HEMH_BRUAB
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 03-AUG-2022, entry version 86.
DE RecName: Full=Ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323};
DE EC=4.99.1.1 {ECO:0000255|HAMAP-Rule:MF_00323};
DE AltName: Full=Heme synthase {ECO:0000255|HAMAP-Rule:MF_00323};
DE AltName: Full=Protoheme ferro-lyase {ECO:0000255|HAMAP-Rule:MF_00323};
GN Name=hemH {ECO:0000255|HAMAP-Rule:MF_00323}; OrderedLocusNames=BruAb2_0076;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
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 PubMed=11553564; 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;
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., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX;
CC Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00323};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}.
CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000255|HAMAP-
CC Rule:MF_00323}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF358663; AAK43712.1; -; Genomic_DNA.
DR EMBL; AY027659; AAK14798.1; -; Genomic_DNA.
DR EMBL; AE017224; AAX75527.1; -; Genomic_DNA.
DR RefSeq; WP_002966503.1; NC_006933.1.
DR AlphaFoldDB; P0A3D8; -.
DR SMR; P0A3D8; -.
DR EnsemblBacteria; AAX75527; AAX75527; BruAb2_0076.
DR GeneID; 3828247; -.
DR KEGG; bmb:BruAb2_0076; -.
DR HOGENOM; CLU_018884_0_0_5; -.
DR OMA; LGDPYHC; -.
DR BRENDA; 4.99.1.1; 994.
DR UniPathway; UPA00252; UER00325.
DR PRO; PR:P0A3D8; -.
DR Proteomes; UP000000540; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00419; Ferrochelatase_C; 1.
DR CDD; cd03411; Ferrochelatase_N; 1.
DR HAMAP; MF_00323; Ferrochelatase; 1.
DR InterPro; IPR001015; Ferrochelatase.
DR InterPro; IPR019772; Ferrochelatase_AS.
DR InterPro; IPR033644; Ferrochelatase_C.
DR InterPro; IPR033659; Ferrochelatase_N.
DR PANTHER; PTHR11108; PTHR11108; 1.
DR Pfam; PF00762; Ferrochelatase; 1.
DR TIGRFAMs; TIGR00109; hemH; 1.
DR PROSITE; PS00534; FERROCHELATASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Heme biosynthesis; Iron; Lyase; Metal-binding;
KW Porphyrin biosynthesis.
FT CHAIN 1..352
FT /note="Ferrochelatase"
FT /id="PRO_0000175120"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 303
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT CONFLICT 208
FT /note="A -> V (in Ref. 2; AAK14798)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="L -> S (in Ref. 1; AAK43712)"
FT /evidence="ECO:0000305"
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
