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Database: UniProt
Entry: Q9T0P9_CHLRE
LinkDB: Q9T0P9_CHLRE
Original site: Q9T0P9_CHLRE 
ID   Q9T0P9_CHLRE            Unreviewed;       563 AA.
AC   Q9T0P9;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 91.
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=Ppx1 {ECO:0000313|EMBL:AAC79630.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055 {ECO:0000313|EMBL:AAC79630.1};
RN   [1] {ECO:0000313|EMBL:AAC79630.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GB-2674 {ECO:0000313|EMBL:AAC79630.1};
RX   PubMed=9862501; DOI=10.1023/A:1006085026294;
RA   Randolph-Anderson B.L., Sato R., Johnson A.M., Harris E.H., Hauser C.R.,
RA   Oeda K., Ishige F., Nishio S., Gillham N.W., Boynton J.E.;
RT   "Isolation and characterization of a mutant protoporphyrinogen oxidase gene
RT   from Chlamydomonas reinhardtii conferring resistance to porphyric
RT   herbicides.";
RL   Plant Mol. Biol. 38:839-859(1998).
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: Plastid, chloroplast
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; AF030179; AAC79630.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9T0P9; -.
DR   UniPathway; UPA00251; UER00324.
DR   ExpressionAtlas; Q9T0P9; baseline.
DR   GO; GO:0009507; C:chloroplast; 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   Gene3D; 1.10.3110.10; protoporphyrinogen ix oxidase, domain 3; 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:SF40; LYSINE-SPECIFIC HISTONE DEMETHYLASE 2; 1.
DR   PANTHER; PTHR42923; 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}.
FT   DOMAIN          91..551
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  59834 MW;  074584EC935CA3AF CRC64;
     MMLTQTPGTA TASSRRSQIR SAAHVSAKVA PRPTPFSVAS PATAASPATA AARRTLHRTA
     AAATGAPTAS GAGVAKTLDN VYDVIVVGGG LSGLVTGQAL AAQHKIQNFL VTEARERVGG
     NITSMSGDGY VWEEGPNSFQ PNDSMLQIAV DSGCEKDLVF GDPTAPRFVW WEGKLRPVPS
     GLDAFTFDLM SIPGKIRAGL GAIGLINGAM PSFEESVEQF IRRNLGDEVF FRLIEPFCSG
     VYAGDPSKLS MKAAFNRIWI LEKNGGSLVG GAIKLFQERQ SNPAPPRDPR LPPKPKGQTV
     GSFRKGLKML PDAIERNIPD KIRVNWKLVS LGREADGRYG LVYDTPEGRV KVFARAVALT
     APSYVVADLV KEQAPAAAEA LGSFDYPPMG AVTLSYPLSA VREERKASDG SVPGFGQLHP
     RTQGITTLGT IYSSSLFPGR APEGHMLLLN YIGGTTNRGI VNQTTEQLVE QVDKDLRNMV
     IKPDAPKPRV VGVRVWPRAI PQFNLGHLEQ LDKARKALDA AGLQGVHLGG NYVSGVALGK
     VVEHGYESAA NLAKSVSKAA VKA
//
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