ID A0A060NIN9_9BURK Unreviewed; 157 AA. AC A0A060NIN9; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 29-SEP-2021, entry version 22. 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=SRAA_2127 {ECO:0000313|EMBL:BAO81981.1}; OS Serpentinomonas raichei. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Serpentinomonas. OX NCBI_TaxID=1458425 {ECO:0000313|EMBL:BAO81981.1, ECO:0000313|Proteomes:UP000067461}; RN [1] {ECO:0000313|EMBL:BAO81981.1, ECO:0000313|Proteomes:UP000067461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A1 {ECO:0000313|EMBL:BAO81981.1, RC ECO:0000313|Proteomes:UP000067461}; RX PubMed=24845058; DOI=10.1038/ncomms4900; RA Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A., RA Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G., RA Nealson K.H.; RT "Physiological and genomic features of highly alkaliphilic hydrogen- RT utilizing Betaproteobacteria from a continental serpentinizing site."; RL Nat. Commun. 5:3900-3900(2014). 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; AP014568; BAO81981.1; -; Genomic_DNA. DR EnsemblBacteria; BAO81981; BAO81981; SRAA_2127. DR KEGG; cbaa:SRAA_2127; -. DR HOGENOM; CLU_125006_2_0_4; -. DR UniPathway; UPA00251; UER00324. DR Proteomes; UP000067461; 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. 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:UP000067461}; 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 23..44 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT TRANSMEM 65..85 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT TRANSMEM 97..120 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT TRANSMEM 132..154 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT METAL 23 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" FT METAL 101 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02239" SQ SEQUENCE 157 AA; 17778 MW; BECCF4E3448F77A0 CRC64; MLLILSLAAP GYTSRMLWVK AFHIIFVASW FAGLFYLPRI YVNLALVPPG SEAERARLLL MARKLLRFMT LLAVPALGLG LWLWIGYGIG WGPGNGWMHA KLLVVVLLLA YHGHCAALLR DFELGRNRRS HVWYRWFNEA PVLLLVAAVL LVVLKPF //