ID P83787_MARNT Unreviewed; 326 AA. AC P83787; DT 15-MAR-2004, integrated into UniProtKB/TrEMBL. DT 15-MAR-2004, sequence version 1. DT 27-MAR-2024, entry version 100. DE SubName: Full=Cytochrome c peroxidase {ECO:0000313|PDB:1NML}; OS Marinobacter nauticus (Marinobacter hydrocarbonoclasticus) (Marinobacter OS aquaeolei). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Marinobacteraceae; Marinobacter. OX NCBI_TaxID=2743 {ECO:0000313|PDB:1NML}; RN [1] {ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ5} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH CALCIUM AND HEME, RP AND ACTIVE SITE. RX PubMed=15274917; DOI=10.1016/j.str.2004.03.025; RA Dias J.M., Alves T., Bonifacio C., Pereira A.S., Trincao J., Bourgeois D., RA Moura I., Romao M.J.; RT "Structural basis for the mechanism of Ca(2+) activation of the di-heme RT cytochrome c peroxidase from Pseudomonas nautica 617."; RL Structure 12:961-973(2004). 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 --------------------------------------------------------------------------- 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 PDB; 1NML; X-ray; 2.20 A; A=1-326. DR PDB; 1RZ5; X-ray; 2.40 A; A=1-326. DR PDB; 1RZ6; X-ray; 2.20 A; A=1-326. DR PDBsum; 1NML; -. DR PDBsum; 1RZ5; -. DR PDBsum; 1RZ6; -. DR AlphaFoldDB; P83787; -. DR SMR; P83787; -. DR DrugBank; DB04272; Citric acid. DR PeroxiBase; 5023; MaqDiHCcP_617. DR EvolutionaryTrace; P83787; -. 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; Cytochrome c-like domain; 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 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ5}; KW Calcium {ECO:0007829|PDB:1RZ5}; 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 Periplasm {ECO:0000256|ARBA:ARBA00022764}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT DOMAIN 29..137 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" FT DOMAIN 183..300 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" FT ACT_SITE 114 FT /note="EMO_00062 proton shuttle (general acid/base)" FT /evidence="ECO:0007829|PDB:1NML" FT BINDING 51 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ6" FT BINDING 51 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:1RZ5" FT BINDING 51 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 54 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ6" FT BINDING 54 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:1RZ5" FT BINDING 54 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 55 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 /ligand_part_note="axial binding residue" FT /evidence="ECO:0007829|PDB:1RZ5" FT BINDING 55 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 /ligand_part_note="axial binding residue" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ6" FT BINDING 55 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 71 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 /ligand_part_note="axial binding residue" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ6" FT BINDING 71 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 78 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ6" FT BINDING 79 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:1RZ5" FT BINDING 89 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1RZ5" FT BINDING 89 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1NML" FT BINDING 93 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ6" FT BINDING 94 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1RZ5" FT BINDING 197 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ5" FT BINDING 197 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 200 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ5" FT BINDING 200 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 201 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /ligand_part_note="axial binding residue" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ5" FT BINDING 201 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 216 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ5" FT BINDING 246 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1RZ5" FT BINDING 246 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ6" FT BINDING 256 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:1RZ5" FT BINDING 258 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:1RZ5" FT BINDING 260 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ5" FT BINDING 261 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ5" FT BINDING 275 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /ligand_part_note="axial binding residue" FT /evidence="ECO:0007829|PDB:1NML, ECO:0007829|PDB:1RZ5" FT BINDING 275 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 326 AA; 35355 MW; FAAABCAC1E4652FF CRC64; DNLMERANSM FEPIPKYPPV IDGNELTQAK VELGKMEFFE PRLSSSHLIS CNTCHNVGLG GDDELPTSIG HGWQKGPRNS PTVFNAVFNA AQFWDGRAAD LAEQAKGPVQ AGVEMSSTPD RVVATLKSMP EYIERFEDAF PGQENPVTFD NMAVAIEAYE ATLITPEAPF DKYLRGDTSA LNESEKEGLA LFMDRGCTAC HSGVNLGGQN YYPFGLVAKP GAEILPEGDK GRFSVTETAS DEYVFRASPL RNIELTAPYF HSGAVWSLEE AVAVMGTAQL GTELNNDEVK SIVAFLKTLT GNVPEVTYPV LPPSTANTPK PVDMIP //