ID A0A3S3UBK9_9BACT Unreviewed; 298 AA. AC A0A3S3UBK9; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 27-NOV-2024, entry version 21. DE SubName: Full=Cytochrome c peroxidase {ECO:0000313|EMBL:RWX48077.1}; DE EC=1.11.1.5 {ECO:0000313|EMBL:RWX48077.1}; GN Name=ccp {ECO:0000313|EMBL:RWX48077.1}; GN ORFNames=H206_05370 {ECO:0000313|EMBL:RWX48077.1}; OS Candidatus Electrothrix aarhusensis. OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales; OC Desulfobulbaceae; Candidatus Electrothrix. OX NCBI_TaxID=1859131 {ECO:0000313|EMBL:RWX48077.1, ECO:0000313|Proteomes:UP000287853}; RN [1] {ECO:0000313|EMBL:RWX48077.1, ECO:0000313|Proteomes:UP000287853} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCF {ECO:0000313|EMBL:RWX48077.1}; RA Schreiber L., Bjerg J.T., Boggild A., Van De Vossenberg J., Meysman F., RA Nielsen L.P., Schramm A., Kjeldsen K.U.; RT "The cable genome- insights into the physiology and evolution of RT filamentous bacteria capable of sulfide oxidation via long distance RT electron transfer."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR000294-1}; CC Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-1}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}. CC -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294- CC 1}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RWX48077.1}. 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; MTKO01000008; RWX48077.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3S3UBK9; -. DR Proteomes; UP000287853; Unassembled WGS sequence. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:UniProtKB-EC. 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 FunFam; 1.10.760.10:FF:000004; Cytochrome c peroxidase; 1. DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR036909; Cyt_c-like_dom_sf. DR InterPro; IPR051395; Cytochrome_c_Peroxidase/MauG. DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae. DR InterPro; IPR026259; MauG/Cytc_peroxidase. DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1. DR PANTHER; PTHR30600:SF7; CYTOCHROME C PEROXIDASE-RELATED; 1. DR Pfam; PF03150; CCP_MauG; 1. DR Pfam; PF00034; Cytochrom_C; 1. DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1. DR SUPFAM; SSF46626; Cytochrome c; 2. DR PROSITE; PS51007; CYTC; 2. PE 4: Predicted; 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 ECO:0000313|EMBL:RWX48077.1}; Periplasm {ECO:0000256|ARBA:ARBA00022764}; KW Peroxidase {ECO:0000313|EMBL:RWX48077.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000287853}. FT DOMAIN 7..115 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" FT DOMAIN 159..273 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" FT BINDING 29 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 32 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 33 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:PIRSR000294-2" FT BINDING 49 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:PIRSR000294-2" FT BINDING 173 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 176 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1" FT BINDING 177 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:PIRSR000294-2" FT BINDING 248 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:PIRSR000294-2" SQ SEQUENCE 298 AA; 32685 MW; D3821966B1174643 CRC64; MKEINLAKAE LGKKLFFDPR LSKSGFISCN SCHNLSMGGT DNLKTSIGHK WQQGPINAPT VLNSSLNFVQ FWDGRAETLK DQAGGPIANP GEMAFTHDLA QDVLVSIPGY ITEFKQVFGD DKVNIDRVTD AIAEFEKTLV TPNSRFDQFL MGDKDAMTAD EQAGYKLFQD SGCISCHYGE AMGGSSFQKM GVMEEYKAKS PAEGRMAVTG KDEDRFAFKV PTLRNVELTY PYFHDGEAGT LTEAVDVMGR LQLGAKFTDE QNAQIVAFLK SLTGDQPAFT LPLLPPSSDK TPPPKPFE //