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Database: UniProt
Entry: A5AP89_VITVI
LinkDB: A5AP89_VITVI
Original site: A5AP89_VITVI 
ID   A5AP89_VITVI            Unreviewed;       549 AA.
AC   A5AP89;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 70.
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   ORFNames=VITISV_004031 {ECO:0000313|EMBL:CAN69262.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CAN69262.1};
RN   [1] {ECO:0000313|EMBL:CAN69262.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA   Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA   Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA   Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA   Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA   Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA   Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA   Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA   Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA   Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT   "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT   vinifera L.): coping with a highly heterozygous genome.";
RL   PLoS ONE 2:e1326-e1326(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: 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; AM431293; CAN69262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5AP89; -.
DR   UniPathway; UPA00251; UER00324.
DR   ExpressionAtlas; A5AP89; baseline and differential.
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          68..540
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          263..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  59075 MW;  534FD095C0D6F64D CRC64;
     MPTLTLADPP TLRLLSPVNL RRSTSISSPF FCRPVRCAVA GESTISSSKV GDGNNYSPVD
     CVIVGAGISG LCIAQALATK HGDVGSNVIV TEARDRVGGN ITTMEGDGYL WEEGPNSFQP
     SDSMLTMAVD SGLKDDLVLG DPNAPRFVLW NGKLRPVPSK PTDLPFFDLM SFPGKLRAGF
     GALGIRPPPP DHEESVEEFV RRNLGDEVFE RLIEPFCSRQ SDSLQPLCSV YAGDPSKLSM
     KAAFGKVWKL EQKGGSIIGG TFKAIQEKNN TPKPPRDPRL PKPKGQTVGS FKKGLIMLPE
     AISKRLGGKV KLSWKLSSII RLDDGGYSLT YETPEGLVSL QSRSVVMTVP SRVASSLLHP
     LSAVAADALS KFYYPPVAAV SISYPKEAIR TECLIEGELK GFGQLHPRSQ GVETLGTIYS
     SSLFPNRAPP GRILLLNYIG GATNPGILSK TESELVEAVD RDLRKMLINP NAKDPLVLGV
     RVWPQAIPQF LIGHLDLLDA AKSALRDGGF QGMFLGGNYV SGVALGRCVE GAYEVAAEVA
     DFLSQYVYK
//
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