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UniProtKB/Swiss-Prot entry Q8S7E1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CAO_ORYSJ
Primary accession number Q8S7E1
Secondary accession numbers Q336Q7 Q336Q8 Q7XC03 Q9FYV0 Q9XJ40
Integrated into Swiss-Prot on September 19, 2006
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 41)
Name and origin of the protein
Protein name Chlorophyllide a oxygenase, chloroplastic [Precursor]
Synonyms Chlorophyll a oxygenase
EC 1.13.12.14
Chlorophyll b synthase
Gene name
Name: CAO
Synonyms: LLS1
OrderedLocusNames: Os10g0567400, LOC_Os10g41780
ORFNames: OSJNBa0057L21.2
From
Oryza sativa subsp. japonica (Rice) [TaxID: 39947] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Ehrhartoideae; Oryzeae; Oryza.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=cv. Hwacheong, and cv. Ilpoom;
Jwa N.-S., Park S.-G., Park C.-H., Kim S.-O., Ahn I.-P., Park S.-Y., Yoon C.-H., Lee Y.-H.;
"Cloning and expression of a rice cDNA encoding a Lls1 homolog of maize.";
Plant Pathol. J. 16:151-155(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
DOI=10.1126/science.1083523; PubMed=12791992 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"In-depth view of structure, activity, and evolution of rice chromosome 10.";
Science 300:1566-1569(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=cv. Nipponbare;
DOI=10.1126/science.1081288; PubMed=12869764 [NCBI, ExPASy, EBI, Israel, Japan]
The rice full-length cDNA consortium;
"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice.";
Science 301:376-379(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 186-541 (ISOFORM 1).
DOI=10.1038/22101; PubMed=10408441 [NCBI, ExPASy, EBI, Israel, Japan]
Tomitani A., Okada K., Miyashita H., Matthijs H.C.P., Ohno T., Tanaka A.;
"Chlorophyll b and phycobilins in the common ancestor of cyanobacteria and chloroplasts.";
Nature 400:159-162(1999).
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+.
  • CATALYTIC ACTIVITY: 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).
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ8S7E1-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ8S7E1-2
    Features which should be applied to build the isoform sequence: VSP_020614.
  • TISSUE SPECIFICITY: Expressed in leaves and germinating seedlings, but not in sheaths and roots.
  • INDUCTION: Down-regulated by treatment with H(2)O(2).
  • 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.
  • SIMILARITY: Contains 1 Rieske domain.
  • SEQUENCE CAUTION:
    • Sequence=AAG03051.1; Type=Frameshift; Positions=495, 499, 513;
    • Sequence=AAP55073.2; Type=Erroneous gene model prediction;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF284781; AAG03051.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC087599; AAL79703.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DP000086; ABB48002.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DP000086; ABB48003.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DP000086; AAP55073.2; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK067730; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
AK065124; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
AB021310; BAA82479.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001065433.1; -.
UniGene Os.22029
3D structure databases
ModBase Q8S7E1.
Organism-specific databases
Gramene Q8S7E1; -.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0010277; Molecular function: chlorophyllide a oxygenase activity (inferred from electronic annotation from EC).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0015995; Biological process: chlorophyll biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013626; PaO.
IPR005806; Rieske_reg.
Graphical view of domain structure.
Gene3D G3DSA:2.102.10.10; Rieske_reg; 1.
Pfam PF08417; PaO; 1.
PF00355; Rieske; 1.
Pfam graphical view of domain structure.
PROSITE PS51296; RIESKE; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8S7E1.
Genome annotation databases
GeneID 4349433; -.
KEGG osa:4349433; -.
NMPDR fig|39947.1.peg.14275; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Alternative splicing; Chlorophyll biosynthesis; Chloroplast; Coiled coil; Iron; Iron-sulfur; Membrane; Metal-binding; NADP; Oxidoreductase; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Chloroplast (Potential). 
CHAIN   ?   541        Chlorophyllide a oxygenase, chloroplastic. PRO_0000250164
DOMAIN   220   320  101     Rieske. 
COILED   114   151  38     Potential. 
METAL   261   261        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   263   263        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
METAL   280   280        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   283   283        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
METAL   359   359        Iron (By similarity). 
METAL   363   363        Iron (By similarity). 
METAL   366   366        Iron (By similarity). 
METAL   371   371        Iron (By similarity). 
VAR_SEQ   1    25        MTTVASLSLLPHLLIKPSFRCCSRK -> MVTLLIETTQ (in isoform 2). VSP_020614
CONFLICT   179   179        E -> K (in Ref. 3; AK067730). 
CONFLICT   186   189        STSS -> PTRP (in Ref. 4; BAA82479). 
CONFLICT   404   404        D -> G (in Ref. 3; AK067730). 
CONFLICT   489   489        L -> V (in Ref. 1; AAG03051). 
Sequence information
Length: 541 AA [This is the length of the unprocessed precursor] Molecular weight: 60855 Da [This is the MW of the unprocessed precursor] CRC64: DE7EFE9CCF68AB21 [This is a checksum on the sequence]
        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 

Q8S7E1 in FASTA format

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