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   27-MAR-2024, entry version 161.
DE   RecName: Full=Ferrochelatase-1, chloroplastic/mitochondrial {ECO:0000305};
DE            Short=AtFC1 {ECO:0000303|PubMed:17416636};
DE            EC=4.98.1.1 {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}, HEM15
GN   {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       undeveloped 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=4.98.1.1;
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}.
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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.P42043; -.
DR   PaxDb; 3702-AT5G26030-1; -.
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; AT5G26030; FC1.
DR   eggNOG; KOG1321; Eukaryota.
DR   HOGENOM; CLU_018884_4_2_1; -.
DR   InParanoid; P42043; -.
DR   OMA; DPYHCEC; -.
DR   OrthoDB; 5970at2759; -.
DR   PhylomeDB; P42043; -.
DR   BioCyc; ARA:AT5G26030-MONOMER; -.
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   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   Gene3D; 3.40.50.1400; -; 2.
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   NCBIfam; TIGR00109; hemH; 1.
DR   PANTHER; PTHR11108; FERROCHELATASE; 1.
DR   PANTHER; PTHR11108:SF4; FERROCHELATASE-1, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   Pfam; PF00762; Ferrochelatase; 1.
DR   SUPFAM; SSF53800; Chelatase; 1.
DR   PROSITE; PS00534; FERROCHELATASE; 1.
DR   Genevisible; P42043; AT.
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
//