ID E4PQ72_MARAH Unreviewed; 398 AA.
AC E4PQ72;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Di-heme cytochrome c peroxidase {ECO:0000313|EMBL:ADP98937.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:ADP98937.1};
GN OrderedLocusNames=HP15_3173 {ECO:0000313|EMBL:ADP98937.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP98937.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP98937.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) 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; CP001978; ADP98937.1; -; Genomic_DNA.
DR RefSeq; WP_014578383.1; NC_017506.1.
DR AlphaFoldDB; E4PQ72; -.
DR STRING; 225937.HP15_3173; -.
DR KEGG; mad:HP15_3173; -.
DR PATRIC; fig|225937.3.peg.3196; -.
DR eggNOG; COG1858; Bacteria.
DR HOGENOM; CLU_034652_3_1_6; -.
DR Proteomes; UP000007077; 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 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; IPR023929; Di-heme_enz_MXAN0977.
DR InterPro; IPR026259; MauG/Cytc_peroxidase.
DR NCBIfam; TIGR04039; MXAN_0977_Heme2; 1.
DR PANTHER; PTHR30600:SF12; BLL6722 PROTEIN; 1.
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; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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:ADP98937.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Peroxidase {ECO:0000313|EMBL:ADP98937.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003187270"
FT DOMAIN 224..376
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 88
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 91
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 92
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 240
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 243
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 244
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 398 AA; 43673 MW; 255112F946F7A323 CRC64;
MFVKKLRAGP VWPALLLCVS ALLSGCLESS STTVDDQGAR VSSFDWGLPE SIPLPREPED
NPMTEAKFQL GRHLFYDRRL STNSTVSCAG CHQQDKAFSD GVARPFGATG EQHPRNSQPL
VNVAWASTVT WGNPSLGTIE RQILLPLFGD DPVEHGLNEA NSEQVLRSLQ ADPTYGPLFQ
AAFPEQNDPL FGDLAWDNVV KALASFVRGL VSFDSKFDRG ELSASAQRGE RLFNSERLEC
FHCHAGYNFS DATVDRLTTF NQLIFHNTGL YNVDGMGGYP EPNTGRHEVT GDPDHMGQFR
APTLRNIALT APYNHDGSVE TLEGVIRNYA AGGRVLITGP NPGDGRMNPF KDGFITSFAI
SEQEIDDVVA FLESLTDESF ITNPRFSNPW NSTGQETP
//
