ID HEMH_MYCUA Reviewed; 340 AA.
AC A0PNU6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 01-MAY-2013, entry version 45.
DE RecName: Full=Ferrochelatase;
DE EC=4.99.1.1;
DE AltName: Full=Heme synthase;
DE AltName: Full=Protoheme ferro-lyase;
GN Name=hemH; OrderedLocusNames=MUL_1493;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L.,
RA Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C.,
RA Jones L.M., Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: Protoheme + 2 H(+) = protoporphyrin + Fe(2+).
CC -!- PATHWAY: Porphyrin metabolism; protoheme biosynthesis; protoheme
CC from protoporphyrin-IX: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the ferrochelatase family.
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DR EMBL; CP000325; ABL04015.1; -; Genomic_DNA.
DR RefSeq; YP_905486.1; NC_008611.1.
DR ProteinModelPortal; A0PNU6; -.
DR STRING; 362242.MUL_1493; -.
DR EnsemblBacteria; ABL04015; ABL04015; MUL_1493.
DR GeneID; 4552377; -.
DR KEGG; mul:MUL_1493; -.
DR PATRIC; 18169880; VBIMycUlc37413_1796.
DR GenoList; MUL_1493; -.
DR eggNOG; COG0276; -.
DR HOGENOM; HOG000060728; -.
DR KO; K01772; -.
DR OMA; PDICDHL; -.
DR ProtClustDB; PRK00035; -.
DR UniPathway; UPA00252; UER00325.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_00323; Ferrochelatase; 1; -.
DR InterPro; IPR001015; Ferrochelatase.
DR InterPro; IPR019772; Ferrochelatase_AS.
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 Complete proteome; Cytoplasm; Heme biosynthesis; Iron; Lyase;
KW Metal-binding; Porphyrin biosynthesis.
FT CHAIN 1 340 Ferrochelatase.
FT /FTId=PRO_1000019326.
FT METAL 172 172 Iron (By similarity).
FT METAL 255 255 Iron (By similarity).
SQ SEQUENCE 340 AA; 36357 MW; 07952AB4780C3D82 CRC64;
MEFDAVLLLS FGGPEGPEQV RPFLENVTRG RGVPPERLDA VAEHYMHFGG VSPINGINRA
LVTELRAEVG LPVYFGNRNW EPYVEDTVMA MRDNGVKRAA VFATSAWSGY SGCTQYVEDI
ARARRAAGPD APELVKLRSY FDHPLFVEMF ADAIAAAAAT VPKGARLVFT AHSIPVAADR
RCGPGLYSRQ VAYAASLVAA AAGYDDYDLA WQSRSGPPQV PWLEPDVADH LEMLRAGGVK
AVIVCPIGFV ADHIEVVWDL DAELRAQAQD AGIALARAAT PNADRRFARL ARGLIEELRS
GGEPARVGGP DSVSGCLAGV NGEPCRPPHC AARETAPQGA
//
