PPOCM_ARATH
ID PPOCM_ARATH Reviewed; 508 AA.
AC Q8S9J1; F4K5H8; Q9FMS9; Q9LYA7;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protoporphyrinogen oxidase 2, chloroplastic/mitochondrial;
DE Short=PPO2;
DE EC=1.3.3.4;
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 61;
DE Flags: Precursor;
GN Name=PPOX2; Synonyms=HEMG2, MEE61, PPO2; OrderedLocusNames=At5g14220;
GN ORFNames=F18O22.10, MUA22.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=21841088; DOI=10.1104/pp.111.182352;
RA Klodmann J., Senkler M., Rode C., Braun H.-P.;
RT "Defining the protein complex proteome of plant mitochondria.";
RL Plant Physiol. 157:587-598(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Mitochondrion
CC {ECO:0000269|PubMed:21841088}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S9J1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S9J1-2; Sequence=VSP_046550;
CC -!- DISRUPTION PHENOTYPE: Embryo development arrested at one-cell zygotic
CC stage. {ECO:0000269|PubMed:15634699}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08301.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB87761.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB007650; BAB08301.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL163817; CAB87761.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92001.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92002.1; -; Genomic_DNA.
DR EMBL; AY075665; AAL77672.1; -; mRNA.
DR EMBL; AY101523; AAM26644.1; -; mRNA.
DR PIR; T48595; T48595.
DR RefSeq; NP_001190307.1; NM_001203378.1. [Q8S9J1-2]
DR RefSeq; NP_196926.2; NM_121426.5. [Q8S9J1-1]
DR AlphaFoldDB; Q8S9J1; -.
DR SMR; Q8S9J1; -.
DR STRING; 3702.AT5G14220.1; -.
DR iPTMnet; Q8S9J1; -.
DR PaxDb; Q8S9J1; -.
DR PRIDE; Q8S9J1; -.
DR ProMEX; Q8S9J1; -.
DR ProteomicsDB; 234866; -. [Q8S9J1-1]
DR DNASU; 831272; -.
DR EnsemblPlants; AT5G14220.1; AT5G14220.1; AT5G14220. [Q8S9J1-1]
DR EnsemblPlants; AT5G14220.2; AT5G14220.2; AT5G14220. [Q8S9J1-2]
DR GeneID; 831272; -.
DR Gramene; AT5G14220.1; AT5G14220.1; AT5G14220. [Q8S9J1-1]
DR Gramene; AT5G14220.2; AT5G14220.2; AT5G14220. [Q8S9J1-2]
DR KEGG; ath:AT5G14220; -.
DR Araport; AT5G14220; -.
DR TAIR; locus:2145603; AT5G14220.
DR eggNOG; KOG1276; Eukaryota.
DR InParanoid; Q8S9J1; -.
DR PhylomeDB; Q8S9J1; -.
DR UniPathway; UPA00251; UER00324.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q8S9J1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8S9J1; baseline and differential.
DR Genevisible; Q8S9J1; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00562; proto_IX_ox; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chlorophyll biosynthesis; Chloroplast; FAD;
KW Flavoprotein; Heme biosynthesis; Mitochondrion; Oxidoreductase; Plastid;
KW Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..508
FT /note="Protoporphyrinogen oxidase 2,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000422669"
FT REGION 219..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 23..28
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 46..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 68..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 475..477
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT VAR_SEQ 112..141
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046550"
SQ SEQUENCE 508 AA; 55630 MW; F092957F1F3DD268 CRC64;
MASGAVADHQ IEAVSGKRVA VVGAGVSGLA AAYKLKSRGL NVTVFEADGR VGGKLRSVMQ
NGLIWDEGAN TMTEAEPEVG SLLDDLGLRE KQQFPISQKK RYIVRNGVPV MLPTNPIELV
TSSVLSTQSK FQILLEPFLW KKKSSKVSDA SAEESVSEFF QRHFGQEVVD YLIDPFVGGT
SAADPDSLSM KHSFPDLWNV EKSFGSIIVG AIRTKFAAKG GKSRDTKSSP GTKKGSRGSF
SFKGGMQILP DTLCKSLSHD EINLDSKVLS LSYNSGSRQE NWSLSCVSHN ETQRQNPHYD
AVIMTAPLCN VKEMKVMKGG QPFQLNFLPE INYMPLSVLI TTFTKEKVKR PLEGFGVLIP
SKEQKHGFKT LGTLFSSMMF PDRSPSDVHL YTTFIGGSRN QELAKASTDE LKQVVTSDLQ
RLLGVEGEPV SVNHYYWRKA FPLYDSSYDS VMEAIDKMEN DLPGFFYAGN HRGGLSVGKS
IASGCKAADL VISYLESCSN DKKPNDSL
