ID A0A0A6XYX3_9FLAO Unreviewed; 178 AA. AC A0A0A6XYX3; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-OCT-2020, entry version 27. DE RecName: Full=Protoporphyrinogen IX oxidase {ECO:0000256|ARBA:ARBA00017504, ECO:0000256|PIRNR:PIRNR004638}; DE EC=1.3.99.- {ECO:0000256|PIRNR:PIRNR004638}; GN ORFNames=HMPREF9074_08990 {ECO:0000313|EMBL:KHE68636.1}; OS Capnocytophaga sp. oral taxon 329 str. F0087. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga; unclassified Capnocytophaga. OX NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE68636.1, ECO:0000313|Proteomes:UP000030579}; RN [1] {ECO:0000313|EMBL:KHE68636.1, ECO:0000313|Proteomes:UP000030579} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0087 {ECO:0000313|EMBL:KHE68636.1, RC ECO:0000313|Proteomes:UP000030579}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L., RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C., RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A., RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W., RA Chinwalla A., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the oxidation of protoporphyrinogen IX to CC protoporphyrin IX. {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, CC ECO:0000256|PIRNR:PIRNR004638}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|PIRNR:PIRNR004638}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. CC {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|PIRNR:PIRNR004638}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane CC {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|PIRNR:PIRNR004638}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KHE68636.1}. 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; AFHP02000161; KHE68636.1; -; Genomic_DNA. DR RefSeq; WP_009389510.1; NZ_KN390028.1. DR STRING; 706436.HMPREF9074_08990; -. DR EnsemblBacteria; KHE68636; KHE68636; HMPREF9074_08990. DR eggNOG; COG1981; Bacteria. DR HOGENOM; CLU_125006_0_0_10; -. DR OrthoDB; 1433260at2; -. DR UniPathway; UPA00251; UER00324. DR Proteomes; UP000030579; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR005265; HemJ-like. DR PANTHER; PTHR40255; PTHR40255; 1. DR Pfam; PF03653; UPF0093; 1. DR PIRSF; PIRSF004638; UCP004638; 2. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, KW ECO:0000256|PIRNR:PIRNR004638}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR004638}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR004638}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR004638, KW ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR004638}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 12..30 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 57..78 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 84..105 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 126..146 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 152..172 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 178 AA; 21182 MW; 0326D9536DB29D23 CRC64; MDLFSITKAI HIIFVVSYFA GIFYMVRLFI YHTEALEKDE PERSILHRQF SFMEERLWNI ITVPALIIMS VTGIYMFYLM DWAYFLFGWM HVKLLFIGIL LWYHYYSWRI MKRLQAGQAT LTSLQLRMLN EVATLILFVV VFAVVLKALF TTYWYFALLA FVAMGALIML IVKLVNRK //