ID   HEMJ_RICPR              Reviewed;         145 AA.
AC   Q9ZC85;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Protoporphyrinogen IX oxidase {ECO:0000250|UniProtKB:P72793};
DE            Short=PPO {ECO:0000250|UniProtKB:P72793};
DE            EC=1.3.99.- {ECO:0000250|UniProtKB:P72793};
GN   OrderedLocusNames=RP883;
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 oxidation of protoporphyrinogen IX to
CC       protoporphyrin IX. Is involved in the biosynthesis of tetrapyrrole
CC       molecules like heme. Does not use oxygen or artificial electron
CC       acceptors such as menadione or benzoquinone.
CC       {ECO:0000250|UniProtKB:P72793}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 A + protoporphyrinogen IX = 3 AH2 + protoporphyrin IX;
CC         Xref=Rhea:RHEA:62000, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:57306, ChEBI:CHEBI:57307;
CC         Evidence={ECO:0000250|UniProtKB:P72793};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P72793};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000250|UniProtKB:P72793};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC       {ECO:0000250|UniProtKB:P72793}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P72793}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P72793};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the HemJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_02239, ECO:0000305}.
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DR   EMBL; AJ235273; CAA15305.1; -; Genomic_DNA.
DR   PIR; A71651; A71651.
DR   RefSeq; NP_221229.1; NC_000963.1.
DR   RefSeq; WP_004599693.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZC85; -.
DR   STRING; 272947.RP883; -.
DR   EnsemblBacteria; CAA15305; CAA15305; CAA15305.
DR   GeneID; 57570006; -.
DR   KEGG; rpr:RP883; -.
DR   PATRIC; fig|272947.5.peg.923; -.
DR   eggNOG; COG1981; Bacteria.
DR   HOGENOM; CLU_125006_1_0_5; -.
DR   OMA; VRLFIYH; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070818; F:protoporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_02239; HemJ; 1.
DR   InterPro; IPR005265; HemJ-like.
DR   PANTHER; PTHR40255; PTHR40255; 1.
DR   Pfam; PF03653; UPF0093; 1.
DR   PIRSF; PIRSF004638; UCP004638; 1.
DR   TIGRFAMs; TIGR00701; TIGR00701; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Heme; Iron; Membrane; Metal-binding; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..145
FT                   /note="Protoporphyrinogen IX oxidase"
FT                   /id="PRO_0000217661"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         12
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P72793"
FT   BINDING         88
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P72793"
SQ   SEQUENCE   145 AA;  16915 MW;  8808506DA34F9612 CRC64;
     MESYYLWFKS AHLISAICWM AGLLYLPRIY VYHTKAKIGS ELDSTLQVME LKLLRFIMNP
     AMISTFIFGL INAHIYGFVA LDTWFQFKMF AVLILVIFHG LLARWRKDFA KGKNVHSKKF
     YRIVNEIPAI CMVIAVIMVI VKPFD