ID   HEMH_HORVU              Reviewed;         484 AA.
AC   P42045; O22524;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Ferrochelatase-2, chloroplastic;
DE            EC=4.99.1.1;
DE   AltName: Full=Ferrochelatase II;
DE   AltName: Full=Heme synthase 2;
DE   AltName: Full=Protoheme ferro-lyase 2;
DE   Flags: Precursor;
GN   Name=HEMH;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Svalofs Bonus;
RX   PubMed=8066144; DOI=10.1104/pp.105.2.769;
RA   Miyamoto K., Tanaka R., Teramoto H., Masuda T., Tsuji H., Inokuchi H.;
RT   "Nucleotide sequences of cDNA clones encoding ferrochelatase from barley
RT   and cucumber.";
RL   Plant Physiol. 105:769-770(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hansson M., Gough S.P., Kannangara C.G., von Wettstein D.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
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   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000305}.
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DR   EMBL; D26105; BAA05101.1; -; mRNA.
DR   EMBL; AF020791; AAB71887.1; -; Genomic_DNA.
DR   PIR; T04373; T04373.
DR   PIR; T05736; T05736.
DR   AlphaFoldDB; P42045; -.
DR   SMR; P42045; -.
DR   UniPathway; UPA00252; UER00325.
DR   ExpressionAtlas; P42045; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblPlants.
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; Plastid;
KW   Porphyrin biosynthesis; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..484
FT                   /note="Ferrochelatase-2, chloroplastic"
FT                   /id="PRO_0000008883"
FT   CONFLICT        165
FT                   /note="N -> K (in Ref. 2; AAB71887)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   484 AA;  53472 MW;  F66B95744DFEE172 CRC64;
     MECVRSGALD LGRSGNFLGK SGSTTSCGKV RCSTNLAGST KCEQNLHGKA KPLLLSASGK
     ARGTSGLVHR SPVLKHQHHL SVRSTSTDVC TTFDEDVKGV SSHAVEEKVG VLLLNLGGPE
     TLNDVQPFLF NLFADPDIIR LPRLFRFLQR PLAKLISTFR APKSNEGYAS IGGGSPLRKI
     TDEQANALKV ALKSKNLEAD IYVGMRYWYP FTEEAIDQIK KDKITKLVVL PLYPQYSIST
     SGSSIRVLQN IVKEDPYFAG LPISIIESWY QREGYVKSMA DLIEKELSVF SNPEEVMIFF
     SAHGVPLTYV KDAGDPYRDQ MEDCIALIME ELKSRGTLND HTLAYQSRVG PVQWLKPYTD
     EVLVELGQKG VKSLLAVPVS FVSEHIETLE EIDMEYRELA LESGIENWGR VPALGCTSSF
     ISDLADAVVE ALPSASAMAT RKVKDTDSDM DMMHYLTKMF LGSVLAFFLL LSPRLVSAFR
     NTLQ