ID A0A077F2L6_9PSED Unreviewed; 141 AA. AC A0A077F2L6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 19-JAN-2022, entry version 40. DE RecName: Full=Protoporphyrinogen IX oxidase {ECO:0000256|ARBA:ARBA00017504, ECO:0000256|HAMAP-Rule:MF_02239}; DE Short=PPO {ECO:0000256|HAMAP-Rule:MF_02239}; DE EC=1.3.99.- {ECO:0000256|HAMAP-Rule:MF_02239, ECO:0000256|PIRNR:PIRNR004638}; GN ORFNames=PSAKL28_04710 {ECO:0000313|EMBL:AIL59707.1}; OS Pseudomonas alkylphenolica. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL59707.1, ECO:0000313|Proteomes:UP000028931}; RN [1] {ECO:0000313|EMBL:AIL59707.1, ECO:0000313|Proteomes:UP000028931} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KL28 {ECO:0000313|EMBL:AIL59707.1, RC ECO:0000313|Proteomes:UP000028931}; RA Lee K., Lim J.Y., Hwang I.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the oxidation of protoporphyrinogen IX to CC protoporphyrin IX. {ECO:0000256|HAMAP-Rule:MF_02239, CC ECO:0000256|PIRNR:PIRNR004638}. 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:0000256|ARBA:ARBA00001093, ECO:0000256|HAMAP- CC Rule:MF_02239, ECO:0000256|PIRNR:PIRNR004638}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02239, CC ECO:0000256|PIRNR:PIRNR004638}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. CC {ECO:0000256|HAMAP-Rule:MF_02239, ECO:0000256|PIRNR:PIRNR004638}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1. CC {ECO:0000256|ARBA:ARBA00005073, ECO:0000256|HAMAP-Rule:MF_02239, CC ECO:0000256|PIRNR:PIRNR004638}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02239}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651, CC ECO:0000256|HAMAP-Rule:MF_02239}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|HAMAP-Rule:MF_02239}. CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the HemJ family. {ECO:0000256|ARBA:ARBA00006501, CC ECO:0000256|HAMAP-Rule:MF_02239, ECO:0000256|PIRNR:PIRNR004638}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP009048; AIL59707.1; -; Genomic_DNA. DR RefSeq; WP_038606118.1; NZ_CP009048.1. DR EnsemblBacteria; AIL59707; AIL59707; PSAKL28_04710. DR KEGG; palk:PSAKL28_04710; -. DR eggNOG; COG1981; Bacteria. DR HOGENOM; CLU_125006_0_1_6; -. DR OrthoDB; 1433260at2; -. DR UniPathway; UPA00251; UER00324. DR Proteomes; UP000028931; 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 {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_02239}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_02239}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02239}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02239}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_02239}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_02239}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_02239}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_02239}. FT TRANSMEM 6..29 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT TRANSMEM 50..70 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT TRANSMEM 76..95 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT TRANSMEM 116..138 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT METAL 10 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT METAL 85 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" SQ SEQUENCE 141 AA; 16448 MW; 886D5D8C81E2EB28 CRC64; MLFLWIKALH IVSVVCWFAG LFYLPRLFVY HAQSQDSTSQ ERFVTMERKL YRGIMLPSMI ATLVFGIWLM SLTPSFLSQG WMHAKLTLVI LLIGYHHMCG AQLKRFARGE NTRSHVFYRW FNEVPVLILL AVVILVVVKP F //