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}.
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; 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
//