ID   HEMH_BRUSU              Reviewed;         352 AA.
AC   P0A3D7; Q939N8; Q93TG2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=BRA0076;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
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.
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DR   EMBL; AE014292; AAN33288.1; -; Genomic_DNA.
DR   RefSeq; NP_699283.1; -.
DR   GeneID; 1164513; -.
DR   GenomeReviews; AE014292_GR; BRA0076.
DR   KEGG; bms:BRA0076; -.
DR   TIGR; BRA0076; -.
DR   HOGENOM; P0A3D7; -.
DR   OMA; P0A3D7; TIEEIGM.
DR   BioCyc; BSUI204722:BR_A0076-MON; -.
DR   BRENDA; 4.99.1.1; 281610.
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    352       Ferrochelatase.
FT                                /FTId=PRO_0000175122.
FT   METAL       222    222       Iron (By similarity).
FT   METAL       303    303       Iron (By similarity).
SQ   SEQUENCE   352 AA;  40057 MW;  5FE6C0F0EA435D32 CRC64;
     MSGTDKVRVN VSQTAQTPLH TSAKLPKVGV LLVNLGTPDG TSYGPMRRYL AEFLSDRRVI
     EWSRLIWYPI LYGIVLNTRP RRSGRLYDRI WNHENNESPL RTYTRAQGEK LAKALSDQPN
     VVVDWAMRYG QPSIESITDR LLQQGCERIV IFPLYPQYSA TTTATVNDKF FEALMKKRFM
     PAIRTVPSYE AEPVYIDALA RSVEKHLATL SFKPEVILTS YHGIPKSYSD KGDPYRQQCL
     ETTRLLRERL GLGEDEMRAT FQSRFGPEEW LQPYTDETVK ELAKNGVKSV AVLNPGFVAD
     CLETVDEIGN EAAEEFLENG GENFSHIPCL NDSEEGMKVI ETLVRRELLG WV
//