HEMH1_ARATH
ID HEMH1_ARATH Reviewed; 466 AA.
AC P42043; C0Z2M8; Q0WW90;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ferrochelatase-1, chloroplastic/mitochondrial {ECO:0000305};
DE Short=AtFC1 {ECO:0000303|PubMed:17416636};
DE EC=4.99.1.1 {ECO:0000305};
DE AltName: Full=Ferrochelatase-I {ECO:0000303|PubMed:9753778};
DE Short=AtFC-I {ECO:0000303|PubMed:12374307};
DE AltName: Full=Heme synthase 1 {ECO:0000305};
DE AltName: Full=Protoheme ferro-lyase 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=FC1 {ECO:0000303|PubMed:24329537};
GN Synonyms=FC-I {ECO:0000303|PubMed:9753778},
GN HEM15 {ECO:0000303|PubMed:8175771}; OrderedLocusNames=At5g26030;
GN ORFNames=T1N24.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Seedling;
RX PubMed=8175771; DOI=10.1016/s0021-9258(17)36847-3;
RA Smith A.G., Santana M.A., Wallace-Cook A.D.M., Roper J.M., Labbe-Bois R.;
RT "Isolation of a cDNA encoding chloroplast ferrochelatase from Arabidopsis
RT thaliana by functional complementation of a yeast mutant.";
RL J. Biol. Chem. 269:13405-13413(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9753778; DOI=10.1046/j.1365-313x.1998.00235.x;
RA Chow K.-S., Singh D.P., Walker A., Smith A.G.;
RT "Two different genes encode ferrochelatase in Arabidopsis: mapping,
RT expression and subcellular targeting of the precursor proteins.";
RL Plant J. 15:531-541(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9210462; DOI=10.1111/j.1432-1033.1997.t01-1-00032.x;
RA Roper J.M., Smith A.G.;
RT "Molecular localisation of ferrochelatase in higher plant chloroplasts.";
RL Eur. J. Biochem. 246:32-37(1997).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=9346891; DOI=10.1074/jbc.272.44.27565;
RA Chow K.-S., Singh D.P., Roper J.M., Smith A.G.;
RT "A single precursor protein for ferrochelatase-I from Arabidopsis is
RT imported in vitro into both chloroplasts and mitochondria.";
RL J. Biol. Chem. 272:27565-27571(1997).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11602264; DOI=10.1016/s0014-5793(01)02925-8;
RA Lister R., Chew O., Rudhe C., Lee M.N., Whelan J.;
RT "Arabidopsis thaliana ferrochelatase-I and -II are not imported into
RT Arabidopsis mitochondria.";
RL FEBS Lett. 506:291-295(2001).
RN [10]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12374307; DOI=10.1023/a:1019959224271;
RA Singh D.P., Cornah J.E., Hadingham S., Smith A.G.;
RT "Expression analysis of the two ferrochelatase genes in Arabidopsis in
RT different tissues and under stress conditions reveals their different roles
RT in haem biosynthesis.";
RL Plant Mol. Biol. 50:773-788(2002).
RN [11]
RP FUNCTION, INDUCTION BY WOUNDING AND REACTIVE OXYGEN SPECIES, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17416636; DOI=10.1104/pp.107.100065;
RA Nagai S., Koide M., Takahashi S., Kikuta A., Aono M., Sasaki-Sekimoto Y.,
RA Ohta H., Takamiya K., Masuda T.;
RT "Induction of isoforms of tetrapyrrole biosynthetic enzymes, AtHEMA2 and
RT AtFC1, under stress conditions and their physiological functions in
RT Arabidopsis.";
RL Plant Physiol. 144:1039-1051(2007).
RN [12]
RP FUNCTION.
RX PubMed=21565502; DOI=10.1016/j.cub.2011.04.004;
RA Woodson J.D., Perez-Ruiz J.M., Chory J.;
RT "Heme synthesis by plastid ferrochelatase I regulates nuclear gene
RT expression in plants.";
RL Curr. Biol. 21:897-903(2011).
RN [13]
RP FUNCTION.
RX PubMed=24329537; DOI=10.1111/pce.12248;
RA Scharfenberg M., Mittermayr L., von Roepenack-Lahaye E., Schlicke H.,
RA Grimm B., Leister D., Kleine T.;
RT "Functional characterization of the two ferrochelatases in Arabidopsis
RT thaliana.";
RL Plant Cell Environ. 38:280-298(2015).
CC -!- FUNCTION: Catalyzes the last step of heme biosynthesis by inserting
CC ferrous iron into protoporphyrin IX to produce protoheme
CC (PubMed:17416636, PubMed:24329537). Produces heme for photosynthetic
CC cytochromes, but does not seem to be involved in stress responses
CC (PubMed:24329537). May be involved in wound-induced supply of heme to
CC defensive hemoproteins outside plastids (PubMed:17416636). Regulates
CC the expression of photosynthesis-associated nuclear genes in
CC undevelopped chloroplasts through production of heme (PubMed:21565502).
CC {ECO:0000269|PubMed:17416636, ECO:0000269|PubMed:21565502,
CC ECO:0000269|PubMed:24329537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX;
CC Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:9210462}; Peripheral membrane protein
CC {ECO:0000305|PubMed:9210462}. Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:9210462}; Peripheral membrane protein
CC {ECO:0000305|PubMed:9210462}. Mitochondrion
CC {ECO:0000269|PubMed:9346891}. Note=(PubMed:9346891) describes
CC experimental in vitro import of FC1 into mitochondria isolated from
CC pea. However, (PubMed:11602264) shows experimental evidences that FC1
CC is not present in Arabidopsis mitochondria in vivo.
CC {ECO:0000305|PubMed:11602264, ECO:0000305|PubMed:9346891}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers
CC (PubMed:12374307). Present in both leaves and roots (PubMed:17416636).
CC {ECO:0000269|PubMed:12374307, ECO:0000269|PubMed:17416636}.
CC -!- INDUCTION: Induced by sucrose, wounding, oxidative stress, salicylic
CC acid, and during hypersensitive response to TMV infection
CC (PubMed:12374307). Up-regulated by wounding and reactive oxygen
CC species. Not regulated by methyl jasmonate.
CC {ECO:0000269|PubMed:12374307, ECO:0000269|PubMed:17416636}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but decreased heme content
CC in roots. {ECO:0000269|PubMed:17416636}.
CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X73417; CAA51819.1; -; mRNA.
DR EMBL; Y13382; CAA73809.1; -; Genomic_DNA.
DR EMBL; AF149413; AAD40138.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93514.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93515.1; -; Genomic_DNA.
DR EMBL; AK318842; BAH56957.1; -; mRNA.
DR EMBL; AK226466; BAE98608.1; -; mRNA.
DR PIR; A54125; A54125.
DR RefSeq; NP_001031941.1; NM_001036864.1.
DR RefSeq; NP_197975.3; NM_122504.5.
DR AlphaFoldDB; P42043; -.
DR SMR; P42043; -.
DR STRING; 3702.AT5G26030.1; -.
DR PaxDb; P42043; -.
DR PRIDE; P42043; -.
DR ProteomicsDB; 230387; -.
DR EnsemblPlants; AT5G26030.1; AT5G26030.1; AT5G26030.
DR EnsemblPlants; AT5G26030.2; AT5G26030.2; AT5G26030.
DR GeneID; 832672; -.
DR Gramene; AT5G26030.1; AT5G26030.1; AT5G26030.
DR Gramene; AT5G26030.2; AT5G26030.2; AT5G26030.
DR KEGG; ath:AT5G26030; -.
DR Araport; AT5G26030; -.
DR TAIR; locus:2180642; AT5G26030.
DR eggNOG; KOG1321; Eukaryota.
DR HOGENOM; CLU_018884_4_2_1; -.
DR InParanoid; P42043; -.
DR OMA; LGDPYHC; -.
DR OrthoDB; 1003638at2759; -.
DR PhylomeDB; P42043; -.
DR BioCyc; ARA:AT5G26030-MON; -.
DR BRENDA; 4.99.1.1; 399.
DR UniPathway; UPA00252; UER00325.
DR PRO; PR:P42043; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P42043; baseline and differential.
DR Genevisible; P42043; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004325; F:ferrochelatase activity; IGI:TAIR.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0033014; P:tetrapyrrole biosynthetic process; IMP:TAIR.
DR CDD; cd00419; Ferrochelatase_C; 1.
DR CDD; cd03411; Ferrochelatase_N; 1.
DR HAMAP; MF_00323; Ferrochelatase; 1.
DR InterPro; IPR001015; Ferrochelatase.
DR InterPro; IPR019772; Ferrochelatase_AS.
DR InterPro; IPR033644; Ferrochelatase_C.
DR InterPro; IPR033659; Ferrochelatase_N.
DR PANTHER; PTHR11108; PTHR11108; 1.
DR Pfam; PF00762; Ferrochelatase; 1.
DR TIGRFAMs; TIGR00109; hemH; 1.
DR PROSITE; PS00534; FERROCHELATASE; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Heme biosynthesis; Iron; Lyase; Membrane; Mitochondrion;
KW Plastid; Porphyrin biosynthesis; Reference proteome; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..466
FT /note="Ferrochelatase-1, chloroplastic/mitochondrial"
FT /id="PRO_0000008880"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 58
FT /note="T -> M (in Ref. 5; BAH56957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 52033 MW; BAB2F960A5AEBB6A CRC64;
MQATALSSGF NPLTKRKDHR FPRSCSQRNS LSLIQCDIKE RSFGESMTIT NRGLSFKTNV
FEQARSVTGD CSYDETSAKA RSHVVAEDKI GVLLLNLGGP ETLNDVQPFL YNLFADPDII
RLPRPFQFLQ GTIAKFISVV RAPKSKEGYA AIGGGSPLRK ITDEQADAIK MSLQAKNIAA
NVYVGMRYWY PFTEEAVQQI KKDKITRLVV LPLYPQYSIS TTGSSIRVLQ DLFRKDPYLA
GVPVAIIKSW YQRRGYVNSM ADLIEKELQT FSDPKEVMIF FSAHGVPVSY VENAGDPYQK
QMEECIDLIM EELKARGVLN DHKLAYQSRV GPVQWLKPYT DEVLVDLGKS GVKSLLAVPV
SFVSEHIETL EEIDMEYREL ALESGVENWG RVPALGLTPS FITDLADAVI ESLPSAEAMS
NPNAVVDSED SESSDAFSYI VKMFFGSILA FVLLLSPKMF HAFRNL
