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Database: UniProt/SWISS-PROT
Entry: HEMH_HELPJ
LinkDB: HEMH_HELPJ
Original site: HEMH_HELPJ 
ID   HEMH_HELPJ              Reviewed;         335 AA.
AC   Q9ZKD4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323};
DE            EC=4.98.1.1 {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=jhp_1005;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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=4.98.1.1;
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; AE001439; AAD06589.1; -; Genomic_DNA.
DR   PIR; A71860; A71860.
DR   RefSeq; WP_001049113.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZKD4; -.
DR   SMR; Q9ZKD4; -.
DR   KEGG; hpj:jhp_1005; -.
DR   PATRIC; fig|85963.30.peg.1585; -.
DR   eggNOG; COG0276; Bacteria.
DR   UniPathway; UPA00252; UER00325.
DR   Proteomes; UP000000804; Chromosome.
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   Gene3D; 3.40.50.1400; -; 2.
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   NCBIfam; TIGR00109; hemH; 1.
DR   PANTHER; PTHR11108; FERROCHELATASE; 1.
DR   PANTHER; PTHR11108:SF1; FERROCHELATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00762; Ferrochelatase; 1.
DR   SUPFAM; SSF53800; Chelatase; 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..335
FT                   /note="Ferrochelatase"
FT                   /id="PRO_0000175150"
FT   BINDING         207
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         288
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   335 AA;  38660 MW;  8AF6F48E3612C20C CRC64;
     MNLINEKLNN LENSATKSPK EAVVLLNMGG PNSLYEVGVF LKNMFDDPFI LTIKNNFMRK
     MVGKMIVNSR IEKSKKIYEK LGGKSPLTPI TFALTERLNE LDPSRFYTYA MRYTPPYASM
     VLQDLALKEI ESLVFFSMYP QYSSTTTLSS FNDAFNALKS LETFRPKVRV IERFYADKKL
     NEIILNTILS ALNNCKSQDF VLIFSVHGLP KSIVDAGDTY QQECEHHVSL LKELMQQKNI
     PFKEVLLSYQ SKLGPMKWLE PSTEELIEKH RKSNIIIYPL AFTIDNSETL YELDMQYRLM
     AERLAVKEYL VCPCLNDSIE FAKFIIELVK NLKSE
//
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