Ferrochelatase

Details

Name
Ferrochelatase
Synonyms
  • 4.99.1.1
  • Heme synthase
  • hemF
  • Protoheme ferro-lyase
Gene Name
hemH
Organism
Bacillus subtilis (strain 168)
Amino acid sequence
>lcl|BSEQ0010912|Ferrochelatase
MSRKKMGLLVMAYGTPYKEEDIERYYTHIRRGRKPEPEMLQDLKDRYEAIGGISPLAQIT
EQQAHNLEQHLNEIQDEITFKAYIGLKHIEPFIEDAVAEMHKDGITEAVSIVLAPHFSTF
SVQSYNKRAKEEAEKLGGLTITSVESWYDEPKFVTYWVDRVKETYASMPEDERENAMLIV
SAHSLPEKIKEFGDPYPDQLHESAKLIAEGAGVSEYAVGWQSEGNTPDPWLGPDVQDLTR
DLFEQKGYQAFVYVPVGFVADHLEVLYDNDYECKVVTDDIGASYYRPEMPNAKPEFIDAL
ATVVLKKLGR
Number of residues
310
Molecular Weight
35347.555
Theoretical pI
4.54
GO Classification
Functions
ferrochelatase activity / metal ion binding
Processes
heme biosynthetic process
Components
cytoplasm
General Function
Metal ion binding
Specific Function
Catalyzes the ferrous insertion into protoporphyrin IX.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0010913|Ferrochelatase (hemH)
GTGAGTAGAAAGAAAATGGGGCTTCTCGTGATGGCGTACGGCACGCCTTATAAGGAAGAA
GATATTGAACGTTATTATACACATATCAGAAGAGGCAGAAAGCCTGAACCTGAAATGCTT
CAAGATTTGAAAGACAGATACGAAGCGATTGGCGGCATTTCACCGCTTGCCCAAATCACA
GAACAGCAGGCGCATAATCTGGAACAGCACTTGAATGAAATTCAGGATGAGATTACGTTT
AAAGCGTATATCGGACTGAAGCATATCGAGCCGTTTATTGAAGACGCCGTAGCAGAGATG
CATAAGGATGGCATTACAGAAGCAGTCAGCATCGTGCTGGCGCCGCATTTCTCCACGTTC
AGCGTTCAGTCCTACAACAAACGCGCCAAAGAAGAGGCTGAAAAACTCGGCGGCTTAACG
ATTACGTCAGTTGAAAGCTGGTACGATGAACCGAAGTTCGTGACATATTGGGTTGACCGA
GTGAAGGAAACATATGCGTCAATGCCTGAGGATGAAAGAGAAAACGCAATGCTCATCGTA
TCCGCACACAGCCTGCCGGAAAAAATCAAAGAATTTGGAGACCCGTACCCGGACCAGCTT
CATGAATCGGCGAAATTAATTGCTGAAGGCGCAGGCGTTTCCGAATATGCTGTCGGCTGG
CAAAGTGAAGGGAACACGCCTGATCCTTGGCTCGGACCCGATGTTCAGGATTTAACACGT
GATTTATTCGAACAAAAAGGCTATCAAGCATTTGTATATGTTCCTGTTGGGTTTGTCGCG
GATCACTTAGAAGTGCTTTATGATAATGATTATGAATGCAAAGTGGTTACTGACGATATC
GGCGCAAGCTATTACCGGCCGGAAATGCCAAATGCCAAGCCTGAATTTATTGATGCTTTG
GCAACAGTCGTATTAAAAAAATTAGGACGTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP32396
UniProtKB Entry NameHEMH_BACSU
GenBank Protein ID143044
GenBank Gene IDM97208
General References
  1. 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. [Article]
  2. 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. 1998 Apr;144 ( Pt 4):859-75. [Article]
  3. 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. [Article]
  4. 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. [Article]
  5. Lecerof D, Fodje M, Hansson A, Hansson M, Al-Karadaghi S: Structural and mechanistic basis of porphyrin metallation by ferrochelatase. J Mol Biol. 2000 Mar 17;297(1):221-32. [Article]
  6. Hansson M, Gough SP, Brody SS: Structure prediction and fold recognition for the ferrochelatase family of proteins. Proteins. 1997 Apr;27(4):517-22. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01911N-MethylmesoporphyrinexperimentalunknownDetails
DB02188N-Methylmesoporphyrin containing copperexperimentalunknownDetails