HEMH_CHLPN
ID HEMH_CHLPN Reviewed; 327 AA.
AC Q9Z7V1; Q9JSD1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=CPn_0603, CP_0144, CpB0627;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP98556.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE001363; AAD18742.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38026.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98810.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98556.1; ALT_INIT; Genomic_DNA.
DR PIR; E72057; E72057.
DR PIR; H86565; H86565.
DR RefSeq; NP_224799.1; NC_000922.1.
DR RefSeq; WP_010883241.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z7V1; -.
DR SMR; Q9Z7V1; -.
DR STRING; 115711.CP_0144; -.
DR EnsemblBacteria; AAD18742; AAD18742; CPn_0603.
DR EnsemblBacteria; AAF38026; AAF38026; CP_0144.
DR GeneID; 45050651; -.
DR KEGG; cpa:CP_0144; -.
DR KEGG; cpj:hemZ; -.
DR KEGG; cpn:CPn_0603; -.
DR KEGG; cpt:CpB0627; -.
DR PATRIC; fig|115713.3.peg.672; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_4_1_0; -.
DR OMA; LGDPYHC; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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.
FT CHAIN 1..327
FT /note="Ferrochelatase"
FT /id="PRO_0000175129"
FT BINDING 187
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT CONFLICT 254
FT /note="V -> A (in Ref. 3; BAA98810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 37503 MW; 608A8DC2B2139D44 CRC64;
MTTPAYLLAN FGGPRHAKDL QEFLISLLTD RDVTGTFLPR VLHRHLFTFI AKKRVPKVLP
QYQSLQNWSP IYFDTETLAK TLSEILRAPV IPFHRYLPST HEKTLLALRT LHTRHVIGIP
LFPHFTYSVT GSIVRFFMKH VPEIPISWIP QFGSDSKFVS LITCHIRDFL QKLGILEKEC
CFLFSVHGLP VRYISQGDPY SKQCYESFSA ITTNFKQSEN FLCFQSKFGP GKWLSPSTAQ
LCQNIDTDKP NVIVVPFGFI SDHLETLYEI ERDYLPLLRS RGYRALRIPA IYSSPLWVST
LVDIVKENST VVAEELIKSG KKHTGIR
