HEMH2_ARATH
ID HEMH2_ARATH Reviewed; 512 AA.
AC O04921; O23623; Q7GB39;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ferrochelatase-2, chloroplastic {ECO:0000305};
DE Short=AtFC2 {ECO:0000305};
DE EC=4.99.1.1 {ECO:0000305};
DE AltName: Full=Ferrochelatase-II {ECO:0000303|PubMed:9753778};
DE Short=AtFC-II {ECO:0000303|PubMed:12374307};
DE AltName: Full=Heme synthase 2 {ECO:0000305};
DE AltName: Full=Protoheme ferro-lyase 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=FC2 {ECO:0000303|PubMed:24329537};
GN Synonyms=FC-II {ECO:0000303|PubMed:9753778}; OrderedLocusNames=At2g30390;
GN ORFNames=T06B20.24, T9D9.1;
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. Columbia; TISSUE=Seedling;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
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 [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-84, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-83, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26494759; DOI=10.1126/science.aac7444;
RA Woodson J.D., Joens M.S., Sinson A.B., Gilkerson J., Salome P.A.,
RA Weigel D., Fitzpatrick J.A., Chory J.;
RT "Ubiquitin facilitates a quality-control pathway that removes damaged
RT chloroplasts.";
RL Science 350:450-454(2015).
CC -!- FUNCTION: Catalyzes the last step of heme biosynthesis by inserting
CC ferrous iron into protoporphyrin IX to produce protoheme. Produces heme
CC for photosynthetic cytochromes, and for proteins involved in abiotic
CC and biotic stress responses (PubMed:24329537). May play a role in the
CC quality control of individual chloroplasts during photo-oxidative
CC stress through regulation of heme biosynthesis (PubMed:26494759).
CC {ECO:0000269|PubMed:24329537, ECO:0000269|PubMed:26494759}.
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}. Note=(PubMed:11602264) shows experimental
CC evidences that FC2 is not present in Arabidopsis mitochondria in vivo.
CC {ECO:0000305|PubMed:11602264}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O04921-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers.
CC {ECO:0000269|PubMed:12374307}.
CC -!- INDUCTION: Down-regulated by wounding or oxidative stress.
CC {ECO:0000269|PubMed:12374307}.
CC -!- DISRUPTION PHENOTYPE: Abnormal, small, and pale green rosette leaves
CC (PubMed:24329537, PubMed:26494759). Low contents in chlorophylls,
CC carotenoids and photosynthetic proteins in leaves. Impaired
CC photosynthetic performance. Increased resistance to salt and flagellin
CC treatment (PubMed:24329537). Increased sensitivity to de-etiolation
CC (PubMed:26494759). {ECO:0000269|PubMed:24329537,
CC ECO:0000269|PubMed:26494759}.
CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000305}.
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DR EMBL; Y13156; CAA73614.1; -; mRNA.
DR EMBL; AC002338; AAM14820.1; -; Genomic_DNA.
DR EMBL; U93215; AAB63095.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08379.1; -; Genomic_DNA.
DR EMBL; BT000465; AAN17442.1; -; mRNA.
DR EMBL; BT008877; AAP68316.1; -; mRNA.
DR PIR; H84707; H84707.
DR RefSeq; NP_180598.1; NM_128592.3. [O04921-1]
DR AlphaFoldDB; O04921; -.
DR SMR; O04921; -.
DR BioGRID; 2938; 6.
DR IntAct; O04921; 4.
DR STRING; 3702.AT2G30390.2; -.
DR iPTMnet; O04921; -.
DR PaxDb; O04921; -.
DR PRIDE; O04921; -.
DR ProteomicsDB; 230359; -. [O04921-1]
DR EnsemblPlants; AT2G30390.1; AT2G30390.1; AT2G30390. [O04921-1]
DR GeneID; 817589; -.
DR Gramene; AT2G30390.1; AT2G30390.1; AT2G30390. [O04921-1]
DR KEGG; ath:AT2G30390; -.
DR Araport; AT2G30390; -.
DR eggNOG; KOG1321; Eukaryota.
DR HOGENOM; CLU_018884_4_3_1; -.
DR InParanoid; O04921; -.
DR PhylomeDB; O04921; -.
DR BioCyc; ARA:AT2G30390-MON; -.
DR UniPathway; UPA00252; UER00325.
DR PRO; PR:O04921; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04921; baseline and differential.
DR Genevisible; O04921; AT.
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; IBA:GO_Central.
DR GO; GO:0055035; C:plastid thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0004325; F:ferrochelatase activity; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:UniProtKB.
DR GO; GO:0033014; P:tetrapyrrole biosynthetic process; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chloroplast; Heme biosynthesis; Iron;
KW Lyase; Membrane; Plastid; Porphyrin biosynthesis; Reference proteome;
KW Thylakoid; Transit peptide.
FT TRANSIT 1..83
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 84..512
FT /note="Ferrochelatase-2, chloroplastic"
FT /id="PRO_0000008881"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 156..159
FT /note="SKEG -> ARR (in Ref. 1; CAA73614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 56619 MW; 521B1FC596E844A7 CRC64;
MNCPAMTASP SSSSSSSYST FRPPPPLLPQ LSNDSQRSVV MHCTRLPFEA FAATSSNRLL
GKHSLPLRAA LVTSNPLNIS SSSVISDAIS SSSVITDDAK IGVLLLNLGG PETLDDVQPF
LFNLFADPDI IRLPPVFQFL QKPLAQFISV ARAPKSKEGY ASIGGGSPLR HITDAQAEEL
RKCLWEKNVP AKVYVGMRYW HPFTEEAIEQ IKRDGITKLV VLPLYPQFSI STSGSSLRLL
ERIFREDEYL VNMQHTVIPS WYQREGYIKA MANLIQSELG KFGSPNQVVI FFSAHGVPLA
YVEEAGDPYK AEMEECVDLI MEELDKRKIT NAYTLAYQSR VGPVEWLKPY TEEAITELGK
KGVENLLAVP ISFVSEHIET LEEIDVEYKE LALKSGIKNW GRVPALGTEP MFISDLADAV
VESLPYVGAM AVSNLEARQS LVPLGSVEEL LATYDSQRRE LPAPVTMWEW GWTKSAETWN
GRAAMLAVLA LLVLEVTTGK GFLHQWGILP SL
