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Database: UniProt
Entry: A0A1M5C7L4_9BURK
LinkDB: A0A1M5C7L4_9BURK
Original site: A0A1M5C7L4_9BURK 
ID   A0A1M5C7L4_9BURK        Unreviewed;       368 AA.
AC   A0A1M5C7L4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Cytochrome c peroxidase {ECO:0000313|EMBL:SHF50743.1};
GN   ORFNames=SAMN02745117_02093 {ECO:0000313|EMBL:SHF50743.1};
OS   Lampropedia hyalina DSM 16112.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Lampropedia.
OX   NCBI_TaxID=1122156 {ECO:0000313|EMBL:SHF50743.1, ECO:0000313|Proteomes:UP000184327};
RN   [1] {ECO:0000313|EMBL:SHF50743.1, ECO:0000313|Proteomes:UP000184327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16112 {ECO:0000313|EMBL:SHF50743.1,
RC   ECO:0000313|Proteomes:UP000184327};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FQUZ01000025; SHF50743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5C7L4; -.
DR   STRING; 1122156.SAMN02745117_02093; -.
DR   OrthoDB; 9805202at2; -.
DR   Proteomes; UP000184327; Unassembled WGS sequence.
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   GO; GO:0004601; F:peroxidase activity; 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   Pfam; PF03150; CCP_MauG; 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:0000313|EMBL:SHF50743.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:SHF50743.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184327};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          82..215
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          234..368
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         104
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         107
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         108
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         249
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         252
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         253
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   368 AA;  39783 MW;  85DBA5E93014EB91 CRC64;
     MALGAVARDG APAEAVQCQQ ASADTAATAD ADASGWRIDC LRQQYQGKPG QWPRPWIDDG
     VPWQELAPVP PAQPPATAAE QARLILGTAL FHDPGLSGKG AVSCATCHQA VRSFTDGLPL
     AVGEDRLMGK RRSQPLFAAP FAPLLFWDGR AASLEEQARG PIENPLEMNS SLEKARAYIA
     SVPQYQQWAE AAFGSDGMAD DEWLSAIASF VRVLRPASTA ADAAIAGDTQ ALDDAQLLGL
     HLFRTKARCM NCHHGALLTD NRFHNIGLSF FGRRNQDLGR FEHTRDPADL GTFRTPSLRG
     VAQAGPWMHN GIFPNLSGIV RMYNAGMGNM ERGNTTDDPL TPVKSPHIQE LNLTDEEIKA
     LVAWLEVL
//
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