Reviewed, UniProtKB/Swiss-Prot Q8S7E1 (CAO_ORYSJ)

Names and origin

Protein names

Recommended name:
    Chlorophyllide a oxygenase, chloroplastic
      Short name=Chlorophyll a oxygenase
    EC=1.13.12.14
Alternative name(s):
    Chlorophyll b synthase

Gene names

Name:	CAO
Synonyms:	LLS1
Ordered Locus Names:	Os10g0567400, LOC_Os10g41780
ORF Names:	OSJNBa0057L21.2

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes a two-step oxygenase reaction involved in the synthesis of chlorophyll b. Acts specifically on the non-esterified chlorophyllide a and not on chlorophyll a.
Catalytic activity	Chlorophyllide a + O2 + NADPH = 7-hydroxychlorophyllide a + H2O + NADP+. 7-hydroxychlorophyllide a + O2 + NADPH = chlorophyllide b + 2 H2O + NADP+.
Subcellular location	Plastid › chloroplast membrane; Peripheral membrane protein. Plastid › chloroplast thylakoid membrane; Peripheral membrane protein By similarity.
Tissue specificity	Expressed in leaves and germinating seedlings, but not in sheaths and roots. Ref.1
Induction	Down-regulated by treatment with H2O2. Ref.1
Domain	Consists of three domains A, B and C. The C-terminal C domain possesses catalytic function while the N-terminal A domain confers protein instability in response to chlorophyll b accumulation.
Sequence similarities	Contains 1 Rieske domain.
Sequence caution	The sequence AAG03051.1 differs from that shown. Reason: Frameshift at positions 495, 499 and 513. The sequence AAP55073.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis
Cellular component	Chloroplast Membrane Plastid Thylakoid
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell thylakoid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW chlorophyllide a oxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8S7E1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8S7E1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MTTVASLSLLPHLLIKPSFRCCSRK → MVTLLIETTQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Chloroplast Potential
	Chain	? – 541		Chlorophyllide a oxygenase, chloroplastic		PRO_0000250164
Regions
	Domain	220 – 320	101	Rieske
	Coiled coil	114 – 151	38	Potential
Sites
	Metal binding	261	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	263	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	280	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	283	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	359	1	Iron By similarity
	Metal binding	363	1	Iron By similarity
	Metal binding	366	1	Iron By similarity
	Metal binding	371	1	Iron By similarity
Natural variations
	Alternative sequence	1 – 25	25	MTTVA…CCSRK → MVTLLIETTQ in isoform 2.		VSP_020614
Experimental info
	Sequence conflict	179	1	E → K in AK067730. Ref.3
	Sequence conflict	186 – 189	4	STSS → PTRP in BAA82479. Ref.4
	Sequence conflict	404	1	D → G in AK067730. Ref.3
	Sequence conflict	489	1	L → V in AAG03051. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: DE7EFE9CCF68AB21	FASTA	541	60,855
	10 20 30 40 50 60 MTTVASLSLL PHLLIKPSFR CCSRKGVGRY GGIKVYAVLG DDGADYAKNN AWEALFHVDD 70 80 90 100 110 120 PGPRVPIAKG KFLDVNQALE VVRFDIQYCD WRARQDLLTI MVLHNKVVEV LNPLAREFKS 130 140 150 160 170 180 IGTLRKELAE LQEELAKAHN QVHLSETRVS SALDKLAQME TLVNDRLLQD GGSSASTAEC 190 200 210 220 230 240 TSLAPSTSSA SRVVNKKPPR RSLNVSGPVQ PYNPSLKNFW YPVAFSSDLK DDTMVPIDCF 250 260 270 280 290 300 EEQWVIFRGK DGRPGCVMNT CAHRACPLHL GSVNEGRIQC PYHGWEYSTD GKCEKMPSTK 310 320 330 340 350 360 MLNVRIRSLP CFEQEGMVWI WPGNDPPKST IPSLLPPSGF TIHAEIVMEL PVEHGLLLDN 370 380 390 400 410 420 LLDLAHAPFT HTSTFAKGWS VPSLVKFLTP SSGLQGYWDP YPIDMEFRPP CMVLSTIGIS 430 440 450 460 470 480 KPGKLEGKST KQCSTHLHQL HICLPSSRNK TRLLYRMSLD FAPWIKHVPF MHILWSHFAE 490 500 510 520 530 540 KVLNEDLRLV LGQQERMING ANVWNWPVSY DKLGIRYRLW RDAIERGVDR LPFSNQSESG S
	Isoform 2. Checksum: AD4A470A2A16C451	FASTA	526	59,201
	10 20 30 40 50 60 MVTLLIETTQ GVGRYGGIKV YAVLGDDGAD YAKNNAWEAL FHVDDPGPRV PIAKGKFLDV 70 80 90 100 110 120 NQALEVVRFD IQYCDWRARQ DLLTIMVLHN KVVEVLNPLA REFKSIGTLR KELAELQEEL 130 140 150 160 170 180 AKAHNQVHLS ETRVSSALDK LAQMETLVND RLLQDGGSSA STAECTSLAP STSSASRVVN 190 200 210 220 230 240 KKPPRRSLNV SGPVQPYNPS LKNFWYPVAF SSDLKDDTMV PIDCFEEQWV IFRGKDGRPG 250 260 270 280 290 300 CVMNTCAHRA CPLHLGSVNE GRIQCPYHGW EYSTDGKCEK MPSTKMLNVR IRSLPCFEQE 310 320 330 340 350 360 GMVWIWPGND PPKSTIPSLL PPSGFTIHAE IVMELPVEHG LLLDNLLDLA HAPFTHTSTF 370 380 390 400 410 420 AKGWSVPSLV KFLTPSSGLQ GYWDPYPIDM EFRPPCMVLS TIGISKPGKL EGKSTKQCST 430 440 450 460 470 480 HLHQLHICLP SSRNKTRLLY RMSLDFAPWI KHVPFMHILW SHFAEKVLNE DLRLVLGQQE 490 500 510 520 RMINGANVWN WPVSYDKLGI RYRLWRDAIE RGVDRLPFSN QSESGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a rice cDNA encoding a Lls1 homolog of maize." Jwa N.-S., Park S.-G., Park C.-H., Kim S.-O., Ahn I.-P., Park S.-Y., Yoon C.-H., Lee Y.-H. Plant Pathol. J. 16:151-155(2000) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION. Strain: cv. Hwacheong and cv. Ilpoom.
[2]	"In-depth view of structure, activity, and evolution of rice chromosome 10." Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H. , Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A. Science 300:1566-1569(2003) [PubMed: 12791992] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[3]	"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice." The rice full-length cDNA consortium Science 301:376-379(2003) [PubMed: 12869764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: cv. Nipponbare.
[4]	"Chlorophyll b and phycobilins in the common ancestor of cyanobacteria and chloroplasts." Tomitani A., Okada K., Miyashita H., Matthijs H.C.P., Ohno T., Tanaka A. Nature 400:159-162(1999) [PubMed: 10408441] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 186-541 (ISOFORM 1).

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF284781 mRNA. Translation: AAG03051.1. Frameshift. AC087599 Genomic DNA. Translation: AAL79703.1. DP000086 Genomic DNA. Translation: ABB48002.2. DP000086 Genomic DNA. Translation: ABB48003.2. DP000086 Genomic DNA. Translation: AAP55073.2. Sequence problems. AK067730 mRNA. No translation available. AK065124 mRNA. No translation available. AB021310 mRNA. Translation: BAA82479.1.
RefSeq	NP_001065433.1.
UniGene	Os.22029
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4349433.
KEGG	osa:4349433.
NMPDR	fig|39947.1.peg.14275.
Organism-specific databases
Gramene	Q8S7E1.
Family and domain databases
InterPro	IPR013626. PaO. IPR017941. Rieske_2Fe-2S. IPR015881. Ring-hydroxy_dOase_2Fe2S_BS. [Graphical view]
Gene3D	G3DSA:2.102.10.10. Rieske_reg. 1 hit.
Pfam	PF08417. PaO. 1 hit. PF00355. Rieske. 1 hit. [Graphical view]
PROSITE	PS51296. RIESKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CAO_ORYSJ

Accession

Primary (citable) accession number: Q8S7E1
Secondary accession number(s): Q336Q7 , Q336Q8, Q7XC03, Q9FYV0, Q9XJ40

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	June 1, 2002
Last modified:	January 19, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)