ID A0A173HEM5_9PSED Unreviewed; 332 AA. AC A0A173HEM5; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 02-JUN-2021, entry version 19. DE SubName: Full=Cytochrome B6 {ECO:0000313|EMBL:ANI34322.1}; GN ORFNames=AA098_12805 {ECO:0000313|EMBL:ANI34322.1}; OS Pseudomonas sp. JY-Q. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1338689 {ECO:0000313|EMBL:ANI34322.1, ECO:0000313|Proteomes:UP000078361}; RN [1] {ECO:0000313|EMBL:ANI34322.1, ECO:0000313|Proteomes:UP000078361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JY-Q {ECO:0000313|EMBL:ANI34322.1, 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 -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR000294-2}; CC Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-2}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}. CC -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294- CC 1}. 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; ANI34322.1; -; Genomic_DNA. DR RefSeq; WP_047604933.1; NZ_CP011525.1. DR EnsemblBacteria; ANI34322; ANI34322; AA098_12805. DR PATRIC; fig|1338689.3.peg.2649; -. DR Proteomes; UP000078361; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.760.10; -; 2. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR036909; Cyt_c-like_dom_sf. DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae. DR InterPro; IPR026259; MauG/Cytc_peroxidase. DR Pfam; PF03150; CCP_MauG; 1. DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1. DR SUPFAM; SSF46626; SSF46626; 2. DR PROSITE; PS51007; CYTC; 2. PE 4: Predicted; KW Electron transport {ECO:0000256|ARBA:ARBA00022982}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000294-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000294-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000294-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Periplasm {ECO:0000256|ARBA:ARBA00022764}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 55..163 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" FT DOMAIN 206..325 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" FT METAL 81 FT /note="Iron (heme 1 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2" FT METAL 224 FT /note="Iron (heme 2 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2" FT METAL 300 FT /note="Iron (heme 2 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2" FT BINDING 77 FT /note="Heme 1; covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 80 FT /note="Heme 1; covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 220 FT /note="Heme 2; covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 223 FT /note="Heme 2; covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" SQ SEQUENCE 332 AA; 37109 MW; 035B0B30B5492474 CRC64; MSARTTCRYR SALHLQRLRR CLGLWVLLVL SGGSGAEPLD EPLKPLPPIP TLTPGRVELG RQLFNDPRLS RNGTRSCASC HRLDKYGADD RAFSMGADGL PLTLNTPTVL NASLNFRQFW NGRVESLEEQ GEAVITSAHE MGGDWRVIEQ RIAADVHYRQ AFKDAYPDAV TKDNILSALA DYQRTLLTPG ARFDRYLQGD TEALTLEEKY GYQRFKDYGC IACHQGVNIG GNMFQKFGVF GDYIADRGHP TEADQGRFNV TGEEADRGVF KVPSLRNVAM TAPYFHDGSA PTLERAIDVM FQYQLGRIPS DEDRRLIMLF LKTLTAEKAG QP //