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Database: UniProt
Entry: A0A0N0M3G9_9SPHN
LinkDB: A0A0N0M3G9_9SPHN
Original site: A0A0N0M3G9_9SPHN 
ID   A0A0N0M3G9_9SPHN        Unreviewed;       352 AA.
AC   A0A0N0M3G9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Cytochrome C peroxidase {ECO:0000313|EMBL:KPH67568.1};
GN   ORFNames=ADT71_02080 {ECO:0000313|EMBL:KPH67568.1};
OS   Novosphingobium sp. ST904.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1684385 {ECO:0000313|EMBL:KPH67568.1, ECO:0000313|Proteomes:UP000037878};
RN   [1] {ECO:0000313|EMBL:KPH67568.1, ECO:0000313|Proteomes:UP000037878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST904 {ECO:0000313|EMBL:KPH67568.1,
RC   ECO:0000313|Proteomes:UP000037878};
RA   Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F.,
RA   Vangronsveld J.;
RT   "Novosphingobium nitrophenolicus strain ST904 degrades p-nitrophenol and
RT   stimulates plant growth.";
RL   Submitted (JUL-2015) 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:KPH67568.1}.
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DR   EMBL; LGJH01000092; KPH67568.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0M3G9; -.
DR   STRING; 1684385.ADT71_02080; -.
DR   PATRIC; fig|1684385.3.peg.6241; -.
DR   Proteomes; UP000037878; 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:KPH67568.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:KPH67568.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037878}.
FT   DOMAIN          67..175
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          219..352
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         89
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                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         93
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         109
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         234
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         237
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         238
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   352 AA;  38598 MW;  E4061D4F004B8B58 CRC64;
     MGGSVAGRAQ QVAGEGRWGE ERRQRGAAGT LCGKPESWPR PRLGEGARFA EFGPLPRLPE
     ASPREKALAE IGRRMFDDPA LSRSGQIACA SCHSPELGMA DGLRTAFGHD RQRGRRNAQS
     LYAAAWMTPL FWDGRAATLE DQAIHPVLDG KEMAGTARLI EPRINRDETY RSAFEALNGH
     RRVTLQDAAA AIAAFERTLR PPRSRWSRVM ERGVAVLTDQ ELEGLHLFRT KAGCAACHNG
     PLLSDGRFHN LGISFYGRAR EDLGRYEVTQ DPADVGRFRT PSLLGVSRSA PYMHNGLFLT
     LENVVALYNG GGGRDRAQQP GRAPAPRPDP LVSRLDLTRE EQAALAAFLR TL
//
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