ID A0A173HEM5_9PSED Unreviewed; 332 AA. AC A0A173HEM5; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 28-FEB-2018, entry version 9. 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 -!- PTM: Binds 2 heme groups per subunit. CC {ECO:0000256|PIRSR:PIRSR000294-1}. 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: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; -; 3. 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 Complete proteome {ECO:0000313|Proteomes:UP000078361}; KW Heme {ECO:0000256|PIRSR:PIRSR000294-1, ECO:0000256|PROSITE- KW ProRule:PRU00433}; KW Iron {ECO:0000256|PIRSR:PIRSR000294-2, ECO:0000256|PROSITE- KW ProRule:PRU00433}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000294-2, ECO:0000256|PROSITE- KW ProRule:PRU00433}. FT DOMAIN 55 163 Cytochrome c. {ECO:0000259|PROSITE: FT PS51007}. FT DOMAIN 206 325 Cytochrome c. {ECO:0000259|PROSITE: FT PS51007}. FT METAL 81 81 Iron (heme 1 axial ligand). FT {ECO:0000256|PIRSR:PIRSR000294-2}. FT METAL 224 224 Iron (heme 2 axial ligand). FT {ECO:0000256|PIRSR:PIRSR000294-2}. FT METAL 300 300 Iron (heme 2 axial ligand). FT {ECO:0000256|PIRSR:PIRSR000294-2}. FT BINDING 77 77 Heme 1 (covalent). {ECO:0000256|PIRSR: FT PIRSR000294-1}. FT BINDING 80 80 Heme 1 (covalent). {ECO:0000256|PIRSR: FT PIRSR000294-1}. FT BINDING 220 220 Heme 2 (covalent). {ECO:0000256|PIRSR: FT PIRSR000294-1}. FT BINDING 223 223 Heme 2 (covalent). {ECO:0000256|PIRSR: FT 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 //