ID   HEMH_ECOUT              Reviewed;         320 AA.
AC   Q1RF60;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Ferrochelatase;
DE            EC=4.99.1.1;
DE   AltName: Full=Protoheme ferro-lyase;
DE   AltName: Full=Heme synthetase;
GN   Name=hemH; OrderedLocusNames=UTI89_C0503;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC   -!- CATALYTIC ACTIVITY: Protoheme + 2 H(+) = protoporphyrin + Fe(2+).
CC   -!- PATHWAY: Porphyrin metabolism; protoheme biosynthesis; protoheme
CC       from protoporphyrin-IX: step 1/1.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ferrochelatase family.
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DR   EMBL; CP000243; ABE06004.1; -; Genomic_DNA.
DR   RefSeq; YP_539535.1; -.
DR   GeneID; 3991671; -.
DR   GenomeReviews; CP000243_GR; UTI89_C0503.
DR   KEGG; eci:UTI89_C0503; -.
DR   HOGENOM; Q1RF60; -.
DR   OMA; Q1RF60; TIEEIGM.
DR   BioCyc; ECOL364106:UTI89_C0503-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00323; -; 1.
DR   InterPro; IPR001015; Ferrochelatase.
DR   InterPro; IPR019772; Ferrochelatase_AS.
DR   PANTHER; PTHR11108; Ferrochelatase; 1.
DR   Pfam; PF00762; Ferrochelatase; 1.
DR   ProDom; PD002792; Ferrochelatase; 1.
DR   TIGRFAMs; TIGR00109; hemH; 1.
DR   PROSITE; PS00534; FERROCHELATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Heme biosynthesis; Iron; Lyase;
KW   Metal-binding; Porphyrin biosynthesis.
FT   CHAIN         1    320       Ferrochelatase.
FT                                /FTId=PRO_1000019296.
FT   METAL       194    194       Iron (By similarity).
FT   METAL       275    275       Iron (By similarity).
SQ   SEQUENCE   320 AA;  35942 MW;  79E6F8BF465B1E7E CRC64;
     MRQTKTGILL ANLGTPDAPT PEAVKRYLKQ FLSDRRVVDT SRLLWWPLLR GVILPLRSPR
     VAKLYASVWM EGGSPLMVYS RQQQQALAQR LPETPVALGM SYGSPSLESA VDELLAEHVD
     HIVVLPLYPQ YSCSTVGAVW DELARILARK RSIPGISFIR DYADNHDYIN ALANSVRASF
     AKHGEPDLLL LSYHGIPQRY ADEGDDYPQR CRTTTRELAS ALEMAPEKVM MTFQSRFGRE
     PWLMPYTDET LKMLGEKGVG HIQVMCPGFA ADCLETLEEI AEQNREVFLG AGGKKYEYIP
     ALNATPEHIE MMANLVAAYR
//