ID   HEMJ_HELPJ              Reviewed;         148 AA.
AC   Q9ZJD5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=jhp_1377;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; 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 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; AE001439; AAD06948.1; -; Genomic_DNA.
DR   PIR; D71815; D71815.
DR   RefSeq; WP_000395115.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZJD5; -.
DR   STRING; 85963.jhp_1377; -.
DR   EnsemblBacteria; AAD06948; AAD06948; jhp_1377.
DR   KEGG; hpj:jhp_1377; -.
DR   PATRIC; fig|85963.30.peg.1174; -.
DR   eggNOG; COG1981; Bacteria.
DR   OMA; VRLFIYH; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000000804; 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   Transmembrane; Transmembrane helix.
FT   CHAIN           1..148
FT                   /note="Protoporphyrinogen IX oxidase"
FT                   /id="PRO_0000217659"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         15
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         92
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   148 AA;  17149 MW;  0CA8E3117D93CC4C CRC64;
     MEFLSGYFLW VKAFHVIAVI SWMAALFYLP RLFVYHAENA HKKEFVGVVQ IQEKKLYSFI
     ASPAMGFTLI TGILMLLIAP EMFKSGGWLH AKLALVVLLL IYHFYCKKCM RELEKDPTGK
     NARFYRVFNE IPTILMILIV ILVVVKPF