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Database: UniProt
Entry: I3E177_BACMT
LinkDB: I3E177_BACMT
Original site: I3E177_BACMT 
ID   I3E177_BACMT            Unreviewed;       248 AA.
AC   I3E177;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Coproheme decarboxylase {ECO:0000256|ARBA:ARBA00014413};
DE   AltName: Full=Coproheme III oxidative decarboxylase {ECO:0000256|ARBA:ARBA00029882};
DE   AltName: Full=Hydrogen peroxide-dependent heme synthase {ECO:0000256|ARBA:ARBA00030236};
GN   ORFNames=PB1_07802 {ECO:0000313|EMBL:EIJ80248.1};
OS   Bacillus methanolicus PB1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=997296 {ECO:0000313|EMBL:EIJ80248.1, ECO:0000313|Proteomes:UP000010523};
RN   [1] {ECO:0000313|EMBL:EIJ80248.1, ECO:0000313|Proteomes:UP000010523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1 {ECO:0000313|EMBL:EIJ80248.1,
RC   ECO:0000313|Proteomes:UP000010523};
RX   PubMed=22610424; DOI=10.1128/AEM.00703-12;
RA   Heggeset T.M., Krog A., Balzer S., Wentzel A., Ellingsen T.E.,
RA   Brautaset T.;
RT   "Genome Sequence of Thermotolerant Bacillus methanolicus: Features and
RT   Regulation Related to Methylotrophy and Production of L-Lysine and L-
RT   Glutamate from Methanol.";
RL   Appl. Environ. Microbiol. 78:5170-5181(2012).
CC   -!- SIMILARITY: Belongs to the ChdC family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009276}.
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:EIJ80248.1}.
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DR   EMBL; AFEU01000002; EIJ80248.1; -; Genomic_DNA.
DR   RefSeq; WP_003351683.1; NZ_AFEU01000002.1.
DR   AlphaFoldDB; I3E177; -.
DR   STRING; 997296.PB1_07802; -.
DR   PATRIC; fig|997296.3.peg.1658; -.
DR   eggNOG; COG3253; Bacteria.
DR   OrthoDB; 9773646at2; -.
DR   Proteomes; UP000010523; Unassembled WGS sequence.
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   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01442; Coproheme_decarbox_1; 1.
DR   InterPro; IPR031332; CHDC.
DR   InterPro; IPR010644; ChdC/CLD.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   PANTHER; PTHR36843:SF1; COPROHEME DECARBOXYLASE; 1.
DR   PANTHER; PTHR36843; HEME-DEPENDENT PEROXIDASE YWFI-RELATED; 1.
DR   Pfam; PF06778; Chlor_dismutase; 1.
DR   SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617};
KW   Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:EIJ80248.1};
KW   Peroxidase {ECO:0000313|EMBL:EIJ80248.1}.
SQ   SEQUENCE   248 AA;  29111 MW;  72FED15DDD385DD3 CRC64;
     MSEATQTLDG WYSLHDFRAI DWTAWKMLSS DERQAAIHEF LGLLEKWNAT QNRKEGSHVL
     YTIVGQKADF MMMILRPTME ELNEIETEFN KTKLAGYTIP TYSYVSVVEL SNYLPSEGDP
     YENPQVRARL YPILPKSKYI CFYPMDKRRQ GNDNWYMLPM EERRNLMKSH SMIGRKYAGL
     VKQIITGSVG FDDYEWGVTL FSDDVLQFKK LVYEMRFDEV SARYGEFGSF FVGNLLEDDR
     ISKFLHVN
//
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