HEMH_PORG3
ID HEMH_PORG3 Reviewed; 345 AA.
AC B2RHB4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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}; OrderedLocusNames=PGN_0240;
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
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; AP009380; BAG32759.1; -; Genomic_DNA.
DR RefSeq; WP_012457358.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RHB4; -.
DR SMR; B2RHB4; -.
DR STRING; 431947.PGN_0240; -.
DR EnsemblBacteria; BAG32759; BAG32759; PGN_0240.
DR GeneID; 29255489; -.
DR KEGG; pgn:PGN_0240; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_0_1_10; -.
DR OMA; FSYHGVP; -.
DR BioCyc; PGIN431947:G1G2V-268-MON; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000008842; 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; IPR033644; Ferrochelatase_C.
DR InterPro; IPR033659; Ferrochelatase_N.
DR PANTHER; PTHR11108; PTHR11108; 1.
DR Pfam; PF00762; Ferrochelatase; 1.
DR TIGRFAMs; TIGR00109; hemH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis.
FT CHAIN 1..345
FT /note="Ferrochelatase"
FT /id="PRO_1000116065"
FT BINDING 199
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ SEQUENCE 345 AA; 39594 MW; A2E7B7207FC8B37C CRC64;
MADRRRTDDN KGAREVVLLL NIGSPDSPEV KDVARYLNSF LTDRRIITLP FLLRQLLVRG
IITPFRKKSS AQKYRTVWDE STRSFPLISH TKAIARALAH TGRDVHVAMR YGKPTVADVL
KELPHGRSLV VLPLFPHYAM SSYETAVEHC KAEIRRLCPN LSFRVVQPFY AHEAYIRVLA
DNIRPYLTKP FDKLILSYHG IPRDHLDKTT RQALDLRHPE GCCTEEDPTA NVCYRYQTYR
TTALIREALC LAEEQVEQVF QSRVGHTEWL RPYLIERLSA WPQEETKRIL IACPSFVCDC
LESLEEVADH GQSIFKKAGG ADFTYIPCLN SGANWIDALR NILEE