ID   HEMH_CUCSA              Reviewed;         514 AA.
AC   P42044;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 86.
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   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Aonagajibai;
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).
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; D26106; BAA05102.1; -; mRNA.
DR   PIR; T10246; T10246.
DR   RefSeq; NP_001295803.1; NM_001308874.1.
DR   AlphaFoldDB; P42044; -.
DR   SMR; P42044; -.
DR   PRIDE; P42044; -.
DR   GeneID; 101216568; -.
DR   KEGG; csv:101216568; -.
DR   UniPathway; UPA00252; UER00325.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
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           ?..514
FT                   /note="Ferrochelatase-2, chloroplastic"
FT                   /id="PRO_0000008882"
SQ   SEQUENCE   514 AA;  57207 MW;  AF85085363B44582 CRC64;
     MDAASSSLAL SNIKLHGSTN TLNSDQRISS LCSLPKSRVT FSCKTSGNLQ VRDRSTGLVV
     SCSSSNGDRD VIQGLHLSGP IEKKSRLGQA CCSVGTFTVG EFALESQSQA VDDKVGVLLL
     NLGGPETLDD VQPFLYNLFA DPDIIRLPRL FRFLQEPLAK LISTYRAPKS KEGYASIGGG
     SPLRKITDEQ AQALKMALAE KNMSTNVYVG MRYWYPFTEE AIQQIKRDGI TRLVVLPLYP
     QYSISTTGSS IRVLQKMFRE DAYLSSLPVS IIKSWYQREG YIKSMADLMQ AELKNFANPQ
     EVMIFFSAHG VPVSYVENAG DPYKDQMEEC ICLIMQELKA RGIGNEHTLA YQSRVGPVQW
     LKPYTDEVLV ELGQKGIKSL LAVPVSFVSE HIETLEEIDM EYKHLALESG IQNWGRVPAL
     NCNSSFISDL ADAVIEALPS ATALAPHTSS TDADDHDPFL YAIKLLFGSV LAFILLLSPK
     AFMVFRNNFL LNYTRIYGYR GERSEFFWVR LIFT