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Protein

Ferrochelatase, mitochondrial

Gene

HEM15

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ferrous insertion into protoporphyrin IX.

Catalytic activityi

Protoheme + 2 H+ = protoporphyrin + Fe2+.

Pathwayi: protoheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes protoheme from protoporphyrin-IX.
Proteins known to be involved in this subpathway in this organism are:
  1. Ferrochelatase, mitochondrial (HEM15)
This subpathway is part of the pathway protoheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protoheme from protoporphyrin-IX, the pathway protoheme biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei351 – 3511By similarity

GO - Molecular functioni

  • ferrochelatase activity Source: SGD

GO - Biological processi

  • heme biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Iron

Enzyme and pathway databases

BioCyciYEAST:YOR176W-MONOMER.
BRENDAi4.99.1.1. 984.
ReactomeiR-SCE-189451. Heme biosynthesis.
SABIO-RKP16622.
UniPathwayiUPA00252; UER00325.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferrochelatase, mitochondrial (EC:4.99.1.1)
Alternative name(s):
Heme synthase
Protoheme ferro-lyase
Gene namesi
Name:HEM15
Ordered Locus Names:YOR176W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR176W.
SGDiS000005702. HEM15.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3131Mitochondrion1 PublicationAdd
BLAST
Chaini32 – 393362Ferrochelatase, mitochondrialPRO_0000008879Add
BLAST

Post-translational modificationi

The leader peptide may be processed in two proteolytic steps, first between Ser-23 and Phe-24, second and by a different protease, to yield the mature protein.

Proteomic databases

MaxQBiP16622.
PeptideAtlasiP16622.

PTM databases

iPTMnetiP16622.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CAMK2BQ13554-33EBI-8261,EBI-11523526From a different organism.

Protein-protein interaction databases

BioGridi34570. 22 interactions.
DIPiDIP-4133N.
IntActiP16622. 1 interaction.
MINTiMINT-501604.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 457Combined sources
Helixi52 – 543Combined sources
Helixi55 – 628Combined sources
Beta strandi67 – 693Combined sources
Beta strandi73 – 753Combined sources
Helixi76 – 9722Combined sources
Helixi104 – 12219Combined sources
Helixi124 – 1263Combined sources
Beta strandi129 – 14012Combined sources
Helixi142 – 1509Combined sources
Turni151 – 1533Combined sources
Beta strandi156 – 1627Combined sources
Turni168 – 1703Combined sources
Helixi171 – 18515Combined sources
Beta strandi191 – 1966Combined sources
Helixi203 – 21816Combined sources
Helixi225 – 2273Combined sources
Beta strandi229 – 2357Combined sources
Helixi239 – 2424Combined sources
Turni243 – 2453Combined sources
Helixi248 – 26215Combined sources
Turni263 – 2653Combined sources
Beta strandi269 – 2746Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi284 – 2863Combined sources
Helixi287 – 2948Combined sources
Helixi295 – 2973Combined sources
Beta strandi301 – 3044Combined sources
Helixi313 – 3164Combined sources
Helixi317 – 3248Combined sources
Helixi330 – 3323Combined sources
Beta strandi333 – 3353Combined sources
Helixi343 – 35917Combined sources
Helixi367 – 3737Combined sources
Helixi383 – 3864Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L8XX-ray2.70A/B32-393[»]
1LBQX-ray2.40A/B32-393[»]
ProteinModelPortaliP16622.
SMRiP16622. Positions 36-391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16622.

Family & Domainsi

Sequence similaritiesi

Belongs to the ferrochelatase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000016258.
HOGENOMiHOG000060727.
InParanoidiP16622.
KOiK01772.
OMAiLPIQNKL.
OrthoDBiEOG7V1G10.

Family and domain databases

HAMAPiMF_00323. Ferrochelatase.
InterProiIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view]
PANTHERiPTHR11108. PTHR11108. 1 hit.
PfamiPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00109. hemH. 1 hit.
PROSITEiPS00534. FERROCHELATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16622-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRTIRTQG SFLRRSQLTI TRSFSVTFNM QNAQKRSPTG IVLMNMGGPS
60 70 80 90 100
KVEETYDFLY QLFADNDLIP ISAKYQKTIA KYIAKFRTPK IEKQYREIGG
110 120 130 140 150
GSPIRKWSEY QATEVCKILD KTCPETAPHK PYVAFRYAKP LTAETYKQML
160 170 180 190 200
KDGVKKAVAF SQYPHFSYST TGSSINELWR QIKALDSERS ISWSVIDRWP
210 220 230 240 250
TNEGLIKAFS ENITKKLQEF PQPVRDKVVL LFSAHSLPMD VVNTGDAYPA
260 270 280 290 300
EVAATVYNIM QKLKFKNPYR LVWQSQVGPK PWLGAQTAEI AEFLGPKVDG
310 320 330 340 350
LMFIPIAFTS DHIETLHEID LGVIGESEYK DKFKRCESLN GNQTFIEGMA
360 370 380 390
DLVKSHLQSN QLYSNQLPLD FALGKSNDPV KDLSLVFGNH EST
Length:393
Mass (Da):44,596
Last modified:August 1, 1990 - v1
Checksum:iF04E7C7AAD36C24F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341Q → E AA sequence (PubMed:3042776).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05395 Genomic DNA. Translation: AAA34667.1.
X54514 Genomic DNA. Translation: CAA38371.1.
Z75084 Genomic DNA. Translation: CAA99385.1.
BK006948 Genomic DNA. Translation: DAA10948.1.
PIRiA35190. IBBYFC.
RefSeqiNP_014819.3. NM_001183595.3.

Genome annotation databases

EnsemblFungiiYOR176W; YOR176W; YOR176W.
GeneIDi854347.
KEGGisce:YOR176W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05395 Genomic DNA. Translation: AAA34667.1.
X54514 Genomic DNA. Translation: CAA38371.1.
Z75084 Genomic DNA. Translation: CAA99385.1.
BK006948 Genomic DNA. Translation: DAA10948.1.
PIRiA35190. IBBYFC.
RefSeqiNP_014819.3. NM_001183595.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L8XX-ray2.70A/B32-393[»]
1LBQX-ray2.40A/B32-393[»]
ProteinModelPortaliP16622.
SMRiP16622. Positions 36-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34570. 22 interactions.
DIPiDIP-4133N.
IntActiP16622. 1 interaction.
MINTiMINT-501604.

PTM databases

iPTMnetiP16622.

Proteomic databases

MaxQBiP16622.
PeptideAtlasiP16622.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR176W; YOR176W; YOR176W.
GeneIDi854347.
KEGGisce:YOR176W.

Organism-specific databases

EuPathDBiFungiDB:YOR176W.
SGDiS000005702. HEM15.

Phylogenomic databases

GeneTreeiENSGT00390000016258.
HOGENOMiHOG000060727.
InParanoidiP16622.
KOiK01772.
OMAiLPIQNKL.
OrthoDBiEOG7V1G10.

Enzyme and pathway databases

UniPathwayiUPA00252; UER00325.
BioCyciYEAST:YOR176W-MONOMER.
BRENDAi4.99.1.1. 984.
ReactomeiR-SCE-189451. Heme biosynthesis.
SABIO-RKP16622.

Miscellaneous databases

EvolutionaryTraceiP16622.
PROiP16622.

Family and domain databases

HAMAPiMF_00323. Ferrochelatase.
InterProiIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view]
PANTHERiPTHR11108. PTHR11108. 1 hit.
PfamiPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00109. hemH. 1 hit.
PROSITEiPS00534. FERROCHELATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ferrochelatase from Saccharomyces cerevisiae. Sequence, disruption, and expression of its structural gene HEM15."
    Labbe-Bois R.
    J. Biol. Chem. 265:7278-7283(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of the ferrochelatase and tRNA(val) gene region from Saccharomyces cerevisiae."
    Gokhman I., Zamir A.
    Nucleic Acids Res. 18:6130-6130(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Purification and properties of ferrochelatase from the yeast Saccharomyces cerevisiae. Evidence for a precursor form of the protein."
    Camadro J.-M., Labbe P.
    J. Biol. Chem. 263:11675-11682(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-51.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHEMH_YEAST
AccessioniPrimary (citable) accession number: P16622
Secondary accession number(s): D6W2N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 8, 2016
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Ferrochelatase interacts with protoprophyrinogen oxidase, and associates with complex 1 of the respiratory chain.
Acidic phospholipids or fatty acids are important for the ferrochelatase activity.
Present with 22700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.