ID W7BK38_9LIST Unreviewed; 251 AA.
AC W7BK38;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=PGRAN_07923 {ECO:0000313|EMBL:EUJ23571.1};
OS Listeria grandensis FSL F6-0971.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265819 {ECO:0000313|EMBL:EUJ23571.1, ECO:0000313|Proteomes:UP000019253};
RN [1] {ECO:0000313|EMBL:EUJ23571.1, ECO:0000313|Proteomes:UP000019253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL F6-971 {ECO:0000313|Proteomes:UP000019253};
RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT sp. nov., from agricultural and natural environments.";
RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
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:EUJ23571.1}.
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DR EMBL; AODD01000009; EUJ23571.1; -; Genomic_DNA.
DR RefSeq; WP_036066165.1; NZ_AODD01000009.1.
DR AlphaFoldDB; W7BK38; -.
DR STRING; 1265819.PGRAN_07923; -.
DR PATRIC; fig|1265819.5.peg.1584; -.
DR OrthoDB; 9773646at2; -.
DR Proteomes; UP000019253; 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:EUJ23571.1};
KW Peroxidase {ECO:0000313|EMBL:EUJ23571.1}.
SQ SEQUENCE 251 AA; 29059 MW; 7EFEE4B276DD15BD CRC64;
MNEAVKTLDG WFSLHDFRSI DWPALREVSP ENRESMLNEL QNFLGDMDIT KKMGEGEHTI
YSILGQKADL LFFTLRPTLE GLNEVENQLN KLRIADYLLP AYSYISVVEL SNYLANHMAK
GEDPYENKHV RERLYPELPA RKHICFYPMT KKRSLSDNWY MLPMEERQAM IRDHGAIGRT
YAGKIKQIIG GSIGLDDFEW GVTLFADDAL DFKRIVTEMR FDESSARFAE FGSFLVGNYV
ATDALQDFFR I
//
