EzCatDB: D00450
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DB codeD00450
CATH domainDomain 13.40.50.1400 : Rossmann fold
Domain 23.40.50.1400 : Rossmann foldCatalytic domain
E.C.4.99.1.1

CATH domainRelated DB codes (homologues)
3.40.50.1400 : Rossmann foldS00842,D00828

Enzyme Name
UniProtKBKEGG

P32396
Protein nameFerrochelataseferrochelatase
ferro-protoporphyrin chelatase
iron chelatase
heme synthetase
heme synthase
protoheme ferro-lyase
SynonymsEC 4.99.1.1
Heme synthase
Protoheme ferro-lyase
RefSeqNP_388894.1 (Protein)
NC_000964.3 (DNA/RNA sequence)
PfamPF00762 (Ferrochelatase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00860Porphyrin and chlorophyll metabolism

UniProtKB:Accession NumberP32396
Entry nameHEMH_BACSU
ActivityProtoheme + 2 H(+) = protoporphyrin + Fe(2+).
Subunit
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC02191C00023C00032C00080
CompoundProtoporphyrinFe2+ProtohemeH+
Typearomatic ring (with nitrogen atoms),carboxyl groupheavy metalaromatic ring (with nitrogen atoms),carboxyl group,heavy metalothers
ChEBI15430
18248
82664
17627
26355
15378
PubChem
23925

1038
            
1ak1A01UnboundUnboundUnbound 
1c1hA01UnboundUnboundUnbound 
1c9eA01UnboundUnboundUnbound 
1dozA01UnboundUnboundUnbound 
1ld3A01UnboundUnboundUnbound 
1n0iA01UnboundUnboundUnbound 
1ak1A02UnboundUnboundUnbound 
1c1hA02Analogue:MMPUnboundUnbound 
1c9eA02UnboundUnboundAnalogue:MP1 
1dozA02UnboundUnboundUnbound 
1ld3A02UnboundAnalogue:_ZNUnbound 
1n0iA02UnboundAnalogue:_CD 910Unbound 

Active-site residues
resource
Swiss-prot;P32396 & literature [6], [7], [9], [12] & [14]
pdbCatalytic residuesCofactor-binding residues
          
1ak1A01 
 
1c1hA01 
 
1c9eA01 
 
1dozA01 
 
1ld3A01 
 
1n0iA01 
 
1ak1A02ASP 261;GLU 264
HIS 183(metal binding)
1c1hA02ASP 261;GLU 264
HIS 183(metal binding)
1c9eA02ASP 261;GLU 264
HIS 183(metal binding)
1dozA02ASP 261;GLU 264
HIS 183(metal binding)
1ld3A02ASP 261;GLU 264
HIS 183(metal binding)
1n0iA02ASP 261;GLU 264
HIS 183(metal binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]

[7]p.1508
[9]p.1915-1916
[10]p.227-230
[12]p.159
[14]Fig.1

references
[1]
PubMed ID6390167
JournalMol Cell Biochem
Year1984
Volume64
Pages127-37
AuthorsCole SP, Marks GS
TitleFerrochelatase and N-alkylated porphyrins.
[2]
PubMed ID3895052
JournalNat Prod Rep
Year1985
Volume2
Pages19-47
AuthorsLeeper FJ
TitleThe biosynthesis of porphyrins, chlorophylls, and vitamin B12.
[3]
PubMed ID7947988
JournalBiochim Biophys Acta
Year1994
Volume1209
Pages95-100
AuthorsKohno H, Okuda M, Furukawa T, Tokunaga R, Taketani S
TitleSite-directed mutagenesis of human ferrochelatase: identification of histidine-263 as a binding site for metal ions.
[4]
PubMed ID8119288
JournalEur J Biochem
Year1994
Volume220
Pages201-8
AuthorsHansson M, Hederstedt L
TitlePurification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis.
[5]
PubMed ID8749860
JournalProteins
Year1995
Volume23
Pages607-9
AuthorsHansson M, Al-Karadaghi S
TitlePurification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase.
[6]
PubMed ID8662602
JournalJ Biol Chem
Year1996
Volume271
Pages11810-6
AuthorsGora M, Grzybowska E, Rytka J, Labbe-Bois R
TitleProbing the active-site residues in Saccharomyces cerevisiae ferrochelatase by directed mutagenesis. In vivo and in vitro analyses.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID98046098
PubMed ID9384565
JournalStructure
Year1997
Volume5
Pages1501-10
AuthorsAl-Karadaghi S, Hansson M, Nikonov S, Jonsson B, Hederstedt L
TitleCrystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis.
Related PDB1ak1
Related UniProtKBP32396
[8]
PubMed ID10582332
JournalInt J Biochem Cell Biol
Year1999
Volume31
Pages995-1000
AuthorsFerreira GC
TitleFerrochelatase.
[9]
PubMed ID11215517
JournalCell Mol Life Sci
Year2000
Volume57
Pages1909-26
AuthorsDailey HA, Dailey TA, Wu CK, Medlock AE, Wang KF, Rose JP, Wang BC
TitleFerrochelatase at the millennium: structures, mechanisms and [2Fe-2S] clusters.
[10]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID20171596
PubMed ID10704318
JournalJ Mol Biol
Year2000
Volume297
Pages221-32
AuthorsLecerof D, Fodje M, Hansson A, Hansson M, Al-Karadaghi S
TitleStructural and mechanistic basis of porphyrin metallation by ferrochelatase.
Related PDB1c1h,1c9e,1doz
Related UniProtKBP32396
[11]
PubMed ID11336654
JournalBiochem J
Year2001
Volume356
Pages217-22
AuthorsFranco R, Pereira AS, Tavares P, Mangravita A, Barber MJ, Moura I, Ferreira GC
TitleSubstitution of murine ferrochelatase glutamate-287 with glutamine or alanine leads to porphyrin substrate-bound variants.
[12]
PubMed ID11175906
JournalNat Struct Biol
Year2001
Volume8
Pages156-60
AuthorsWu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC
TitleThe 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.
Related PDB1hrk
[13]
PubMed ID12196143
JournalBiochem Soc Trans
Year2002
Volume30
Pages590-5
AuthorsDailey HA
TitleTerminal steps of haem biosynthesis.
[14]
PubMed ID12427010
JournalBiochemistry
Year2002
Volume41
Pages13499-506
AuthorsKarlberg T, Lecerof D, Gora M, Silvegren G, Labbe-Bois R, Hansson M, Al-Karadaghi S
TitleMetal binding to Saccharomyces cerevisiae ferrochelatase.
Related PDB1l8x
[15]
PubMed ID14981080
JournalJ Biol Chem
Year2004
Volume279
Pages19977-86
AuthorsShi Z, Ferreira GC
TitleProbing the active site loop motif of murine ferrochelatase by random mutagenesis.
[16]
PubMed ID12761666
JournalJ Biol Inorg Chem
Year2003
Volume8
Pages452-8
AuthorsLecerof D, Fodje MN, Alvarez Leon R, Olsson U, Hansson A, Sigfridsson E, Ryde U, Hansson M, Al-Karadaghi S
TitleMetal binding to Bacillus subtilis ferrochelatase and interaction between metal sites.
Related PDB1ld3,1n0i

comments
The reaction catalyzed by this enzyme is distinct from the other ones, such as elimination, catalyzed by other lyase enzymes.

createdupdated
2004-07-132009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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