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P42043

- HEMH1_ARATH

UniProt

P42043 - HEMH1_ARATH

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Protein
Ferrochelatase-1, chloroplastic/mitochondrial
Gene
HEM15, At5g26030, T1N24.17
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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+.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. ferrochelatase activity Source: TAIR
Complete GO annotation...

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.
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: Chromosome 5

Organism-specific databases

TAIRiAT5G26030.

Subcellular locationi

Plastidchloroplast membrane; Peripheral membrane protein. Plastidchloroplast thylakoid membrane; Peripheral membrane protein. Mitochondrion 2 Publications

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 mitochondrion Reviewed prediction
Add
BLAST
Chaini36 – 466431Ferrochelatase-1, chloroplastic/mitochondrialUniRule annotation
PRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the ferrochelatase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0276.
HOGENOMiHOG000060727.
InParanoidiP42043.
KOiK01772.
OMAiESGVENW.
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

MQATALSSGF NPLTKRKDHR FPRSCSQRNS LSLIQCDIKE RSFGESMTIT    50
NRGLSFKTNV FEQARSVTGD CSYDETSAKA RSHVVAEDKI GVLLLNLGGP 100
ETLNDVQPFL YNLFADPDII RLPRPFQFLQ GTIAKFISVV RAPKSKEGYA 150
AIGGGSPLRK ITDEQADAIK MSLQAKNIAA NVYVGMRYWY PFTEEAVQQI 200
KKDKITRLVV LPLYPQYSIS TTGSSIRVLQ DLFRKDPYLA GVPVAIIKSW 250
YQRRGYVNSM ADLIEKELQT FSDPKEVMIF FSAHGVPVSY VENAGDPYQK 300
QMEECIDLIM EELKARGVLN DHKLAYQSRV GPVQWLKPYT DEVLVDLGKS 350
GVKSLLAVPV SFVSEHIETL EEIDMEYREL ALESGVENWG RVPALGLTPS 400
FITDLADAVI ESLPSAEAMS NPNAVVDSED SESSDAFSYI VKMFFGSILA 450
FVLLLSPKMF HAFRNL 466
Length:466
Mass (Da):52,033
Last modified:November 1, 1995 - v1
Checksum:iBAB2F960A5AEBB6A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A54125.
RefSeqi NP_001031941.1. NM_001036864.1.
NP_197975.3. NM_122504.4.
UniGenei At.58.
At.70191.

3D structure databases

ProteinModelPortali P42043.
SMRi P42043. Positions 89-420.
ModBasei Search...

Proteomic databases

PaxDbi P42043.
PRIDEi P42043.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G26030.1 ; AT5G26030.1 ; AT5G26030 .
AT5G26030.2 ; AT5G26030.2 ; AT5G26030 .
GeneIDi 832672.
KEGGi ath:AT5G26030.

Organism-specific databases

TAIRi AT5G26030.

Phylogenomic databases

eggNOGi COG0276.
HOGENOMi HOG000060727.
InParanoidi P42043.
KOi K01772.
OMAi ESGVENW.
PhylomeDBi P42043.

Enzyme and pathway databases

UniPathwayi UPA00668 .
BioCyci ARA:AT5G26030-MONOMER.
ARA:GQT-1215-MONOMER.

Miscellaneous databases

PROi P42043.

Gene expression databases

Genevestigatori P42043.

Family and domain databases

HAMAPi MF_00323. Ferrochelatase.
InterProi IPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view ]
PANTHERi PTHR11108. PTHR11108. 1 hit.
Pfami PF00762. Ferrochelatase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00109. hemH. 1 hit.
PROSITEi PS00534. FERROCHELATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1994) [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(1998) [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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-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(1997) [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(1997) [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(2007) [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: June 11, 2014
This is version 115 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

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