ID B4F9N9_MAIZE Unreviewed; 544 AA.
AC B4F9N9; A0A3L6G044;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, 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=541866 {ECO:0000313|EnsemblPlants:Zm00001eb078900_P004};
GN ORFNames=ZEAMMB73_Zm00001d003214 {ECO:0000313|EMBL:ONM16434.1},
GN Zm00014a_029343 {ECO:0000313|EMBL:PWZ38740.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF78832.1};
RN [1] {ECO:0000313|EMBL:ACF78832.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACF78832.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [2] {ECO:0000313|EMBL:ONM16434.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb078900_P004,
RC ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM16434.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PWZ38740.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:PWZ38740.1};
RX PubMed=30061735; DOI=10.1038/s41588-018-0182-0;
RA Sun S., Zhou Y., Chen J., Shi J., Zhao H., Zhao H., Song W., Zhang M.,
RA Cui Y., Dong X., Liu H., Ma X., Jiao Y., Wang B., Wei X., Stein J.C.,
RA Glaubitz J.C., Lu F., Yu G., Liang C., Fengler K., Li B., Rafalski A.,
RA Schnable P.S., Ware D.H., Buckler E.S., Lai J.;
RT "Extensive intraspecific gene order and gene structural variations between
RT Mo17 and other maize genomes.";
RL Nat. Genet. 50:1289-1295(2018).
RN [4] {ECO:0000313|EnsemblPlants:Zm00001eb078900_P004}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb078900_P004};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
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; BT033827; ACF78832.1; -; mRNA.
DR EMBL; CM007648; ONM16434.1; -; Genomic_DNA.
DR EMBL; NCVQ01000003; PWZ38740.1; -; Genomic_DNA.
DR RefSeq; NP_001105004.2; NM_001111534.2.
DR AlphaFoldDB; B4F9N9; -.
DR SMR; B4F9N9; -.
DR PaxDb; 4577-GRMZM2G364901_P04; -.
DR EnsemblPlants; Zm00001eb078900_T004; Zm00001eb078900_P004; Zm00001eb078900.
DR GeneID; 541866; -.
DR Gramene; Zm00001eb078900_T004; Zm00001eb078900_P004; Zm00001eb078900.
DR eggNOG; KOG1276; Eukaryota.
DR HOGENOM; CLU_009629_3_2_1; -.
DR OMA; EHNQAVQ; -.
DR OrthoDB; 65450at2759; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000007305; Chromosome 2.
DR Proteomes; UP000251960; Chromosome 2.
DR ExpressionAtlas; B4F9N9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
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; PROTOPORPHYRINOGEN OXIDASE; 1.
DR PANTHER; PTHR42923:SF3; PROTOPORPHYRINOGEN OXIDASE; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:B4F9N9};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT DOMAIN 55..529
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 59047 MW; 101CFFB8E56A151B CRC64;
MLALTASASS ASSHPYRHAS AHTRRPRLRA VLAMAGSDDP RAAPARSVAV VGAGVSGLAA
AYRLRQSGVN VTVFEAADRA GGKIRTNSEG GFVWDEGANT MTEGEWEASR LIDDLGLQDK
QQYPNSQHKR YIVKDGAPAL IPSDPISLMK SSVLSTKSKI ALFFEPFLYK KANTRNSGKV
SEEHLSESVG SFCERHFGRE VVDYFVDPFV AGTSAGDPES LSIRHAFPAL WNLERKYGSV
IVGAILSKLA AKGDPVKTRH DSSGKRRNRR VSFSFHGGMQ SLINALHNEV GDDNVKLGTE
VLSLACTFDG VPALGRWSIS VDSKDSGDKD LASNQTFDAV IMTAPLSNVR RMKFTKGGAP
VVLDFLPKMD YLPLSLMVTA FKKDDVKKPL EGFGVLIPYK EQQKHGLKTL GTLFSSMMFP
DRAPDDQYLY TTFVGGSHNR DLAGAPTSIL KQLVTSDLKK LLGVEGQPTF VKHVYWGNAF
PLYGHDYSSV LEAIEKMEKN LPGFFYAGNN KDGLAVGSVI ASGSKAADLA ISYLESHTKH
NNSH
//