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P22600 (HEMH_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ferrochelatase, mitochondrial

EC=4.99.1.1
Alternative name(s):
Heme synthase
Protoheme ferro-lyase
Gene names
Name:FECH
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the ferrous insertion into protoporphyrin IX.

Catalytic activity

Protoheme + 2 H+ = protoporphyrin + Fe2+.

Cofactor

Binds 1 2Fe-2S cluster.

Enzyme regulation

Inhibited by nitric oxide (NO). The 2Fe-2S cluster could act as a NO sensor 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.

Sequence similarities

Belongs to the ferrochelatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4747Mitochondrion Potential
Chain48 – 416369Ferrochelatase, mitochondrial
PRO_0000008872

Sites

Active site2231 By similarity
Active site3761 By similarity
Metal binding1891Iron-sulfur (2Fe-2S)
Metal binding3961Iron-sulfur (2Fe-2S) By similarity
Metal binding3991Iron-sulfur (2Fe-2S) By similarity
Metal binding4041Iron-sulfur (2Fe-2S) By similarity

Experimental info

Sequence conflict2821D → E AA sequence Ref.2
Sequence conflict2871S → P AA sequence Ref.2
Sequence conflict2871S → P AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P22600 [UniParc].

Last modified February 1, 1996. Version 3.
Checksum: ECE1D43F9DC4B78E

FASTA41646,935
        10         20         30         40         50         60 
MAAALRSAGV LLRDRLLYGG SRACQPRRCQ SGAATAAAAT ETAQRARSPK PQAQPGNRKP 

        70         80         90        100        110        120 
RTGILMLNMG GPETVEEVQD FLQRLFLDQD LMTLPVQDKL GPFIAKRRTP KIQEQYRRIG 

       130        140        150        160        170        180 
GGSPIKMWTS KQGEGMVKLL DELSPHTAPH KYYIGFRYVH PLTEEAIEEM ERDGLERAVA 

       190        200        210        220        230        240 
FTQYPQYSCS TTGSSLNAIY RYYNEVGRKP TMKWSTIDRW PTHPLLIQCF ADHILKELDH 

       250        260        270        280        290        300 
FPPEKRREVV ILFSAHSLPM SVVNRGDPYP QEVGATVQRV MDKLGYSNPY RLVWQSKVGP 

       310        320        330        340        350        360 
MPWLGPQTDE AIKGLCKRGR KNILLVPIAF TSDHIETLYE LDIEYSQVLA SECGLENIRR 

       370        380        390        400        410 
AESLNGNPLF SKALADLVHS HLQSKERCST QLTLSCPLCV NPTCRETKSF FTSQQL 

« Hide

References

[1]"The coding sequence of the bovine ferrochelatase gene."
Shibuya H., Nonneman D., Tamassia M., Allphin O.L., Johnson G.S.
Biochim. Biophys. Acta 1231:117-120(1995) [PubMed: 7640290] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of murine ferrochelatase."
Brenner D.A., Frasier F.
Proc. Natl. Acad. Sci. U.S.A. 88:849-853(1991) [PubMed: 1704134] [Abstract]
Cited for: PROTEIN SEQUENCE OF 281-311.
Tissue: Liver.
[3]"Molecular cloning, sequencing, and expression of mouse ferrochelatase."
Taketani S., Nakahashi Y., Osumi T., Tokunaga R.
J. Biol. Chem. 265:19377-19380(1990) [PubMed: 2246229] [Abstract]
Cited for: PROTEIN SEQUENCE OF 152-157; 266-275; 284-291 AND 373-381.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L34173 mRNA. Translation: AAA79169.1.
IPIIPI00701579.
PIRI45890.
RefSeqNP_776479.1. NM_174054.2.
UniGeneBt.88608.

3D structure databases

ProteinModelPortalP22600.
SMRP22600. Positions 58-416.
ModBaseSearch...

Protein-protein interaction databases

STRINGP22600.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000008384; ENSBTAP00000008384; ENSBTAG00000006393.
GeneID281158.
KEGGbta:281158.

Organism-specific databases

CTD2235.

Phylogenomic databases

eggNOGmaNOG04866.
GeneTreeENSGT00390000016258.
HOVERGENHBG051898.
InParanoidP22600.
OMALQKPLAW.
OrthoDBEOG4GXFN0.
PhylomeDBP22600.

Family and domain databases

InterProIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view]
KOK01772.
PANTHERPTHR11108. Ferrochelatase. 1 hit.
PfamPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00109. HemH. 1 hit.
PROSITEPS00534. FERROCHELATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEMH_BOVIN
AccessionPrimary (citable) accession number: P22600
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1996
Last modified: November 16, 2011
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families