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Protein

Ferrochelatase-1, chloroplastic/mitochondrial

Gene

HEM15

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the ferrous insertion into protoporphyrin IX. May have a role in dealing with oxidative stress. May be involved in wound-induced supply of heme to defensive hemoproteins outside plastids.1 Publication

Catalytic activityi

Protoheme + 2 H+ = protoporphyrin + Fe2+.

Pathwayi

GO - Molecular functioni

  1. ferrochelatase activity Source: TAIR

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-UniPathway
  2. heme biosynthetic process Source: TAIR
  3. response to oxidative stress Source: TAIR
  4. tetrapyrrole biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Iron

Enzyme and pathway databases

BioCyciARA:AT5G26030-MONOMER.
ARA:GQT-1215-MONOMER.
BRENDAi4.99.1.1. 399.
ReactomeiREACT_340934. Heme biosynthesis.
UniPathwayiUPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferrochelatase-1, chloroplastic/mitochondrial (EC:4.99.1.1)
Short name:
AtFC1
Alternative name(s):
Ferrochelatase I
Heme synthase 1
Protoheme ferro-lyase 1
Gene namesi
Name:HEM15
Ordered Locus Names:At5g26030
ORF Names:T1N24.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G26030.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast membrane Source: UniProtKB-SubCell
  3. chloroplast thylakoid membrane Source: UniProtKB-SubCell
  4. mitochondrion Source: TAIR
  5. plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Mitochondrion, Plastid, Thylakoid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype, but decreased heme content in roots.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535Chloroplast and mitochondrionSequence AnalysisAdd
BLAST
Chaini36 – 466431Ferrochelatase-1, chloroplastic/mitochondrialPRO_0000008880Add
BLAST

Proteomic databases

PaxDbiP42043.
PRIDEiP42043.

Expressioni

Tissue specificityi

Present in both leaves and roots.1 Publication

Inductioni

Up-regulated by wounding and reactive oxygen species. Not regulated by methyl jasmonate.1 Publication

Gene expression databases

GenevestigatoriP42043.

Structurei

3D structure databases

ProteinModelPortaliP42043.
SMRiP42043. Positions 89-420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ferrochelatase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0276.
HOGENOMiHOG000060727.
InParanoidiP42043.
KOiK01772.
OMAiVHRSPVL.
PhylomeDBiP42043.

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.

P42043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQATALSSGF NPLTKRKDHR FPRSCSQRNS LSLIQCDIKE RSFGESMTIT
60 70 80 90 100
NRGLSFKTNV FEQARSVTGD CSYDETSAKA RSHVVAEDKI GVLLLNLGGP
110 120 130 140 150
ETLNDVQPFL YNLFADPDII RLPRPFQFLQ GTIAKFISVV RAPKSKEGYA
160 170 180 190 200
AIGGGSPLRK ITDEQADAIK MSLQAKNIAA NVYVGMRYWY PFTEEAVQQI
210 220 230 240 250
KKDKITRLVV LPLYPQYSIS TTGSSIRVLQ DLFRKDPYLA GVPVAIIKSW
260 270 280 290 300
YQRRGYVNSM ADLIEKELQT FSDPKEVMIF FSAHGVPVSY VENAGDPYQK
310 320 330 340 350
QMEECIDLIM EELKARGVLN DHKLAYQSRV GPVQWLKPYT DEVLVDLGKS
360 370 380 390 400
GVKSLLAVPV SFVSEHIETL EEIDMEYREL ALESGVENWG RVPALGLTPS
410 420 430 440 450
FITDLADAVI ESLPSAEAMS NPNAVVDSED SESSDAFSYI VKMFFGSILA
460
FVLLLSPKMF HAFRNL
Length:466
Mass (Da):52,033
Last modified:November 1, 1995 - v1
Checksum:iBAB2F960A5AEBB6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73417 mRNA. Translation: CAA51819.1.
Y13382 Genomic DNA. Translation: CAA73809.1.
AF149413 Genomic DNA. Translation: AAD40138.1.
CP002688 Genomic DNA. Translation: AED93514.1.
CP002688 Genomic DNA. Translation: AED93515.1.
PIRiA54125.
RefSeqiNP_001031941.1. NM_001036864.1.
NP_197975.3. NM_122504.4.
UniGeneiAt.58.
At.70191.

Genome annotation databases

EnsemblPlantsiAT5G26030.1; AT5G26030.1; AT5G26030.
AT5G26030.2; AT5G26030.2; AT5G26030.
GeneIDi832672.
KEGGiath:AT5G26030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73417 mRNA. Translation: CAA51819.1.
Y13382 Genomic DNA. Translation: CAA73809.1.
AF149413 Genomic DNA. Translation: AAD40138.1.
CP002688 Genomic DNA. Translation: AED93514.1.
CP002688 Genomic DNA. Translation: AED93515.1.
PIRiA54125.
RefSeqiNP_001031941.1. NM_001036864.1.
NP_197975.3. NM_122504.4.
UniGeneiAt.58.
At.70191.

3D structure databases

ProteinModelPortaliP42043.
SMRiP42043. Positions 89-420.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiP42043.
PRIDEiP42043.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G26030.1; AT5G26030.1; AT5G26030.
AT5G26030.2; AT5G26030.2; AT5G26030.
GeneIDi832672.
KEGGiath:AT5G26030.

Organism-specific databases

TAIRiAT5G26030.

Phylogenomic databases

eggNOGiCOG0276.
HOGENOMiHOG000060727.
InParanoidiP42043.
KOiK01772.
OMAiVHRSPVL.
PhylomeDBiP42043.

Enzyme and pathway databases

UniPathwayiUPA00668.
BioCyciARA:AT5G26030-MONOMER.
ARA:GQT-1215-MONOMER.
BRENDAi4.99.1.1. 399.
ReactomeiREACT_340934. Heme biosynthesis.

Miscellaneous databases

PROiP42043.

Gene expression databases

GenevestigatoriP42043.

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 of a cDNA encoding chloroplast ferrochelatase from Arabidopsis thaliana by functional complementation of a yeast mutant."
    Smith A.G., Santana M.A., Wallace-Cook A.D.M., Roper J.M., Labbe-Bois R.
    J. Biol. Chem. 269:13405-13413(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Landsberg erecta.
    Tissue: Seedling.
  2. "Two different genes encode ferrochelatase in Arabidopsis: mapping, expression and subcellular targeting of the precursor proteins."
    Chow K.-S., Singh D.P., Walker A., Smith A.G.
    Plant J. 15:531-541(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  3. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Molecular localisation of ferrochelatase in higher plant chloroplasts."
    Roper J.M., Smith A.G.
    Eur. J. Biochem. 246:32-37(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "A single precursor protein for ferrochelatase-I from Arabidopsis is imported in vitro into both chloroplasts and mitochondria."
    Chow K.-S., Singh D.P., Roper J.M., Smith A.G.
    J. Biol. Chem. 272:27565-27571(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Induction of isoforms of tetrapyrrole biosynthetic enzymes, AtHEMA2 and AtFC1, under stress conditions and their physiological functions in Arabidopsis."
    Nagai S., Koide M., Takahashi S., Kikuta A., Aono M., Sasaki-Sekimoto Y., Ohta H., Takamiya K., Masuda T.
    Plant Physiol. 144:1039-1051(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY WOUNDING AND REACTIVE OXYGEN SPECIES, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiHEMH1_ARATH
AccessioniPrimary (citable) accession number: P42043
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.