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Protein

Ferrochelatase, mitochondrial

Gene

HEM15

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

Functioni

Catalyzes the ferrous insertion into protoporphyrin IX.

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

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

Keywordsi

Molecular functionLyase
Biological processHeme biosynthesis, Porphyrin biosynthesis
LigandIron

Enzyme and pathway databases

BioCyciYEAST:YOR176W-MONOMER
BRENDAi4.99.1.1 984
ReactomeiR-SCE-189451 Heme biosynthesis
SABIO-RKiP16622
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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP16622
PRIDEiP16622

PTM databases

iPTMnetiP16622

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi34570, 26 interactors
DIPiDIP-4133N
IntActiP16622, 8 interactors
STRINGi4932.YOR176W

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
OMAiLGDPYHC
OrthoDBiEOG092C2CWC

Family and domain databases

CDDicd00419 Ferrochelatase_C, 1 hit
cd03411 Ferrochelatase_N, 1 hit
HAMAPiMF_00323 Ferrochelatase, 1 hit
InterProiView protein in InterPro
IPR001015 Ferrochelatase
IPR019772 Ferrochelatase_AS
IPR033644 Ferrochelatase_C
IPR033659 Ferrochelatase_N
PANTHERiPTHR11108 PTHR11108, 1 hit
PfamiView protein in Pfam
PF00762 Ferrochelatase, 1 hit
TIGRFAMsiTIGR00109 hemH, 1 hit
PROSITEiView protein in PROSITE
PS00534 FERROCHELATASE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiHEMH_YEAST
AccessioniPrimary (citable) accession number: P16622
Secondary accession number(s): D6W2N2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: March 28, 2018
This is version 171 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health