CHDC_BACSU
ID CHDC_BACSU Reviewed; 254 AA.
AC P39645;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Coproheme decarboxylase {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000303|PubMed:25646457};
DE EC=1.3.98.5 {ECO:0000255|HAMAP-Rule:MF_01442};
DE AltName: Full=Coproheme III oxidative decarboxylase {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305};
DE AltName: Full=Hydrogen peroxide-dependent heme synthase {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305};
DE AltName: Full=Iron-coproporphyrin oxidative decarboxylase {ECO:0000303|PubMed:25711532};
GN Name=chdC {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000303|PubMed:28123057};
GN Synonyms=hemQ {ECO:0000303|PubMed:20543190}, ywfI;
GN OrderedLocusNames=BSU37670; ORFNames=ipa-87r;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PATHWAY.
RX PubMed=20543190; DOI=10.1074/jbc.m110.142604;
RA Dailey T.A., Boynton T.O., Albetel A.N., Gerdes S., Johnson M.K.,
RA Dailey H.A.;
RT "Discovery and characterization of HemQ: an essential heme biosynthetic
RT pathway component.";
RL J. Biol. Chem. 285:25978-25986(2010).
RN [4]
RP FUNCTION, AND PATHWAY.
RX PubMed=25646457; DOI=10.1073/pnas.1416285112;
RA Dailey H.A., Gerdes S., Dailey T.A., Burch J.S., Phillips J.D.;
RT "Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway
RT that does not use protoporphyrin.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:2210-2215(2015).
RN [5]
RP PATHWAY, AND REVIEW.
RX PubMed=25711532; DOI=10.1016/j.abb.2015.02.017;
RA Dailey H.A., Gerdes S.;
RT "HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme
RT synthesis in Firmicutes and Actinobacteria.";
RL Arch. Biochem. Biophys. 574:27-35(2015).
RN [6]
RP NOMENCLATURE, AND REVIEW.
RX PubMed=28123057; DOI=10.1128/mmbr.00048-16;
RA Dailey H.A., Dailey T.A., Gerdes S., Jahn D., Jahn M., O'Brian M.R.,
RA Warren M.J.;
RT "Prokaryotic heme biosynthesis: multiple pathways to a common essential
RT product.";
RL Microbiol. Mol. Biol. Rev. 81:e00048-e00048(2017).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis
CC (PubMed:25646457). Catalyzes the decarboxylation of Fe-coproporphyrin
CC III (coproheme) to heme b (protoheme IX), the last step of the pathway
CC (By similarity). The reaction occurs in a stepwise manner with a three-
CC propionate harderoheme intermediate (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000269|PubMed:25646457}.
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:0000255|HAMAP-
CC Rule:MF_01442};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56517;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442};
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:0000255|HAMAP-
CC Rule:MF_01442};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57941;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442};
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:0000255|HAMAP-Rule:MF_01442};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57945;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442};
CC -!- COFACTOR:
CC Name=Fe-coproporphyrin III; Xref=ChEBI:CHEBI:68438;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01442};
CC Note=Fe-coproporphyrin III acts as both substrate and redox cofactor.
CC {ECO:0000255|HAMAP-Rule:MF_01442};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01442,
CC ECO:0000269|PubMed:20543190, ECO:0000269|PubMed:25646457,
CC ECO:0000305|PubMed:25711532}.
CC -!- SIMILARITY: Belongs to the ChdC family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01442, ECO:0000305}.
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DR EMBL; X73124; CAA51643.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15794.1; -; Genomic_DNA.
DR PIR; S39742; S39742.
DR RefSeq; NP_391647.2; NC_000964.3.
DR RefSeq; WP_003242896.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39645; -.
DR SMR; P39645; -.
DR STRING; 224308.BSU37670; -.
DR jPOST; P39645; -.
DR PaxDb; P39645; -.
DR PRIDE; P39645; -.
DR EnsemblBacteria; CAB15794; CAB15794; BSU_37670.
DR GeneID; 936512; -.
DR KEGG; bsu:BSU37670; -.
DR PATRIC; fig|224308.179.peg.4079; -.
DR eggNOG; COG3253; Bacteria.
DR InParanoid; P39645; -.
DR OMA; RYTMWSV; -.
DR BioCyc; BSUB:BSU37670-MON; -.
DR BioCyc; MetaCyc:BSU37670-MON; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000001570; Chromosome.
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:InterPro.
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; PTHR36843; 1.
DR Pfam; PF06778; Chlor_dismutase; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
PE 3: Inferred from homology;
KW Heme; Heme biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Coproheme decarboxylase"
FT /id="PRO_0000049971"
FT ACT_SITE 150
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 136
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 150..154
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 177
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:0000255|HAMAP-Rule:MF_01442"
FT BINDING 190
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
FT BINDING 228
FT /ligand="Fe-coproporphyrin III"
FT /ligand_id="ChEBI:CHEBI:68438"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01442"
SQ SEQUENCE 254 AA; 29505 MW; 14B6AC68C0682D08 CRC64;
MSEQQMTNEA AKTLDGWYAL HDFRTMDWAS WKLLSSDERQ SIIHEFTGLL EKWGVAQKEG
KGSQTLYSIV GQKADFMLMI LRPTMEELNQ IELEFNKSRL AEFTIPAYSY VSVVELSNYL
ASGDGDPYEN PHVRARLYPE LPESKYVCFY PMDKRRSGND NWYMLSMEER RNLMRSHGLI
GRSYAGKVKQ IITGSVGFDD YEWGVTLFSD DVLQFKKLVY EMRFDEVSAR YGEFGSFFVG
NHLSLDTLPQ FLYV
