PPOC_ARATH
ID PPOC_ARATH Reviewed; 537 AA.
AC P55826; F4JG44; Q5M730; Q94F25; Q9ZSI5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Protoporphyrinogen oxidase 1, chloroplastic;
DE Short=PPO1;
DE EC=1.3.3.4;
DE Flags: Precursor;
GN Name=PPOX1; Synonyms=HEMG1, PPOP1; OrderedLocusNames=At4g01690;
GN ORFNames=T15B16.13;
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 [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=8982084; DOI=10.1016/s0378-1119(96)00545-8;
RA Narita S., Tanaka R., Ito T., Okada K., Taketani S., Inokuchi H.;
RT "Molecular cloning and characterization of a cDNA that encodes
RT protoporphyrinogen oxidase of Arabidopsis thaliana.";
RL Gene 182:169-175(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-35, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER CYS-34, AND IDENTIFICATION BY MASS
RP 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:0000269|PubMed:8982084}.
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:0000269|PubMed:8982084};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by acifluorfen.
CC {ECO:0000269|PubMed:8982084}.
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 {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55826-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55826-2; Sequence=VSP_046547;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the leaves and at low
CC levels in the roots and floral buds.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72870.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D83139; BAA11820.1; -; mRNA.
DR EMBL; AF104919; AAC72870.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161492; CAB77739.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82064.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82065.1; -; Genomic_DNA.
DR EMBL; AF386944; AAK62389.1; -; mRNA.
DR EMBL; BT020418; AAV97809.1; -; mRNA.
DR EMBL; BT020535; AAW70381.1; -; mRNA.
DR PIR; G85021; G85021.
DR PIR; T02005; T02005.
DR RefSeq; NP_192078.1; NM_116399.4. [P55826-1]
DR RefSeq; NP_849283.1; NM_178952.2. [P55826-2]
DR AlphaFoldDB; P55826; -.
DR SMR; P55826; -.
DR BioGRID; 13282; 3.
DR STRING; 3702.AT4G01690.1; -.
DR ChEMBL; CHEMBL2366479; -.
DR iPTMnet; P55826; -.
DR PaxDb; P55826; -.
DR PRIDE; P55826; -.
DR ProteomicsDB; 236592; -. [P55826-1]
DR EnsemblPlants; AT4G01690.1; AT4G01690.1; AT4G01690. [P55826-1]
DR EnsemblPlants; AT4G01690.2; AT4G01690.2; AT4G01690. [P55826-2]
DR GeneID; 827991; -.
DR Gramene; AT4G01690.1; AT4G01690.1; AT4G01690. [P55826-1]
DR Gramene; AT4G01690.2; AT4G01690.2; AT4G01690. [P55826-2]
DR KEGG; ath:AT4G01690; -.
DR Araport; AT4G01690; -.
DR TAIR; locus:2133397; AT4G01690.
DR eggNOG; KOG1276; Eukaryota.
DR HOGENOM; CLU_009629_3_0_1; -.
DR InParanoid; P55826; -.
DR OMA; WFDQWFG; -.
DR PhylomeDB; P55826; -.
DR BioCyc; ARA:AT4G01690-MON; -.
DR BioCyc; MetaCyc:AT4G01690-MON; -.
DR BRENDA; 1.3.3.4; 399.
DR UniPathway; UPA00251; UER00324.
DR UniPathway; UPA00668; -.
DR PRO; PR:P55826; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P55826; baseline and differential.
DR Genevisible; P55826; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IBA:GO_Central.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; TAS: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 Acetylation; Alternative splicing; Chlorophyll biosynthesis; Chloroplast;
KW FAD; Flavoprotein; Heme biosynthesis; Oxidoreductase; Plastid;
KW Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 35..537
FT /note="Protoporphyrinogen oxidase 1, chloroplastic"
FT /id="PRO_0000013325"
FT REGION 256..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63..68
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 90..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 112..115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 511..513
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 447..477
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046547"
FT CONFLICT 302
FT /note="W -> C (in Ref. 4; AAK62389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 57695 MW; C125B0EE1D3187D5 CRC64;
MELSLLRPTT QSLLPSFSKP NLRLNVYKPL RLRCSVAGGP TVGSSKIEGG GGTTITTDCV
IVGGGISGLC IAQALATKHP DAAPNLIVTE AKDRVGGNII TREENGFLWE EGPNSFQPSD
PMLTMVVDSG LKDDLVLGDP TAPRFVLWNG KLRPVPSKLT DLPFFDLMSI GGKIRAGFGA
LGIRPSPPGR EESVEEFVRR NLGDEVFERL IEPFCSGVYA GDPSKLSMKA AFGKVWKLEQ
NGGSIIGGTF KAIQERKNAP KAERDPRLPK PQGQTVGSFR KGLRMLPEAI SARLGSKVKL
SWKLSGITKL ESGGYNLTYE TPDGLVSVQS KSVVMTVPSH VASGLLRPLS ESAANALSKL
YYPPVAAVSI SYPKEAIRTE CLIDGELKGF GQLHPRTQGV ETLGTIYSSS LFPNRAPPGR
ILLLNYIGGS TNTGILSKSE GELVEAVDRD LRKMLIKPNS TDPLKLGVRV WPQAIPQFLV
GHFDILDTAK SSLTSSGYEG LFLGGNYVAG VALGRCVEGA YETAIEVNNF MSRYAYK
