PPH_ARATH
ID PPH_ARATH Reviewed; 484 AA.
AC Q9FFZ1;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Pheophytinase, chloroplastic;
DE EC=3.1.1.-;
DE AltName: Full=Pheophytin pheophorbide hydrolase;
DE AltName: Full=Protein CO-REGULATED WITH NYE1;
DE Flags: Precursor;
GN Name=PPH; Synonyms=CRN1; OrderedLocusNames=At5g13800; ORFNames=MAC12.25;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBSTRATE SPECIFICITY, MUTAGENESIS OF
RP SER-221, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19304936; DOI=10.1105/tpc.108.064089;
RA Schelbert S., Aubry S., Burla B., Agne B., Kessler F., Krupinska K.,
RA Hortensteiner S.;
RT "Pheophytin pheophorbide hydrolase (pheophytinase) is involved in
RT chlorophyll breakdown during leaf senescence in Arabidopsis.";
RL Plant Cell 21:767-785(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20537045; DOI=10.1111/j.1744-7909.2010.00945.x;
RA Ren G., Zhou Q., Wu S., Zhang Y., Zhang L., Huang J., Sun Z., Kuai B.;
RT "Reverse genetic identification of CRN1 and its distinctive role in
RT chlorophyll degradation in Arabidopsis.";
RL J. Integr. Plant Biol. 52:496-504(2010).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RCCR; PAO AND LHCII COMPLEX.
RX PubMed=22366162; DOI=10.1105/tpc.111.089474;
RA Sakuraba Y., Schelbert S., Park S.Y., Han S.H., Lee B.D., Andres C.B.,
RA Kessler F., Hortensteiner S., Paek N.C.;
RT "STAY-GREEN and chlorophyll catabolic enzymes interact at light-harvesting
RT complex II for chlorophyll detoxification during leaf senescence in
RT Arabidopsis.";
RL Plant Cell 24:507-518(2012).
RN [8]
RP INTERACTION WITH HCAR, AND DEVELOPMENTAL STAGE.
RX PubMed=23200839; DOI=10.1016/j.bbrc.2012.11.050;
RA Sakuraba Y., Kim Y.S., Yoo S.C., Hortensteiner S., Paek N.C.;
RT "7-Hydroxymethyl chlorophyll a reductase functions in metabolic channeling
RT of chlorophyll breakdown intermediates during leaf senescence.";
RL Biochem. Biophys. Res. Commun. 430:32-37(2013).
CC -!- FUNCTION: Alpha/beta hydrolase dephytylating specifically the Mg-free
CC chlorophyll pigment (pheophytin), yielding pheophorbide. No activity on
CC chlorophyll. Belongs to the chlorophyll catabolic enzymes (CCEs).
CC {ECO:0000269|PubMed:19304936, ECO:0000269|PubMed:20537045}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 25-30 degrees Celsius.
CC {ECO:0000269|PubMed:19304936};
CC -!- SUBUNIT: Interacts with HCAR, RCCR, PAO and the LHCII complex. Part of
CC a SGR1-CCE-LHCII complex, which acts in chlorophyll breakdown.
CC {ECO:0000269|PubMed:22366162, ECO:0000269|PubMed:23200839}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane. Plastid,
CC chloroplast stroma.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during senescence.
CC {ECO:0000269|PubMed:23200839}.
CC -!- DISRUPTION PHENOTYPE: Stay-green phenotype during leaf senescence.
CC Delayed chlorophyll breakdown during developmental senescence.
CC {ECO:0000269|PubMed:19304936, ECO:0000269|PubMed:20537045}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; AB005230; BAB11108.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91942.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91943.1; -; Genomic_DNA.
DR EMBL; AY056386; AAL08242.1; -; mRNA.
DR EMBL; AY070736; AAL50077.1; -; mRNA.
DR EMBL; AY149934; AAN31088.1; -; mRNA.
DR EMBL; AK317089; BAH19780.1; -; mRNA.
DR RefSeq; NP_196884.1; NM_121383.4.
DR RefSeq; NP_850815.1; NM_180484.3.
DR AlphaFoldDB; Q9FFZ1; -.
DR BioGRID; 16503; 6.
DR STRING; 3702.AT5G13800.1; -.
DR ESTHER; arath-Q9FFZ1; Pheophytinase.
DR MEROPS; S33.A34; -.
DR iPTMnet; Q9FFZ1; -.
DR PaxDb; Q9FFZ1; -.
DR ProteomicsDB; 249344; -.
DR EnsemblPlants; AT5G13800.1; AT5G13800.1; AT5G13800.
DR EnsemblPlants; AT5G13800.2; AT5G13800.2; AT5G13800.
DR GeneID; 831225; -.
DR Gramene; AT5G13800.1; AT5G13800.1; AT5G13800.
DR Gramene; AT5G13800.2; AT5G13800.2; AT5G13800.
DR KEGG; ath:AT5G13800; -.
DR Araport; AT5G13800; -.
DR TAIR; locus:2159033; AT5G13800.
DR eggNOG; KOG1454; Eukaryota.
DR HOGENOM; CLU_020336_21_0_1; -.
DR InParanoid; Q9FFZ1; -.
DR PhylomeDB; Q9FFZ1; -.
DR BioCyc; ARA:AT5G13800-MON; -.
DR BioCyc; MetaCyc:AT5G13800-MON; -.
DR PRO; PR:Q9FFZ1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFZ1; baseline and differential.
DR Genevisible; Q9FFZ1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0080124; F:pheophytinase activity; IDA:TAIR.
DR GO; GO:0015996; P:chlorophyll catabolic process; IMP:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR044211; PPH_chloroplastic.
DR PANTHER; PTHR47280; PTHR47280; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Chlorophyll catabolism; Chloroplast; Hydrolase; Membrane; Plastid;
KW Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 48..484
FT /note="Pheophytinase, chloroplastic"
FT /id="PRO_0000425230"
FT MUTAGEN 221
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19304936"
SQ SEQUENCE 484 AA; 54572 MW; 816939E0AFFAA12F CRC64;
MEIISLNVVP QCSVVTWSSK LATKRLVPNR SSLLFSGVKK SRLVIRSGNS DGYVVGENDD
LGRIARRGES TSKVLIPGLP DESNGEIAAR ISHSHCEWKP KLRVHYEKAG CDNLDAPAVL
FLPGFGVGSF HYEKQLTDLG RDYRVWAIDF LGQGLSLPTE DPTTMTEETS SSEDKEPFWG
FGDKTEPWAD QLVFSLDLWR DQVQYFVEEV IGEPVYIAGN SLGGYVALYF AATHPHLVKG
VTLLNATPFW GFFPNPVRSP KLARLFPWPG AFPLPERVKK ITELVWQKIS DPESIAEILK
QVYTDHSINV DKVFSRIVEV TQHPAAAASF ASIMLAPGGE LSFSEALSRC KENNVQICLM
YGREDPWVRP LWGKKIKKEI PNAPYYEISP AGHCPHDEVP EVVNYLMRGW IKHLESGGFE
ALPLLEDTEE DWEESRIGRE IEFPRDGWKK AVNLWLYGSN YTYWRGVRES FRSSFIRVFG
GKSA
