ID   HEMH_BURCM              Reviewed;         354 AA.
AC   Q0BI24;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=Bamb_0640;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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; CP000440; ABI86199.1; -; Genomic_DNA.
DR   RefSeq; YP_772533.1; -.
DR   GeneID; 4309287; -.
DR   GenomeReviews; CP000440_GR; Bamb_0640.
DR   KEGG; bam:Bamb_0640; -.
DR   NMPDR; fig|339670.3.peg.3167; -.
DR   OMA; Q0BI24; TIEEIGM.
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    354       Ferrochelatase.
FT                                /FTId=PRO_1000019278.
FT   METAL       214    214       Iron (By similarity).
FT   METAL       295    295       Iron (By similarity).
SQ   SEQUENCE   354 AA;  39156 MW;  5A3846DB1970472F CRC64;
     MRFDLEPPSS VAAAHRTGVL LINLGTPDAP TPRAVRRYLA EFLSDPRVVE IPQVVWQVLL
     RTLILPLRGR ASAKKYAAVW MPEGSPLRVY TERQTEGVRH LLASNAYQVT VDYAMRYGSP
     NIAQALAQFK RAGVERVLLM PMYPQYSAST TATAFDAAFA ALARMRNQPE VRTVRQYADH
     PAYIHALAEQ VRQYWAQHGR PDFAAGDKLV LSFHGVPKRT LDLGDPYHDQ CQQTGALLMA
     ALGLSTLECR VTFQSRFGKA EWLQPYTAPT LRELGAAGVR RADVFCPGFT ADCLETIEEI
     GMEVRDEFIA GGGQAFHRIP CLNGAHAWIG ALGEIVAENL QGWPVKAAQP DMVN
//