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Database: UniProt
Entry: A0A1M3BHY4_9ACTN
LinkDB: A0A1M3BHY4_9ACTN
Original site: A0A1M3BHY4_9ACTN 
ID   A0A1M3BHY4_9ACTN        Unreviewed;       375 AA.
AC   A0A1M3BHY4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Di-heme enzyme {ECO:0000313|EMBL:OJU83738.1};
GN   ORFNames=BGO11_09990 {ECO:0000313|EMBL:OJU83738.1};
OS   Solirubrobacterales bacterium 70-9.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales.
OX   NCBI_TaxID=1895833 {ECO:0000313|EMBL:OJU83738.1, ECO:0000313|Proteomes:UP000184118};
RN   [1] {ECO:0000313|EMBL:OJU83738.1, ECO:0000313|Proteomes:UP000184118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-9 {ECO:0000313|EMBL:OJU83738.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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}.
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:OJU83738.1}.
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DR   EMBL; MKSH01000113; OJU83738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3BHY4; -.
DR   Proteomes; UP000184118; 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   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.
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   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          197..349
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         60
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         63
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         64
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         213
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         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         217
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   375 AA;  41583 MW;  665283E9388D89E1 CRC64;
     MQAAGALTPP QVNNRWAWSL PPGMPQPRVP ADNPMTRGKV AIGHRLFYDV RLSGNETQSC
     STCHQPQLAF TDGKTTSVGS TGETLPRNSP SIVDSAYRTT LTWANPALTS LESQMDVPLF
     ATHPVELGVN DRNKGAILNR LRKDPWYAKR FPRVFPTAKH PVSWTNVIRS IASFERSIVS
     ANSKYDRYLQ GKAELSAEER RGMDLFMGEE GECHHCHGSF LFDDQDTYVG SPEERPKFHN
     TGLYNVGETG EYPYPNRGLY EISGKAKDMG AFRAPSLRNV VRTAPYMHDG SVATLKEVVE
     NYAAGGRVIT EGPYAGDGRK NPHKDPLISG IHLSERDEED LVAFLTTLTE PDFSKISRFA
     DPFKHGKNAA RGNDE
//
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