HEMJ_HELPY
ID HEMJ_HELPY Reviewed; 148 AA.
AC O26018;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=HP_1484;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD08519.1; -; Genomic_DNA.
DR PIR; D64705; D64705.
DR RefSeq; NP_208275.1; NC_000915.1.
DR RefSeq; WP_000506456.1; NC_018939.1.
DR AlphaFoldDB; O26018; -.
DR IntAct; O26018; 1.
DR STRING; 85962.C694_07685; -.
DR PaxDb; O26018; -.
DR EnsemblBacteria; AAD08519; AAD08519; HP_1484.
DR KEGG; hpy:HP_1484; -.
DR PATRIC; fig|85962.47.peg.1595; -.
DR eggNOG; COG1981; Bacteria.
DR OMA; VRLFIYH; -.
DR PhylomeDB; O26018; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000000429; 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..148
FT /note="Protoporphyrinogen IX oxidase"
FT /id="PRO_0000217658"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
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; 17159 MW; B3A4B71CBE0243E6 CRC64;
MGFLNGYFLW VKAFHVIAVI SWMAALFYLP RLFVYHAENA HKKEFVGVVQ IQEKKLYSFI
ASPAMGFTLI TGILMLLIEP TLFKSGGWLH AKLALVVLLL AYHFYCKKCM RELEKDPTRR
NARFYRVFNE APTILMILIV ILVVVKPF
