1338689 {ECO:0000313|EMBL:ANI35563.1, ECO:0000313|Proteomes:UP000078361}; RN [1] {ECO:0000313|EMBL:ANI35563.1, ECO:0000313|Proteomes:UP000078361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JY-Q {ECO:0000313|EMBL:ANI35563.1, RC ECO:0000313|Proteomes:UP000078361}; RA Zhong W.; RT "Pseudomonas sp. JY-Q genome sequencing and assembly."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase CC complex. {ECO:0000256|PIRNR:PIRNR000006}. CC -!- COFACTOR: CC Name=heme c; Xref=ChEBI:CHEBI:61717; CC Evidence={ECO:0000256|PIRNR:PIRNR000006, CC ECO:0000256|PIRSR:PIRSR000006-2}; CC Note=Binds 2 heme C groups per subunit. {ECO:0000256|PIRNR:PIRNR000006, CC ECO:0000256|PIRSR:PIRSR000006-2}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|PIRNR:PIRNR000006}. CC -!- SUBUNIT: Component of the cbb3-type cytochrome c oxidase. CC {ECO:0000256|PIRNR:PIRNR000006}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|PIRNR:PIRNR000006}. CC -!- SIMILARITY: Belongs to the CcoP / FixP family. CC {ECO:0000256|ARBA:ARBA00006113, ECO:0000256|PIRNR:PIRNR000006}. 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; CP011525; ANI35563.1; -; Genomic_DNA. DR RefSeq; WP_003254289.1; NZ_CP011525.1. DR AlphaFoldDB; A0A173HIG6; -. DR EnsemblBacteria; ANI35563; ANI35563; AA098_19470. DR PATRIC; fig|1338689.3.peg.4062; -. DR UniPathway; UPA00705; -. DR Proteomes; UP000078361; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.760.10; -; 2. DR Gene3D; 6.10.280.130; -; 1. DR InterPro; IPR032858; CcoP_N. DR InterPro; IPR038414; CcoP_N_sf. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR036909; Cyt_c-like_dom_sf. DR InterPro; IPR008168; Cyt_C_IC. DR InterPro; IPR004678; Cyt_c_oxidase_cbb3_su3. DR Pfam; PF13442; Cytochrome_CBB3; 2. DR Pfam; PF14715; FixP_N; 1. DR PIRSF; PIRSF000006; Cbb3-Cox_fixP; 1. DR PRINTS; PR00605; CYTCHROMECIC. DR SUPFAM; SSF46626; Cytochrome c; 2. DR TIGRFAMs; TIGR00782; ccoP; 1. DR PROSITE; PS51007; CYTC; 2. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, KW ECO:0000256|PIRNR:PIRNR000006}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, KW ECO:0000256|PIRNR:PIRNR000006}; KW Electron transport {ECO:0000256|PIRNR:PIRNR000006}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000006}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, KW ECO:0000256|PIRNR:PIRNR000006}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, KW ECO:0000256|PIRNR:PIRNR000006}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000006}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000006}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR000006}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000006}; Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Respiratory chain {ECO:0000256|PIRNR:PIRNR000006}; 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|PIRNR:PIRNR000006}. FT TRANSMEM 7..25 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 57..76 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 144..223 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" FT DOMAIN 234..316 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" FT BINDING 157 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000006-2" FT BINDING 160 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000006-2" FT BINDING 161 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR000006-1" FT BINDING 200 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR000006-1" FT BINDING 247 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000006-2" FT BINDING 250 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000006-2" FT BINDING 251 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR000006-1" FT BINDING 293 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR000006-1" SQ SEQUENCE 325 AA; 35585 MW; 30F47A002D86031C CRC64; MTTFWSLYVT VLTLGTIFSL TWLLLSTRKG QREEVTDETV GHAFDGIEEY DNPLPKWWFW LFVGTIIFAL GYLVLYPGLG NWKGVLPGYS YLDNDKQTEF SNGQPGWTGV HEWEKEMAKA DARFGPIFAK FAAMPIEDVA KDPQALKMGA RLFASNCSVC HGSDAKGAFG FPNLTDNDWR WGGEPDTIKT TIMGGRHGVM PAWAEVIGDQ GVADVAAFVV SKLDGRTLPE GAKADVENGQ KIFAANCVAC HGPEGKGTPA MGAPNLTHPQ AFIYGSSFAQ LQQTIRYGRQ GQMPAQEQLQ GNDKVHLLAA YVYSLSHQAE PAKAE //