Hmdb loader
Identification
HMDB Protein ID HMDBP13348
Secondary Accession Numbers None
Name Coproporphyrin III ferrochelatase
Synonyms
  1. Water-soluble ferrochelatase
Gene Name CPFC
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457, PubMed:25908396). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457, PubMed:25908396). It can also insert iron into protoporphyrin IX (PubMed:1459957, PubMed:8119288, PubMed:21052751, PubMed:25646457). Has weaker activity with 2,4 disulfonate, deuteroporphyrin and 2,4 hydroxyethyl (PubMed:25646457, PubMed:12761666). In vitro, can also use Zn(2+) or Cu(2+) (PubMed:8119288, PubMed:16140324, PubMed:21052751, PubMed:12761666).
Pathways
  • Biosynthesis of cofactors
  • Biosynthesis of secondary metabolites
  • Porphyrin and chlorophyll metabolism
  • protoheme biosynthesis
Reactions Not Available
GO Classification
Biological Process
heme biosynthetic process
Cellular Component
cytoplasm
Molecular Function
metal ion binding
ferrochelatase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 310
Molecular Weight 35347.555
Theoretical pI 4.9
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P32396
UniProtKB/Swiss-Prot Entry Name CPFC_BACSU
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azevedo V, Bertero MG, Bessieres P, Bolotin A, Borchert S, Borriss R, Boursier L, Brans A, Braun M, Brignell SC, Bron S, Brouillet S, Bruschi CV, Caldwell B, Capuano V, Carter NM, Choi SK, Cordani JJ, Connerton IF, Cummings NJ, Daniel RA, Denziot F, Devine KM, Dusterhoft A, Ehrlich SD, Emmerson PT, Entian KD, Errington J, Fabret C, Ferrari E, Foulger D, Fritz C, Fujita M, Fujita Y, Fuma S, Galizzi A, Galleron N, Ghim SY, Glaser P, Goffeau A, Golightly EJ, Grandi G, Guiseppi G, Guy BJ, Haga K, Haiech J, Harwood CR, Henaut A, Hilbert H, Holsappel S, Hosono S, Hullo MF, Itaya M, Jones L, Joris B, Karamata D, Kasahara Y, Klaerr-Blanchard M, Klein C, Kobayashi Y, Koetter P, Koningstein G, Krogh S, Kumano M, Kurita K, Lapidus A, Lardinois S, Lauber J, Lazarevic V, Lee SM, Levine A, Liu H, Masuda S, Mauel C, Medigue C, Medina N, Mellado RP, Mizuno M, Moestl D, Nakai S, Noback M, Noone D, O'Reilly M, Ogawa K, Ogiwara A, Oudega B, Park SH, Parro V, Pohl TM, Portelle D, Porwollik S, Prescott AM, Presecan E, Pujic P, Purnelle B, Rapoport G, Rey M, Reynolds S, Rieger M, Rivolta C, Rocha E, Roche B, Rose M, Sadaie Y, Sato T, Scanlan E, Schleich S, Schroeter R, Scoffone F, Sekiguchi J, Sekowska A, Seror SJ, Serror P, Shin BS, Soldo B, Sorokin A, Tacconi E, Takagi T, Takahashi H, Takemaru K, Takeuchi M, Tamakoshi A, Tanaka T, Terpstra P, Togoni A, Tosato V, Uchiyama S, Vandebol M, Vannier F, Vassarotti A, Viari A, Wambutt R, Wedler H, Weitzenegger T, Winters P, Wipat A, Yamamoto H, Yamane K, Yasumoto K, Yata K, Yoshida K, Yoshikawa HF, Zumstein E, Yoshikawa H, Danchin A: The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature. 1997 Nov 20;390(6657):249-56. doi: 10.1038/36786. [PubMed:9384377 ]
  2. Hansson M, Hederstedt L: Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. J Bacteriol. 1992 Dec;174(24):8081-93. doi: 10.1128/jb.174.24.8081-8093.1992. [PubMed:1459957 ]
  3. Noback MA, Holsappel S, Kiewiet R, Terpstra P, Wambutt R, Wedler H, Venema G, Bron S: The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene. Microbiology (Reading). 1998 Apr;144 ( Pt 4):859-875. doi: 10.1099/00221287-144-4-859. [PubMed:9579061 ]
  4. Hansson M, Hederstedt L: Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis. Eur J Biochem. 1994 Feb 15;220(1):201-8. doi: 10.1111/j.1432-1033.1994.tb18615.x. [PubMed:8119288 ]
  5. Dailey HA, Gerdes S, Dailey TA, Burch JS, Phillips JD: Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin. Proc Natl Acad Sci U S A. 2015 Feb 17;112(7):2210-5. doi: 10.1073/pnas.1416285112. Epub 2015 Feb 2. [PubMed:25646457 ]
  6. Dailey HA, Gerdes S: HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme synthesis in Firmicutes and Actinobacteria. Arch Biochem Biophys. 2015 May 15;574:27-35. doi: 10.1016/j.abb.2015.02.017. Epub 2015 Feb 21. [PubMed:25711532 ]
  7. Lobo SA, Scott A, Videira MA, Winpenny D, Gardner M, Palmer MJ, Schroeder S, Lawrence AD, Parkinson T, Warren MJ, Saraiva LM: Staphylococcus aureus haem biosynthesis: characterisation of the enzymes involved in final steps of the pathway. Mol Microbiol. 2015 Aug;97(3):472-87. doi: 10.1111/mmi.13041. Epub 2015 May 26. [PubMed:25908396 ]
  8. Dailey HA, Dailey TA, Gerdes S, Jahn D, Jahn M, O'Brian MR, Warren MJ: Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product. Microbiol Mol Biol Rev. 2017 Jan 25;81(1). pii: 81/1/e00048-16. doi: 10.1128/MMBR.00048-16. Print 2017 Mar. [PubMed:28123057 ]
  9. Hansson M, Gough SP, Brody SS: Structure prediction and fold recognition for the ferrochelatase family of proteins. Proteins. 1997 Apr;27(4):517-22. [PubMed:9141132 ]
  10. Al-Karadaghi S, Hansson M, Nikonov S, Jonsson B, Hederstedt L: Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure. 1997 Nov 15;5(11):1501-10. doi: 10.1016/s0969-2126(97)00299-2. [PubMed:9384565 ]
  11. Lecerof D, Fodje MN, Alvarez Leon R, Olsson U, Hansson A, Sigfridsson E, Ryde U, Hansson M, Al-Karadaghi S: Metal binding to Bacillus subtilis ferrochelatase and interaction between metal sites. J Biol Inorg Chem. 2003 Apr;8(4):452-8. doi: 10.1007/s00775-002-0436-1. Epub 2003 Jan 18. [PubMed:12761666 ]
  12. Shipovskov S, Karlberg T, Fodje M, Hansson MD, Ferreira GC, Hansson M, Reimann CT, Al-Karadaghi S: Metallation of the transition-state inhibitor N-methyl mesoporphyrin by ferrochelatase: implications for the catalytic reaction mechanism. J Mol Biol. 2005 Oct 7;352(5):1081-90. doi: 10.1016/j.jmb.2005.08.002. [PubMed:16140324 ]
  13. Hansson MD, Karlberg T, Rahardja MA, Al-Karadaghi S, Hansson M: Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX. Biochemistry. 2007 Jan 9;46(1):87-94. doi: 10.1021/bi061760a. [PubMed:17198378 ]
  14. Hansson MD, Karlberg T, Soderberg CA, Rajan S, Warren MJ, Al-Karadaghi S, Rigby SE, Hansson M: Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase. J Biol Inorg Chem. 2011 Feb;16(2):235-42. doi: 10.1007/s00775-010-0720-4. Epub 2010 Nov 4. [PubMed:21052751 ]