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HEMH_RICPR
ID   HEMH_RICPR              Reviewed;         342 AA.
AC   Q9ZC84;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   03-AUG-2022, entry version 105.
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=RP884;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA15306.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ235273; CAA15306.1; ALT_INIT; Genomic_DNA.
DR   PIR; B71651; B71651.
DR   RefSeq; NP_221230.1; NC_000963.1.
DR   RefSeq; WP_004599695.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZC84; -.
DR   SMR; Q9ZC84; -.
DR   STRING; 272947.RP884; -.
DR   EnsemblBacteria; CAA15306; CAA15306; CAA15306.
DR   GeneID; 57570007; -.
DR   KEGG; rpr:RP884; -.
DR   PATRIC; fig|272947.5.peg.924; -.
DR   eggNOG; COG0276; Bacteria.
DR   HOGENOM; CLU_018884_4_1_5; -.
DR   UniPathway; UPA00252; UER00325.
DR   Proteomes; UP000002480; 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   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..342
FT                   /note="Ferrochelatase"
FT                   /id="PRO_0000175194"
FT   BINDING         188
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
FT   BINDING         268
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00323"
SQ   SEQUENCE   342 AA;  39611 MW;  33EA8548F5CF0372 CRC64;
     MNKRIAIVLF NLGGPEDIEY VKPFLFNLFY DKAIINLPNP LRYIIAKIIS ITREKKSQKI
     YSLIGSKSYL IQETEKQKLA ITEKLKEFIK EDFIIFINMR YSTPFAKEVI GQIKEYNPSE
     IILLPLYPQF SSTTTGSSVK NFLQNIDIDI PIKTICCYPI EEDFIKAHVS IIKEKLYDKN
     FRILFSAHGL PKRIIKAGDP YSFQIKETVN KIVKELNIKD LDYKITYQSR VGPIEWLKPN
     TEDEIELAGK LKKDIIIVPI SFVSEHVETL VELDIEYKLI ADKYKIQYTR IPTLGTNKIF
     INSLTNILLR FINNTNTNLV MSSSSKRICP NKFTKCLCNL TN
 
 
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