Q9FYC2 (PAO_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pheophorbide a oxygenase, chloroplastic
Short name=AtPaO
Short name=Pheide a oxygenase
EC=1.14.12.20

Alternative name(s):
Accelerated cell death 1
Lethal leaf-spot 1 homolog
Short name=Lls1

Gene names

Name:	PAO
Synonyms:	ACD1
Ordered Locus Names:	At3g44880
ORF Names:	F28D10_70

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the key reaction of chlorophyll catabolism, porphyrin macrocycle cleavage of pheophorbide a (pheide a) to a primary fluorescent catabolite (pFCC). Works in a two-step reaction with red chlorophyll catabolite reductase (RCCR). Creates the intermediate RCC through the opening of the porphyrin macrocycle by the introduction of one atom of molecular oxygen at the alpha-methine bridge. Seems to be specific for pheide a. Ref.8
Catalytic activity	Pheophorbide a + NADPH + O2 = red chlorophyll catabolite + NADP+.
Enzyme regulation	Might be regulated by a phosphorylation/dephosphorylation mechanism.
Pathway	Porphyrin degradation; chlorophyll degradation.
Subcellular location	Plastid › chloroplast inner membrane By similarity.
Developmental stage	Expressed during senescence.
Sequence similarities	Contains 1 Rieske domain.
Sequence caution	The sequence AAC49679.1 differs from that shown. Reason: Frameshift at positions 55 and 71.

Ontologies

Keywords
Biological process	Chlorophyll catabolism
Cellular component	Chloroplast Membrane Plastid Plastid inner membrane
Domain	Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell death Inferred from mutant phenotype. Source: TAIR chlorophyll catabolic process Inferred from mutant phenotype. Source: TAIR defense response to bacterium, incompatible interaction Inferred from mutant phenotype. Source: TAIR flower development Inferred from mutant phenotype. Source: TAIR fruit development Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast inner membrane Traceable author statement Ref.7. Source: TAIR chloroplast thylakoid Inferred from direct assay. Source: TAIR
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW chlorophyllide a oxygenase [overall] activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pheophorbide a oxygenase activity Inferred from direct assay Ref.7. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 49	49	Chloroplast Potential
	Chain	50 – 537	488	Pheophorbide a oxygenase, chloroplastic		PRO_0000021999
Regions
	Domain	88 – 200	113	Rieske
Sites
	Metal binding	130	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	132	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	150	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	153	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Experimental info
	Sequence conflict	98	1	D → V in AAC49679. Ref.1
	Sequence conflict	98	1	D → V in AAR05797. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9FYC2 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 61C86A08A00D8940	FASTA	537	60,756
	10 20 30 40 50 60 MSVVLLSSTS ATITKSQSKK IPFLSPTTKF PLKVSISPSR SKLFHNPLRV AAPPSVPTSD 70 80 90 100 110 120 STEEKRIEEE YGGDKEEEGS EFKWRDHWYP VSLVEDLDPN VPTPFQLLGR DLVLWFDRND 130 140 150 160 170 180 QKWAAFDDLC PHRLAPLSEG RLDENGHLQC SYHGWSFGGC GSCTRIPQAA TSGPEARAVK 190 200 210 220 230 240 SPRACAIKFP TMVSQGLLFV WPDENGWDRA NSIEPPRLPD DFDKPEFSTV TIQRDLFYGY 250 260 270 280 290 300 DTLMENVSDP SHIDFAHHKV TGRRDRAKPL PFKVESSGPW GFQGANDDSP RITAKFVAPC 310 320 330 340 350 360 YSMNKIELDA KLPIVGNQKW VIWICSFNIP MAPGKTRSIV CSARNFFQFS VPGPAWWQVV 370 380 390 400 410 420 PRWYEHWTSN LVYDGDMIVL QGQEKVFLAK SMESPDYDVN KQYTKLTFTP TQADRFVLAF 430 440 450 460 470 480 RNWLRRHGKS QPEWFGSTPS NQPLPSTVLT KRQMLDRFDQ HTQVCSSCKG AYNSFQILKK 490 500 510 520 530 FLVGATVFWA ATAGVPSDVQ IRLVLAGLSL ISAASAYALH EQEKNFVFRD YVHSEIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel suppressor of cell death in plants encoded by the Lls1 gene of maize." Gray J., Close P.S., Briggs S.P., Johal G.S. Cell 89:25-31(1997) [PubMed: 9094711] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Light-dependent death of maize lls1 cells is mediated by mature chloroplasts." Gray J., Janick-Buckner D., Buckner B., Close P.S., Johal G.S. Plant Physiol. 130:1894-1907(2002) [PubMed: 12481072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[3]	"The wound-inducible Lls1 gene from maize is an orthologue of the Arabidopsis Acd1 gene, and the LLS1 protein is present in non-photosynthetic tissues." Yang M., Wardzala E., Johal G.S., Gray J. Plant Mol. Biol. 54:175-191(2004) [PubMed: 15159621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[4]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[7]	"Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene." Pruzinska A., Tanner G., Anders I., Roca M., Hortensteiner S. Proc. Natl. Acad. Sci. U.S.A. 100:15259-15264(2003) [PubMed: 14657372] [Abstract] Cited for: CHARACTERIZATION.
[8]	"The Arabidopsis-accelerated cell death gene ACD1 is involved in oxygenation of pheophorbide a: inhibition of the pheophorbide a oxygenase activity does not lead to the 'Stay-Green' phenotype in Arabidopsis." Tanaka R., Hirashima M., Satoh S., Tanaka A. Plant Cell Physiol. 44:1266-1274(2003) [PubMed: 14701922] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U77347 mRNA. Translation: AAC49679.1. Frameshift. AY344061 mRNA. Translation: AAR05797.1. AL391254 Genomic DNA. Translation: CAC03538.1. CP002686 Genomic DNA. Translation: AEE77964.1. AY093092 mRNA. Translation: AAM13091.1.
IPI	IPI00530021.
PIR	T51785.
RefSeq	NP_190074.1. NM_114357.5.
UniGene	At.21728. At.36095.
3D structure databases
ProteinModelPortal	Q9FYC2.
SMR	Q9FYC2. Positions 87-202.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9FYC2.
Proteomic databases
PRIDE	Q9FYC2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G44880.1; AT3G44880.1; AT3G44880.
GeneID	823622.
GenomeReviews	Gene locus AT3G44880 in contig BA000014_GR.
KEGG	ath:AT3G44880.
NMPDR	fig|3702.1.peg.15696.
Organism-specific databases
TAIR	At3g44880.
Phylogenomic databases
GeneTree	EPGT00070000031021.
HOGENOM	HBG748445.
InParanoid	Q9FYC2.
OMA	VVYATPI.
PhylomeDB	Q9FYC2.
ProtClustDB	PLN02518.
Enzyme and pathway databases
BioCyc	ARA:AT3G44880-MONOMER. MetaCyc:AT3G44880-MONOMER.
BRENDA	1.14.12.20. 399.
Gene expression databases
ArrayExpress	Q9FYC2.
Genevestigator	Q9FYC2.
GermOnline	AT3G44880. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR013626. PaO. IPR017941. Rieske_2Fe-2S. [Graphical view]
Gene3D	G3DSA:2.102.10.10. Rieske_reg. 1 hit.
KO	K13071.
Pfam	PF08417. PaO. 1 hit. PF00355. Rieske. 1 hit. [Graphical view]
SUPFAM	SSF50022. Rieske_dom. 1 hit.
PROSITE	PS51296. RIESKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PAO_ARATH

Accession

Primary (citable) accession number: Q9FYC2
Secondary accession number(s): O04422

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 2, 2004
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program