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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)DescriptionActionsGraphical viewLength
Active sitei351By similarity1

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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 31Mitochondrion1 PublicationAdd BLAST31
ChainiPRO_000000887932 – 393Ferrochelatase, mitochondrialAdd BLAST362

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.
PRIDEiP16622.

PTM databases

iPTMnetiP16622.

Interactioni

Protein-protein interaction databases

BioGridi34570. 22 interactors.
DIPiDIP-4133N.
IntActiP16622. 1 interactor.
MINTiMINT-501604.

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 45Combined sources7
Helixi52 – 54Combined sources3
Helixi55 – 62Combined sources8
Beta strandi67 – 69Combined sources3
Beta strandi73 – 75Combined sources3
Helixi76 – 97Combined sources22
Helixi104 – 122Combined sources19
Helixi124 – 126Combined sources3
Beta strandi129 – 140Combined sources12
Helixi142 – 150Combined sources9
Turni151 – 153Combined sources3
Beta strandi156 – 162Combined sources7
Turni168 – 170Combined sources3
Helixi171 – 185Combined sources15
Beta strandi191 – 196Combined sources6
Helixi203 – 218Combined sources16
Helixi225 – 227Combined sources3
Beta strandi229 – 235Combined sources7
Helixi239 – 242Combined sources4
Turni243 – 245Combined sources3
Helixi248 – 262Combined sources15
Turni263 – 265Combined sources3
Beta strandi269 – 274Combined sources6
Beta strandi278 – 280Combined sources3
Beta strandi284 – 286Combined sources3
Helixi287 – 294Combined sources8
Helixi295 – 297Combined sources3
Beta strandi301 – 304Combined sources4
Helixi313 – 316Combined sources4
Helixi317 – 324Combined sources8
Helixi330 – 332Combined sources3
Beta strandi333 – 335Combined sources3
Helixi343 – 359Combined sources17
Helixi367 – 373Combined sources7
Helixi383 – 386Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L8XX-ray2.70A/B32-393[»]
1LBQX-ray2.40A/B32-393[»]
ProteinModelPortaliP16622.
SMRiP16622.
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.
OMAiCYQSKVG.
OrthoDBiEOG092C2CWC.

Family and domain databases

CDDicd00419. Ferrochelatase_C. 1 hit.
cd03411. Ferrochelatase_N. 1 hit.
HAMAPiMF_00323. Ferrochelatase. 1 hit.
InterProiIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
IPR033644. Ferrochelatase_C.
IPR033659. Ferrochelatase_N.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti34Q → E AA sequence (PubMed:3042776).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L8XX-ray2.70A/B32-393[»]
1LBQX-ray2.40A/B32-393[»]
ProteinModelPortaliP16622.
SMRiP16622.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34570. 22 interactors.
DIPiDIP-4133N.
IntActiP16622. 1 interactor.
MINTiMINT-501604.

PTM databases

iPTMnetiP16622.

Proteomic databases

MaxQBiP16622.
PRIDEiP16622.

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.
OMAiCYQSKVG.
OrthoDBiEOG092C2CWC.

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

CDDicd00419. Ferrochelatase_C. 1 hit.
cd03411. Ferrochelatase_N. 1 hit.
HAMAPiMF_00323. Ferrochelatase. 1 hit.
InterProiIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
IPR033644. Ferrochelatase_C.
IPR033659. Ferrochelatase_N.
[Graphical view]
PANTHERiPTHR11108. PTHR11108. 1 hit.
PfamiPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00109. hemH. 1 hit.
PROSITEiPS00534. FERROCHELATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 161 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.