Q54IA8 (HEMH_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ferrochelatase, mitochondrial
EC=4.99.1.1

Alternative name(s):
Heme synthase
Protoheme ferro-lyase

Gene names

Name:	hemH
ORF Names:	DDB_G0288891

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the ferrous insertion into protoporphyrin IX By similarity.
Catalytic activity	Protoheme + 2 H+ = protoporphyrin + Fe2+.
Cofactor	Binds 1 2Fe-2S cluster By similarity.
Pathway	Porphyrin metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.
Sequence similarities	Belongs to the ferrochelatase family.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from sequence or structural similarity. Source: dictyBase
Cellular component	mitochondrial inner membrane Inferred from sequence or structural similarity. Source: dictyBase
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW ferrochelatase activity Inferred from sequence or structural similarity. Source: dictyBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 29	29	Mitochondrion Potential
	Chain	30 – 423	394	Ferrochelatase, mitochondrial		PRO_0000327542
Sites
	Active site	207	1	By similarity
	Active site	380	1	By similarity
	Metal binding	173	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	401	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	404	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	411	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54IA8 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 16089D79F5CD2FAF	FASTA	423	47,990
	10 20 30 40 50 60 MISRKIISTI NSKTFYNKSL SYCTVNNNKN TTININNNNE KPKIKTGILM LNLGGPSKLE 70 80 90 100 110 120 EVEPFLTRLF TDKEIFKLPF QKYTGTLIAK RRSNAVMKLY EAIGGGSPIR KWTEKQGELL 130 140 150 160 170 180 SSMMDKISPE TAPHKHYIGF RYSDPLIADT LDQMENDNVE RVVAFSQYPQ YSCTTTGSSL 190 200 210 220 230 240 NNLWKTLEEK QMQSKFKWSV IDRWQDHKGF IDATIHKIKK AYNQFNSKLR ELDIDDVDAN 250 260 270 280 290 300 NNNNNNKPVL VFSAHSLPMS TVEKGDPYPQ EVAETVCRVM DGLGIRDEET GKPLEYILAW 310 320 330 340 350 360 QSKVGPLPWL SPKTSFVIEQ LAKKGRNAIV IPIAFTSDHI ETLSEIDIEL QHLAKKCGMK 370 380 390 400 410 420 LLVRSESLND DPLIISAMAD LVNTHLKSNK TIHSNQYHLK CPGCKDDSTF CRTISNPIQA LKL

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000126 Genomic DNA. Translation: EAL62969.1.
RefSeq	XP_636471.1. XM_631379.1.
3D structure databases
HSSP	HSSP built from PDB template 1HRK based on UniProtKB P22830.
ProteinModelPortal	Q54IA8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54IA8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0231413; DDB0231413; DDB_G0288891.
GeneID	8626854.
GenomeReviews	Gene locus hemH in contig CM000154_GR.
KEGG	ddi:DDB_G0288891.
Organism-specific databases
dictyBase	DDB_G0288891. hemH.
Phylogenomic databases
eggNOG	KOG1321.
GeneTree	EPrGT00050000005135.
HOGENOM	HBG697135.
OMA	LQKPLAW.
PhylomeDB	Q54IA8.
ProtClustDB	CLSZ2456097.
Family and domain databases
InterPro	IPR001015. Ferrochelatase. IPR019772. Ferrochelatase_AS. [Graphical view]
KO	K01772.
PANTHER	PTHR11108. Ferrochelatase. 1 hit.
Pfam	PF00762. Ferrochelatase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00109. HemH. 1 hit.
PROSITE	PS00534. FERROCHELATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEMH_DICDI

Accession

Primary (citable) accession number: Q54IA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)