ID HEMH_ALCBS Reviewed; 341 AA. AC Q0VSV6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 23. 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=ABO_0294; OS Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., RA Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., RA Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., RA Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., RA Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., RA Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine RT bacterium Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(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 -!- 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; AM286690; CAL15742.1; -; Genomic_DNA. DR RefSeq; YP_692014.1; -. DR GeneID; 4212187; -. DR GenomeReviews; AM286690_GR; ABO_0294. DR KEGG; abo:ABO_0294; -. DR NMPDR; fig|393595.12.peg.292; -. DR HOGENOM; Q0VSV6; -. DR OMA; Q0VSV6; MSFHGLP. DR BioCyc; ABOR393595:ABO_0294-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 1 341 Ferrochelatase. FT /FTId=PRO_1000019271. FT METAL 210 210 Iron (By similarity). FT METAL 291 291 Iron (By similarity). SQ SEQUENCE 341 AA; 38529 MW; 2C5B379B9284C704 CRC64; MAYKGQENLE HLNPRKVGVL ITNLGTPDAP ETGALRRYLR EFLSDPRVVE IPRFIWFFIL NLVILVIRPR KSAEAYKSVW TEEGSPLLVY SLAQGEGIRQ RLQSKYGDDV VVRVAMRYGN PSIASQLQAF EDEGIRKLVV LPLYPQYSGS TNGSTFDAVA QDFMGRRLLP DLRFISHYPD YPPYIQAMAE HIRAYREKNG SADKLVFSFH GVPKRFLLKG DPYFHECHQT SQLLAKALGL SDGQWMTTFQ SRFGAEEWLQ PYTDATMKSL PGEGVKSVQV FCPGFSADCL ETVEEIDQEN REYFEEAGGE SFAYISALNA EPAHLDALAQ LVEDNLQGFL P //