PAO_ARATH
ID PAO_ARATH Reviewed; 537 AA.
AC Q9FYC2; O04422;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Pheophorbide a oxygenase, chloroplastic;
DE Short=AtPaO;
DE Short=Pheide a oxygenase;
DE EC=1.14.15.17 {ECO:0000269|PubMed:14657372};
DE AltName: Full=Accelerated cell death 1;
DE AltName: Full=Lethal leaf-spot 1 homolog;
DE Short=Lls1;
DE Flags: Precursor;
GN Name=PAO; Synonyms=ACD1; OrderedLocusNames=At3g44880; ORFNames=F28D10_70;
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].
RC STRAIN=cv. Columbia;
RX PubMed=9094711; DOI=10.1016/s0092-8674(00)80179-8;
RA Gray J., Close P.S., Briggs S.P., Johal G.S.;
RT "A novel suppressor of cell death in plants encoded by the Lls1 gene of
RT maize.";
RL Cell 89:25-31(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12481072; DOI=10.1104/pp.008441;
RA Gray J., Janick-Buckner D., Buckner B., Close P.S., Johal G.S.;
RT "Light-dependent death of maize lls1 cells is mediated by mature
RT chloroplasts.";
RL Plant Physiol. 130:1894-1907(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=15159621; DOI=10.1023/b:plan.0000028789.51807.6a;
RA Yang M., Wardzala E., Johal G.S., Gray J.;
RT "The wound-inducible Lls1 gene from maize is an orthologue of the
RT Arabidopsis Acd1 gene, and the LLS1 protein is present in non-
RT photosynthetic tissues.";
RL Plant Mol. Biol. 54:175-191(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [5]
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CHARACTERIZATION.
RX PubMed=14657372; DOI=10.1073/pnas.2036571100;
RA Pruzinska A., Tanner G., Anders I., Roca M., Hortensteiner S.;
RT "Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-
RT sulfur protein, encoded by the accelerated cell death 1 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15259-15264(2003).
RN [8]
RP FUNCTION.
RX PubMed=14701922; DOI=10.1093/pcp/pcg172;
RA Tanaka R., Hirashima M., Satoh S., Tanaka A.;
RT "The Arabidopsis-accelerated cell death gene ACD1 is involved in
RT oxygenation of pheophorbide a: inhibition of the pheophorbide a oxygenase
RT activity does not lead to the 'Stay-Green' phenotype in Arabidopsis.";
RL Plant Cell Physiol. 44:1266-1274(2003).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SGR1; RCCR; PPH AND LHCII
RP 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 [10]
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: Catalyzes the key reaction of chlorophyll catabolism,
CC porphyrin macrocycle cleavage of pheophorbide a (pheide a) to a primary
CC fluorescent catabolite (pFCC). Works in a two-step reaction with red
CC chlorophyll catabolite reductase (RCCR). Creates the intermediate RCC
CC through the opening of the porphyrin macrocycle by the introduction of
CC one atom of molecular oxygen at the alpha-methine bridge. Seems to be
CC specific for pheide a. Belongs to the chlorophyll catabolic enzymes
CC (CCEs). {ECO:0000269|PubMed:14657372, ECO:0000269|PubMed:14701922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + O2 + pheophorbide a + 2 reduced [2Fe-2S]-[ferredoxin]
CC = 2 oxidized [2Fe-2S]-[ferredoxin] + red chlorophyll catabolite;
CC Xref=Rhea:RHEA:48140, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:58687, ChEBI:CHEBI:58716;
CC EC=1.14.15.17; Evidence={ECO:0000269|PubMed:14657372};
CC -!- ACTIVITY REGULATION: Might be regulated by a
CC phosphorylation/dephosphorylation mechanism.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 mM for pheophorbide a {ECO:0000269|PubMed:14657372};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC degradation.
CC -!- SUBUNIT: Interacts with HCAR, SGR1, RCCR, PPH and the LHCII complex.
CC Part of 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
CC {ECO:0000269|PubMed:22366162}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during senescence.
CC {ECO:0000269|PubMed:23200839}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49679.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U77347; AAC49679.1; ALT_FRAME; mRNA.
DR EMBL; AY344061; AAR05797.1; -; mRNA.
DR EMBL; AL391254; CAC03538.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77964.1; -; Genomic_DNA.
DR EMBL; AY093092; AAM13091.1; -; mRNA.
DR PIR; T51785; T51785.
DR RefSeq; NP_190074.1; NM_114357.6.
DR AlphaFoldDB; Q9FYC2; -.
DR SMR; Q9FYC2; -.
DR BioGRID; 8942; 6.
DR IntAct; Q9FYC2; 2.
DR MINT; Q9FYC2; -.
DR STRING; 3702.AT3G44880.1; -.
DR SwissPalm; Q9FYC2; -.
DR PaxDb; Q9FYC2; -.
DR PRIDE; Q9FYC2; -.
DR ProteomicsDB; 236837; -.
DR EnsemblPlants; AT3G44880.1; AT3G44880.1; AT3G44880.
DR GeneID; 823622; -.
DR Gramene; AT3G44880.1; AT3G44880.1; AT3G44880.
DR KEGG; ath:AT3G44880; -.
DR Araport; AT3G44880; -.
DR TAIR; locus:2082122; AT3G44880.
DR eggNOG; ENOG502QQ8U; Eukaryota.
DR HOGENOM; CLU_003927_1_0_1; -.
DR InParanoid; Q9FYC2; -.
DR OMA; MWHDLTS; -.
DR OrthoDB; 1199207at2759; -.
DR PhylomeDB; Q9FYC2; -.
DR BioCyc; ARA:AT3G44880-MON; -.
DR BioCyc; MetaCyc:AT3G44880-MON; -.
DR BRENDA; 1.14.15.17; 399.
DR UniPathway; UPA00674; -.
DR PRO; PR:Q9FYC2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FYC2; baseline and differential.
DR Genevisible; Q9FYC2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; TAS:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010277; F:chlorophyllide a oxygenase [overall] activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0032441; F:pheophorbide a oxygenase activity; IDA:TAIR.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0015996; P:chlorophyll catabolic process; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR013626; PaO.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF08417; PaO; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Chlorophyll catabolism; Chloroplast; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Oxidoreductase; Plastid; Reference proteome; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 50..537
FT /note="Pheophorbide a oxygenase, chloroplastic"
FT /id="PRO_0000021999"
FT DOMAIN 88..200
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 51..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 132
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 150
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 153
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT CONFLICT 98
FT /note="D -> V (in Ref. 1; AAC49679 and 3; AAR05797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 60756 MW; 61C86A08A00D8940 CRC64;
MSVVLLSSTS ATITKSQSKK IPFLSPTTKF PLKVSISPSR SKLFHNPLRV AAPPSVPTSD
STEEKRIEEE YGGDKEEEGS EFKWRDHWYP VSLVEDLDPN VPTPFQLLGR DLVLWFDRND
QKWAAFDDLC PHRLAPLSEG RLDENGHLQC SYHGWSFGGC GSCTRIPQAA TSGPEARAVK
SPRACAIKFP TMVSQGLLFV WPDENGWDRA NSIEPPRLPD DFDKPEFSTV TIQRDLFYGY
DTLMENVSDP SHIDFAHHKV TGRRDRAKPL PFKVESSGPW GFQGANDDSP RITAKFVAPC
YSMNKIELDA KLPIVGNQKW VIWICSFNIP MAPGKTRSIV CSARNFFQFS VPGPAWWQVV
PRWYEHWTSN LVYDGDMIVL QGQEKVFLAK SMESPDYDVN KQYTKLTFTP TQADRFVLAF
RNWLRRHGKS QPEWFGSTPS NQPLPSTVLT KRQMLDRFDQ HTQVCSSCKG AYNSFQILKK
FLVGATVFWA ATAGVPSDVQ IRLVLAGLSL ISAASAYALH EQEKNFVFRD YVHSEIE
