ID HEMH_BURTA Reviewed; 355 AA. AC Q2SYZ9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-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=BTH_I1303; OS Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / OS CIP 106301). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., RA Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., RA Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., RA Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., RA Roberts K., Hatch B., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. 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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the ferrochelatase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000086; ABC36533.1; -; Genomic_DNA. DR RefSeq; YP_441850.1; -. DR GeneID; 3847181; -. DR GenomeReviews; CP000086_GR; BTH_I1303. DR KEGG; bte:BTH_I1303; -. DR TIGR; BTH_I1303; -. DR HOGENOM; Q2SYZ9; -. DR OMA; Q2SYZ9; TIEEIGM. DR BioCyc; BTHA271848:BTH_I1303-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 1 355 Ferrochelatase. FT /FTId=PRO_1000059476. FT METAL 214 214 Iron (By similarity). FT METAL 295 295 Iron (By similarity). SQ SEQUENCE 355 AA; 39370 MW; B04F91B3988547DF CRC64; MRFDLEPPSH ASAAHRVAVL LVNLGTPDEP TPRAVRRYLA QFLSDPRVVE IPQLVWQVIL RTLILPLRGR ASAKKYAAVW LPEGSPLRVY TERQVESLKP LFAANGYRVI VDYAMRYGTP SIADVLAQLK RAGAERVLLL PMYPQYSAST TATAFDAAFA ALGRMRNQPE VRTVRHYADH PAYIHALAEQ VRQYWAAHGR PAFDSGDKLV LSFHGVPKRT LDLGDPYHDQ CQQTAALLMS ALGLTTFECR VTFQSRFGKA EWLQPYTAPT LKELGAAGVR RADVFCPGFT ADCLETIEEI GMEVRDEFLH GGGKEFHRIP CLNASHAWIA ALGEIAAENL QGWPVRVATA PEAVT //