CPLM-005075

Genbank Nucleotide ID

Ferrochelatase, mitochondrial

Protein Synonyms/Alias

Heme synthase; Protoheme ferro-lyase

Mus musculus (Mouse)

Position	Peptide	Type	References
56	VHHAKTTKPQAQPER	acetylation	[1, 2, 3]
105	MTLPIQNKLAPFIAK	ubiquitination	[4]
135	PIKMWTSKQGEGMVK	acetylation	[5]
135	PIKMWTSKQGEGMVK	succinylation	[5]
142	KQGEGMVKLLDELSP	acetylation	[1, 2, 3]
213	YYNEVGQKPTMKWST	acetylation	[1]
249	LNHFPEEKRSEVVIL	acetylation	[1, 3]
283	EVGATVHKVMEKLGY	acetylation	[1, 2, 3]
287	TVHKVMEKLGYPNPY	acetylation	[1, 2, 3, 5, 6]
287	TVHKVMEKLGYPNPY	succinylation	[5]
301	YRLVWQSKVGPVPWL	acetylation	[2]
376	NGNPLFSKALADLVH	acetylation	[1, 2, 3]
390	HSHIQSNKLCSTQLS	acetylation	[2]
412	NPVCRKTKSFFTSQQ	acetylation	[2, 3, 5]
412	NPVCRKTKSFFTSQQ	succinylation	[5]

[1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
[3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]

Functional Description

Catalyzes the ferrous insertion into protoporphyrin IX.

ACT_SITE 227 227 By similarity.
ACT_SITE 380 380 By similarity.
METAL 193 193 Iron-sulfur (2Fe-2S).
METAL 400 400 Iron-sulfur (2Fe-2S) (By similarity).
METAL 403 403 Iron-sulfur (2Fe-2S) (By similarity).
METAL 408 408 Iron-sulfur (2Fe-2S) (By similarity).

2Fe-2S; Complete proteome; Direct protein sequencing; Disease mutation; Heme biosynthesis; Iron; Iron-sulfur; Lyase; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Porphyrin biosynthesis; Reference proteome; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005743; C:mitochondrial inner membrane; TAS:MGI.
GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO:0004325; F:ferrochelatase activity; IDA:MGI.
GO:0020037; F:heme binding; IDA:MGI.
GO:0005506; F:iron ion binding; IDA:MGI.
GO:0030350; F:iron-responsive element binding; IDA:MGI.
GO:0008203; P:cholesterol metabolic process; IMP:MGI.
GO:0009589; P:detection of UV; IMP:MGI.
GO:0030218; P:erythrocyte differentiation; IMP:MGI.
GO:0006783; P:heme biosynthetic process; IDA:MGI.
GO:0055072; P:iron ion homeostasis; IMP:MGI.
GO:0046501; P:protoporphyrinogen IX metabolic process; IGI:MGI.
GO:0010999; P:regulation of eIF2 alpha phosphorylation by heme; IMP:MGI.
GO:0046984; P:regulation of hemoglobin biosynthetic process; IGI:MGI.
GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:MGI.

IPR001015; Ferrochelatase.
IPR019772; Ferrochelatase_AS.

PF00762; Ferrochelatase

PS00534; FERROCHELATASE