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Database: UniProt
Entry: J2LFB7_9SPHN
LinkDB: J2LFB7_9SPHN
Original site: J2LFB7_9SPHN 
ID   J2LFB7_9SPHN            Unreviewed;       334 AA.
AC   J2LFB7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Cytochrome c peroxidase {ECO:0000313|EMBL:EJK86171.1};
GN   ORFNames=PMI04_00588 {ECO:0000313|EMBL:EJK86171.1};
OS   Sphingobium sp. AP49.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK86171.1};
RN   [1] {ECO:0000313|EMBL:EJK86171.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP49 {ECO:0000313|EMBL:EJK86171.1};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJK86171.1}.
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DR   EMBL; AJVL01000009; EJK86171.1; -; Genomic_DNA.
DR   RefSeq; WP_007705533.1; NZ_CP124576.1.
DR   AlphaFoldDB; J2LFB7; -.
DR   STRING; 1144307.PMI04_00588; -.
DR   PATRIC; fig|1144307.3.peg.551; -.
DR   eggNOG; COG1858; Bacteria.
DR   OrthoDB; 9805202at2; -.
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: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; 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:EJK86171.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:EJK86171.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          49..188
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          202..313
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         71
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         74
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         75
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         216
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         219
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         220
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   334 AA;  34532 MW;  BC7545204DFF6396 CRC64;
     MRLGGAAIIG AAALLATGLG AVRPTWRWPA LPAGVAAPSI PADNGMSAAK VALGRRLFYD
     RALSADGSMA CADCHQQEKG FADGLSTHRG VMGDMGVRNV PGLANVAWRS GLTWTEAGLS
     TLEQQAMVPM TGTKPVEMGL AQDDAGLARR IGADPCYRRM FAAAFPGAQG GVGFAEVTAA
     LAVFQRTMIS FGSAHDRGAL SPLAARGAAQ FKAAGCADCH SGTDLTDSKT HYVGTSAPRE
     ADSAAYGGKP LPPGVEPPPE QFRTPSLRNV AVTGPWLHDG QSPTIESAIR RHAAPMLADV
     DMPALLAFLD ALTDHDFLNN AALARPPATC PIPT
//
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