ID   HEMH_BRUAB              Reviewed;         352 AA.
AC   P0A3D8; Q57A07; Q939N8; Q93TG2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   16-JUN-2009, entry version 32.
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=BruAb2_0076;
OS   Brucella abortus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=544 / Biovar 1;
RA   Tibor A., Aidant N., Letesson J.-J.;
RT   "Omp10 gene is located upstream of hemH in Brucella.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=21437627; PubMed=11553564;
RX   DOI=10.1128/IAI.69.10.6225-6230.2001;
RA   Almiron M., Martinez M., Sanjuan N., Ugalde R.A.;
RT   "Ferrochelatase is present in Brucella abortus and is critical for its
RT   intracellular survival and virulence.";
RL   Infect. Immun. 69:6225-6230(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941 / Biovar 1;
RX   PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L.,
RA   Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison
RT   to the highly similar genomes of Brucella melitensis and Brucella
RT   suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AF358663; AAK43712.1; -; Genomic_DNA.
DR   EMBL; AY027659; AAK14798.1; -; Genomic_DNA.
DR   EMBL; AE017224; AAX75527.1; -; Genomic_DNA.
DR   RefSeq; YP_222888.1; -.
DR   GeneID; 3341660; -.
DR   GenomeReviews; AE017224_GR; BruAb2_0076.
DR   KEGG; bmb:BruAb2_0076; -.
DR   HOGENOM; P0A3D8; -.
DR   OMA; P0A3D8; TIEEIGM.
DR   BioCyc; BABO262698:BRUAB2_0076-MON; -.
DR   BRENDA; 4.99.1.1; 575.
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_0000175120.
FT   METAL       222    222       Iron (By similarity).
FT   METAL       303    303       Iron (By similarity).
FT   CONFLICT    208    208       A -> V (in Ref. 2; AAK14798).
FT   CONFLICT    289    289       L -> S (in Ref. 1; AAK43712).
SQ   SEQUENCE   352 AA;  40083 MW;  4D76D2727A435D2D 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 ELAKNGVKLV AVLNPGFVAD
     CLETVDEIGN EAAEEFLENG GENFSHIPCL NDSEEGMKVI ETLVRRELLG WV
//