HEMH_BRADU
ID HEMH_BRADU Reviewed; 345 AA.
AC P28602;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 3.
DT 03-AUG-2022, entry version 130.
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=bll7752;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LO;
RX PubMed=1624416; DOI=10.1128/jb.174.13.4223-4229.1992;
RA Frustaci J.M., O'Brian M.R.;
RT "Characterization of a Bradyrhizobium japonicum ferrochelatase mutant and
RT isolation of the hemH gene.";
RL J. Bacteriol. 174:4223-4229(1992).
RN [2]
RP SEQUENCE REVISION.
RA O'Brian M.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
CC Essential for normal nodule development.
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, ECO:0000305}.
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DR EMBL; M92427; AAA26217.2; -; Genomic_DNA.
DR EMBL; BA000040; BAC53017.1; -; Genomic_DNA.
DR PIR; A42883; A42883.
DR RefSeq; NP_774392.1; NC_004463.1.
DR RefSeq; WP_011090477.1; NZ_CP011360.1.
DR AlphaFoldDB; P28602; -.
DR SMR; P28602; -.
DR STRING; 224911.27356036; -.
DR EnsemblBacteria; BAC53017; BAC53017; BAC53017.
DR GeneID; 64027499; -.
DR KEGG; bja:bll7752; -.
DR PATRIC; fig|224911.44.peg.7894; -.
DR eggNOG; COG0276; Bacteria.
DR HOGENOM; CLU_018884_0_0_5; -.
DR InParanoid; P28602; -.
DR OMA; LGDPYHC; -.
DR PhylomeDB; P28602; -.
DR UniPathway; UPA00252; UER00325.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004325; F:ferrochelatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..345
FT /note="Ferrochelatase"
FT /id="PRO_0000175119"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT CONFLICT 15
FT /note="Q -> R (in Ref. 1; AAA26217)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="T -> S (in Ref. 1; AAA26217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 38418 MW; 67833BFE08E0784C CRC64;
MSTAAPNETT QPTVQSGQKR VGVLLVNLGT PDTADAPGVR VYLKEFLSDA RVIEDQGLVW
KVVLNGIILR SRPRTKALDY QKIWNNEKNE SPLKTITRSQ SDKLAAALSD RDHVVVDWAM
RYGNPSIKSG IDALIAEGCD RILAVPLYPQ YSASTSATVC DEVFRVLARL RAQPTLRVTP
PYYEDEAYIE ALAVSIETHL ATLPFKPELI VASFHGMPKS YVDKGDPYQE HCIATTEALR
RRLGVDASKL LLTFQSRFGN DEWLQPYTDK TMERLAKEGV RRIAVVTPGF AADCLETLEE
IAQENAEIFK HNGGEQFSAI PCLNDSEPGM DVIRTLVLRE LQGWI
