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Protein

Ferrochelatase

Gene

hemH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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 (hemH)
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
Metal bindingi194 – 1941IronBy similarity
Metal bindingi275 – 2751IronBy similarity

GO - Molecular functioni

  • ferrochelatase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • heme biosynthetic process Source: EcoliWiki
  • protoporphyrinogen IX metabolic process Source: EcoliWiki
  • response to light stimulus Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:PROTOHEME-FERROCHELAT-MONOMER.
ECOL316407:JW0464-MONOMER.
MetaCyc:PROTOHEME-FERROCHELAT-MONOMER.
UniPathwayiUPA00252; UER00325.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferrochelatase (EC:4.99.1.1)
Alternative name(s):
Heme synthase
Protoheme ferro-lyase
Gene namesi
Name:hemH
Synonyms:popA, visA
Ordered Locus Names:b0475, JW0464
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10431. hemH.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells are sensitive to visible light (which is lethal).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320FerrochelatasePRO_0000175138Add
BLAST

Proteomic databases

PaxDbiP23871.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP23871. 9 interactions.
STRINGi511145.b0475.

Structurei

3D structure databases

ProteinModelPortaliP23871.
SMRiP23871. Positions 6-319.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ferrochelatase family.Curated

Phylogenomic databases

eggNOGiENOG4105CFX. Bacteria.
COG0276. LUCA.
HOGENOMiHOG000060730.
InParanoidiP23871.
KOiK01772.
OMAiWEEGSPL.
OrthoDBiEOG6XHC5H.
PhylomeDBiP23871.

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.

P23871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQTKTGILL ANLGTPDAPT PEAVKRYLKQ FLSDRRVVDT SRLLWWPLLR
60 70 80 90 100
GVILPLRSPR VAKLYASVWM EGGSPLMVYS RQQQQALAQR LPEMPVALGM
110 120 130 140 150
SYGSPSLESA VDELLAEHVD HIVVLPLYPQ FSCSTVGAVW DELARILARK
160 170 180 190 200
RSIPGISFIR DYADNHDYIN ALANSVRASF AKHGEPDLLL LSYHGIPQRY
210 220 230 240 250
ADEGDDYPQR CRTTTRELAS ALGMAPEKVM MTFQSRFGRE PWLMPYTDET
260 270 280 290 300
LKMLGEKGVG HIQVMCPGFA ADCLETLEEI AEQNREVFLG AGGKKYEYIP
310 320
ALNATPEHIE MMANLVAAYR
Length:320
Mass (Da):35,884
Last modified:November 1, 1997 - v3
Checksum:i65BB56EBFDD95D5C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541L → F in BAA14304 (PubMed:2051480).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90259 Genomic DNA. Translation: BAA14304.1.
U82664 Genomic DNA. Translation: AAB40229.1.
U00096 Genomic DNA. Translation: AAC73577.1.
AP009048 Genomic DNA. Translation: BAE76254.1.
PIRiB64778.
RefSeqiNP_415008.1. NC_000913.3.
WP_001250103.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73577; AAC73577; b0475.
BAE76254; BAE76254; BAE76254.
GeneIDi947532.
KEGGiecj:JW0464.
eco:b0475.
PATRICi32116107. VBIEscCol129921_0495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90259 Genomic DNA. Translation: BAA14304.1.
U82664 Genomic DNA. Translation: AAB40229.1.
U00096 Genomic DNA. Translation: AAC73577.1.
AP009048 Genomic DNA. Translation: BAE76254.1.
PIRiB64778.
RefSeqiNP_415008.1. NC_000913.3.
WP_001250103.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP23871.
SMRiP23871. Positions 6-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP23871. 9 interactions.
STRINGi511145.b0475.

Proteomic databases

PaxDbiP23871.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73577; AAC73577; b0475.
BAE76254; BAE76254; BAE76254.
GeneIDi947532.
KEGGiecj:JW0464.
eco:b0475.
PATRICi32116107. VBIEscCol129921_0495.

Organism-specific databases

EchoBASEiEB0426.
EcoGeneiEG10431. hemH.

Phylogenomic databases

eggNOGiENOG4105CFX. Bacteria.
COG0276. LUCA.
HOGENOMiHOG000060730.
InParanoidiP23871.
KOiK01772.
OMAiWEEGSPL.
OrthoDBiEOG6XHC5H.
PhylomeDBiP23871.

Enzyme and pathway databases

UniPathwayiUPA00252; UER00325.
BioCyciEcoCyc:PROTOHEME-FERROCHELAT-MONOMER.
ECOL316407:JW0464-MONOMER.
MetaCyc:PROTOHEME-FERROCHELAT-MONOMER.

Miscellaneous databases

PROiP23871.

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. "Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12."
    Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.
    J. Mol. Biol. 219:393-398(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
    Strain: K12.
  2. "Overproduction, purification, and characterization of ferrochelatase from Escherichia coli."
    Miyamoto K., Kanaya S., Morikawa K., Inokuchi H.
    J. Biochem. 115:545-551(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
  3. Miyamoto K.
    Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 54.
  4. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "The Escherichia coli visA gene encodes ferrochelatase, the final enzyme of the heme biosynthetic pathway."
    Frustaci J.M., O'Brian M.R.
    J. Bacteriol. 175:2154-2156(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiHEMH_ECOLI
AccessioniPrimary (citable) accession number: P23871
Secondary accession number(s): P78232, Q2MBV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: November 11, 2015
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.