ID A0A0S3EVR3_9SPHN Unreviewed; 146 AA. AC A0A0S3EVR3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 03-MAY-2023, entry version 23. 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=ATN00_03620 {ECO:0000313|EMBL:ALR19532.1}; OS Sphingobium baderi. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR19532.1, ECO:0000313|Proteomes:UP000056968}; RN [1] {ECO:0000313|EMBL:ALR19532.1, ECO:0000313|Proteomes:UP000056968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR19532.1, RC ECO:0000313|Proteomes:UP000056968}; RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.; RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for RT para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in RT Sphingobium baderi DE-13."; RL Submitted (NOV-2015) 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; CP013264; ALR19532.1; -; Genomic_DNA. DR RefSeq; WP_062062262.1; NZ_CP013264.1. DR AlphaFoldDB; A0A0S3EVR3; -. DR STRING; 1332080.ATN00_03620; -. DR EnsemblBacteria; ALR19532; ALR19532; ATN00_03620. DR KEGG; sbd:ATN00_03620; -. DR OrthoDB; 9800824at2; -. DR UniPathway; UPA00251; UER00324. DR Proteomes; UP000056968; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070818; F:protoporphyrinogen oxidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_02239; HemJ; 1. DR InterPro; IPR005265; HemJ-like. DR PANTHER; PTHR40255:SF1; PROTOPORPHYRINOGEN IX OXIDASE; 1. DR PANTHER; PTHR40255; UPF0093 MEMBRANE PROTEIN SLR1790; 1. DR Pfam; PF03653; UPF0093; 1. DR PIRSF; PIRSF004638; UCP004638; 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}; Reference proteome {ECO:0000313|Proteomes:UP000056968}; 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..28 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT TRANSMEM 56..77 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT TRANSMEM 83..104 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT TRANSMEM 125..143 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" 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:0000256|HAMAP-Rule:MF_02239" FT BINDING 90 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:0000256|HAMAP-Rule:MF_02239" SQ SEQUENCE 146 AA; 16786 MW; 2F0E6BB10C2733CA CRC64; MAYLGAAYLW VKAAHLIFVI FLMAGLFMMP RFFVYHQQCA VGSDEDHKWI DRERRLLKII LNPSLLLVWI FGLMLMVEIG AWHFGWFHLK LLFVLGLSGY HGWIAGYAKK LARGERPMTD KRLRLMNEIP GVAAAVIVIA VIVKPF //