ID D7UBE4_VITVI Unreviewed; 508 AA.
AC D7UBE4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
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 OrderedLocusNames=VIT_14s0171g00190 {ECO:0000313|EMBL:CBI40059.3};
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:CBI40059.3, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(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; FN596749; CBI40059.3; -; Genomic_DNA.
DR RefSeq; XP_002263321.1; XM_002263285.3.
DR AlphaFoldDB; D7UBE4; -.
DR STRING; 29760.D7UBE4; -.
DR PaxDb; 29760-VIT_14s0171g00190-t01; -.
DR EnsemblPlants; Vitvi14g01579_t001; Vitvi14g01579_P001; Vitvi14g01579.
DR GeneID; 100254398; -.
DR Gramene; Vitvi14g01579_t001; Vitvi14g01579_P001; Vitvi14g01579.
DR KEGG; vvi:100254398; -.
DR eggNOG; KOG1276; Eukaryota.
DR HOGENOM; CLU_009629_3_2_1; -.
DR InParanoid; D7UBE4; -.
DR OMA; EHNQAVQ; -.
DR OrthoDB; 65450at2759; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000009183; Chromosome 14.
DR ExpressionAtlas; D7UBE4; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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; PROTOPORPHYRINOGEN OXIDASE; 1.
DR PANTHER; PTHR42923:SF45; PROTOPORPHYRINOGEN OXIDASE 2, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00419; ADXRDTASE.
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:UP000009183}.
FT DOMAIN 25..494
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 219..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 56134 MW; CC33901762D37400 CRC64;
MAEKSDAQSH YNGSGKRVAV VGAGVSGLAA AYKLKLHGVN ITLYEAEERA GGKLRSVSQH
GLVWDEGANT MTESEIEVGS LLDNLRLREK QQFPISQNKR YIVRNGMPVL LPSNPIALIK
SNILSAKSKF QIILEPFLWK KSDLSKVSDD HMKESVGGFF QRHFGKEVVD YLIDPFVAGT
SGGDPESLSM HHTFPELWNL EKRFGSIIAG AVLSKLSAKR EKRGETKGSS EKKKRQRGSF
SFQGGMQTLT DTLCKELGKD KLRLKSKVLS LSYSHGEKSA LENWSVAYAS NPGKQSKDLS
FDAVIMTAPL CNVREMKIMK KGNPFLLDFL PEVSYLPLSV IITTFKKENV KRPLEGFGVL
VPSKEQQNGL KTLGTLFSSM MFPDRAPNDL YLYTTFIGGS RNRELAKAST DELKQIVTSD
LRQLLGAEGE PTFVNHFYWS KAFPLFGHNY DSVLEAIDKM EKDLPGFFYA GNHKGGLSVG
KAIASGCKAA DLVISYLNSS SDGKMFKE
//
