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HEMH_RIPO1
ID   HEMH_RIPO1              Reviewed;         387 AA.
AC   B7K399;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323};
DE            EC=4.99.1.1 {ECO:0000255|HAMAP-Rule:MF_00323};
DE   AltName: Full=Heme synthase {ECO:0000255|HAMAP-Rule:MF_00323};
DE   AltName: Full=Protoheme ferro-lyase {ECO:0000255|HAMAP-Rule:MF_00323};
GN   Name=hemH {ECO:0000255|HAMAP-Rule:MF_00323};
GN   OrderedLocusNames=PCC8801_0320;
OS   Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX   NCBI_TaxID=41431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
CC   -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC       {ECO:0000255|HAMAP-Rule:MF_00323}.
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:0000255|HAMAP-Rule:MF_00323};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00323}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}.
CC   -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00323}.
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DR   EMBL; CP001287; ACK64419.1; -; Genomic_DNA.
DR   RefSeq; WP_012593696.1; NC_011726.1.
DR   AlphaFoldDB; B7K399; -.
DR   SMR; B7K399; -.
DR   STRING; 41431.PCC8801_0320; -.
DR   EnsemblBacteria; ACK64419; ACK64419; PCC8801_0320.
DR   KEGG; cyp:PCC8801_0320; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_4_1_3; -.
DR   OMA; LGDPYHC; -.
DR   OrthoDB; 780534at2; -.
DR   UniPathway; UPA00252; UER00325.
DR   Proteomes; UP000008204; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW   Porphyrin biosynthesis; Reference proteome.
FT   CHAIN           1..387
FT                   /note="Ferrochelatase"
FT                   /id="PRO_1000119605"
FT   BINDING         196
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         277
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   387 AA;  44262 MW;  51F419426C029CC8 CRC64;
     MDRVGVLLLN LGGPEQLEDV RPFLFNLFSD PEIIRLPFPW LQKPLAWLIS SLRSEKSQEN
     YKQIGGGSPL RKITEAQAEA LEQRLAEIGH TAQIYIGMRY WHPFTEEAIA RIKRDRLKNL
     VILPLYPQFS ISTSGSSFRV LEEMWNADPQ LKAINYTLIP SWYDDPRYLA AMADLIAQEL
     DKCEEPNRVH IFFSAHGVPQ SYVDEAGDPY QAEIEACTRL IMQTLNRPND YTLAYQSRVG
     PVEWLKPYTE DALKELGEQG VQDLLVVPIS FVSEHIETLQ EIDIEYREVA EEAGIENFYR
     VPALNTHPVF IDSLAQLVTK SLQEPPCTFN QVIHPKENMK MYPQERWQWG LTTAAEVWNG
     RLAMVGFIAL LIELISGHGP LHFVGLL
 
 
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