GenomeNet

Database: UniProt
Entry: D2SEC2_GEOOG
LinkDB: D2SEC2_GEOOG
Original site: D2SEC2_GEOOG 
ID   D2SEC2_GEOOG            Unreviewed;       238 AA.
AC   D2SEC2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Coproheme decarboxylase {ECO:0000256|HAMAP-Rule:MF_02244};
DE            EC=1.3.98.5 {ECO:0000256|HAMAP-Rule:MF_02244};
DE   AltName: Full=Coproheme III oxidative decarboxylase {ECO:0000256|HAMAP-Rule:MF_02244};
DE   AltName: Full=Hydrogen peroxide-dependent heme synthase {ECO:0000256|HAMAP-Rule:MF_02244};
GN   Name=chdC {ECO:0000256|HAMAP-Rule:MF_02244};
GN   OrderedLocusNames=Gobs_1891 {ECO:0000313|EMBL:ADB74594.1};
OS   Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS   A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB74594.1, ECO:0000313|Proteomes:UP000001382};
RN   [1] {ECO:0000313|EMBL:ADB74594.1, ECO:0000313|Proteomes:UP000001382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC   NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RX   PubMed=21304698;
RA   Ivanova N., Sikorski J., Jando M., Munk C., Lapidus A., Glavina Del Rio T.,
RA   Copeland A., Tice H., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Meincke L.,
RA   Brettin T., Detter J.C., Detter J.C., Rohde M., Goeker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT   "Complete genome sequence of Geodermatophilus obscurus type strain (G-
RT   20).";
RL   Stand. Genomic Sci. 2:158-167(2010).
RN   [2] {ECO:0000313|Proteomes:UP000001382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC   NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC       Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to
CC       heme b (protoheme IX), the last step of the pathway. The reaction
CC       occurs in a stepwise manner with a three-propionate intermediate.
CC       {ECO:0000256|HAMAP-Rule:MF_02244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe-coproporphyrin III + 2 H(+) + 2 H2O2 = 2 CO2 + 4 H2O + heme
CC         b; Xref=Rhea:RHEA:56516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:60344,
CC         ChEBI:CHEBI:68438; EC=1.3.98.5; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02244};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe-coproporphyrin III + H(+) + H2O2 = CO2 + 2 H2O +
CC         harderoheme III; Xref=Rhea:RHEA:57940, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:68438, ChEBI:CHEBI:142463; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02244};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O2 + harderoheme III = CO2 + 2 H2O + heme b;
CC         Xref=Rhea:RHEA:57944, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:60344,
CC         ChEBI:CHEBI:142463; Evidence={ECO:0000256|HAMAP-Rule:MF_02244};
CC   -!- COFACTOR:
CC       Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02244};
CC       Note=Fe-coproporphyrin III acts as both substrate and redox cofactor.
CC       {ECO:0000256|HAMAP-Rule:MF_02244};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02244}.
CC   -!- SIMILARITY: Belongs to the ChdC family. Type 2 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02244}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001867; ADB74594.1; -; Genomic_DNA.
DR   RefSeq; WP_012948033.1; NC_013757.1.
DR   AlphaFoldDB; D2SEC2; -.
DR   STRING; 526225.Gobs_1891; -.
DR   KEGG; gob:Gobs_1891; -.
DR   eggNOG; COG3253; Bacteria.
DR   HOGENOM; CLU_076582_1_0_11; -.
DR   OrthoDB; 9773646at2; -.
DR   Proteomes; UP000001382; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016634; F:oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0006785; P:heme B biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02244; Coproheme_decarbox_2; 1.
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, ECO:0000256|HAMAP-Rule:MF_02244};
KW   Heme biosynthesis {ECO:0000256|HAMAP-Rule:MF_02244};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02244};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_02244}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001382}.
FT   ACT_SITE        140
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02244"
FT   BINDING         163
FT                   /ligand="Fe-coproporphyrin III"
FT                   /ligand_id="ChEBI:CHEBI:68438"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02244"
SQ   SEQUENCE   238 AA;  27697 MW;  C4CFE712ED3A20E6 CRC64;
     MSEQTDQRSI GKRANELNAA IRYTMWSVFR LARPLGEEQR TAVADEVQGL LDELAGKDVV
     VRGTYDVAGF RADADLMVWW HAETPEALQE AYTRLRRTAL GRHLEPVWSQ LALHRPAEFN
     RSHIPAFLAD EEPRRYVCVY PFVRSYEWYL LPDEERRDML KEHGMQARPY PDVRANTVAA
     FALGDYEWML AFEADELHRI VDLMRDLRAS RARRHVREEV PFYTGVRKPV AELVADLP
//
DBGET integrated database retrieval system