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Database: UniProt
Entry: B4JEJ4_DROGR
LinkDB: B4JEJ4_DROGR
Original site: B4JEJ4_DROGR 
ID   B4JEJ4_DROGR            Unreviewed;       480 AA.
AC   B4JEJ4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Protoporphyrinogen oxidase {ECO:0000256|ARBA:ARBA00012867, ECO:0000256|RuleBase:RU367069};
DE            EC=1.3.3.4 {ECO:0000256|ARBA:ARBA00012867, ECO:0000256|RuleBase:RU367069};
GN   Name=Dgri\GH19131 {ECO:0000313|EMBL:EDV93125.1};
GN   ORFNames=Dgri_GH19131 {ECO:0000313|EMBL:EDV93125.1};
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070};
RN   [1] {ECO:0000313|EMBL:EDV93125.1, ECO:0000313|Proteomes:UP000001070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC       to form protoporphyrin-IX. {ECO:0000256|ARBA:ARBA00002600,
CC       ECO:0000256|RuleBase:RU367069}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX;
CC         Xref=Rhea:RHEA:25576, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.3.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000672,
CC         ECO:0000256|RuleBase:RU367069};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU367069};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU367069};
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|RuleBase:RU367069}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU367069}.
CC   -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC       oxidase family. Protoporphyrinogen oxidase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010551, ECO:0000256|RuleBase:RU367069}.
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DR   EMBL; CH916369; EDV93125.1; -; Genomic_DNA.
DR   RefSeq; XP_001990063.1; XM_001990027.1.
DR   AlphaFoldDB; B4JEJ4; -.
DR   SMR; B4JEJ4; -.
DR   STRING; 7222.B4JEJ4; -.
DR   EnsemblMetazoa; FBtr0154545; FBpp0153037; FBgn0126598.
DR   GeneID; 6563279; -.
DR   KEGG; dgr:6563279; -.
DR   eggNOG; KOG1276; Eukaryota.
DR   HOGENOM; CLU_009629_2_1_1; -.
DR   InParanoid; B4JEJ4; -.
DR   OMA; WFDQWFG; -.
DR   OrthoDB; 65450at2759; -.
DR   PhylomeDB; B4JEJ4; -.
DR   UniPathway; UPA00251; UER00324.
DR   Proteomes; UP000001070; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR   NCBIfam; TIGR00562; proto_IX_ox; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   PANTHER; PTHR42923:SF3; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU367069};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU367069};
KW   Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133,
KW   ECO:0000256|RuleBase:RU367069};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU367069};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW   ECO:0000256|RuleBase:RU367069};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001070}.
FT   DOMAIN          11..472
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   480 AA;  53875 MW;  99FAB5D06D738E5B CRC64;
     MTTTAVLGGG ISGLSAGYYL LRRFGKPLTI YEASPRVGGW IRTEWHKERG FIFETGPRTI
     RPKGVAGANT LELVEQLKLP VKPIRSSHVA ARNRMLYAKG QVCMLPNSPK GLIATVPPFT
     KPLYRALLHD LTTGGTVAKN EDESIYSFAE RRFGKEIADY AISPMICGIC AGDAREISVR
     FLMDSLFEKE QKYGGVIKGV LYSRLNKNED KDKDVDRPID EPSNLYKQAV QEKWAMYSLT
     DGLEQLPRAL RKYLGEHDVN VQLSSRCNNL SFSSDGARLG LRNAELPVSH VVSSLPAYQL
     APLVRQQHPS LCAQLLEIPY VDVVVVNLQY NSDQLLKQNG FGLLVPPVEN LPVLGVIFDS
     CCFDMAGNTI LTVMMGGKWF EQWFGHQPSQ KELRDTAQQH VRKILNIKEE PTFSRVHLLH
     KCIPQYTVGH KRRVQQIRDY IRNYKLPLSL CGAAYDGVGI NDVILSARRQ VELLPMPQTH
//
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