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UniProtKB/Swiss-Prot entry Q9MBA1


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

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Entry information
Entry name CAO_ARATH
Primary accession number Q9MBA1
Secondary accession numbers Q3ECX2 Q3ECX3 Q9SPF2 Q9XJ37
Integrated into Swiss-Prot on January 24, 2006
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 51)
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
AtCAO
Gene name
Name: CAO
OrderedLocusNames: At1g44446
ORFNames: T18F15.7
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), MUTANTS CHL-2 AND CHL-3, AND INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1073/pnas.96.18.10507; PubMed=10468639 [NCBI, ExPASy, EBI, Israel, Japan]
Espineda C.E., Linford A.S., Devine D., Brusslan J.A.;
"The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 96:10507-10511(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND FUNCTION.
PubMed=10758481 [NCBI, ExPASy, EBI, Israel, Japan]
Oster U., Tanaka R., Tanaka A., Ruediger W.;
"Cloning and functional expression of the gene encoding the key enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana.";
Plant J. 21:305-310(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[6]
CHARACTERIZATION.
DOI=10.1007/s00425-003-1181-6; PubMed=14716565 [NCBI, ExPASy, EBI, Israel, Japan]
Nagata N., Satoh S., Tanaka R., Tanaka A.;
"Domain structures of chlorophyllide a oxygenase of green plants and Prochlorothrix hollandica in relation to catalytic functions.";
Planta 218:1019-1025(2004).
[7]
SUBCELLULAR LOCATION.
DOI=10.1186/1471-2229-4-5; PubMed=15086960 [NCBI, ExPASy, EBI, Israel, Japan]
Eggink L.L., LoBrutto R., Brune D.C., Brusslan J., Yamasato A., Tanaka A., Hoober J.K.;
"Synthesis of chlorophyll b: localization of chlorophyllide a oxygenase and discovery of a stable radical in the catalytic subunit.";
BMC Plant Biol. 4:5-5(2004).
[8]
CHARACTERIZATION, AND SUBCELLULAR LOCATION.
DOI=10.1105/tpc.105.031518; PubMed=15805480 [NCBI, ExPASy, EBI, Israel, Japan]
Yamasato A., Nagata N., Tanaka R., Tanaka A.;
"The N-terminal domain of chlorophyllide a oxygenase confers protein instability in response to chlorophyll b accumulation in Arabidopsis.";
Plant Cell 17:1585-1597(2005).
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.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ9MBA1-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ9MBA1-2
    Note: Derived from EST data. No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_017073, VSP_017074.
    Name3
    Isoform IDQ9MBA1-3
    Note: Derived from EST data. No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_017071, VSP_017072.
  • INDUCTION: By light. Probable feedback regulation.
  • 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.
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
AB021316; BAA82484.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177200; AAD54323.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030565; BAA90462.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC084807; AAK43487.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128357; AAM91560.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT002075; AAN72086.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T52458; T52458.
RefSeq NP_175088.1; -.
NP_973969.1; -.
NP_973970.1; -.
UniGene At.19047
3D structure databases
ModBase Q9MBA1.
Enzyme and pathway databases
BioCyc MetaCyc:AT1G44446-MON; -.
Organism-specific databases
TAIR At1g44446; -.
Gene expression databases
ArrayExpress Q9MBA1; -.
GermOnline AT1G44446; Arabidopsis thaliana.
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).
BLOCKS Q9MBA1.
Genome annotation databases
GeneID 841029; -.
GenomeReviews CT485782_GR; AT1G44446.
KEGG ath:AT1G44446; -.
NMPDR fig|3702.1.peg.4097; -.
Other
ProtoNet Q9MBA1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Alternative splicing; Chlorophyll biosynthesis; Chloroplast; Coiled coil; Complete proteome; 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    36  36     Chloroplast (Potential). 
CHAIN   37   536  500     Chlorophyllide a oxygenase, chloroplastic. PRO_0000045788
DOMAIN   221   321  101     Rieske. 
COILED   123   150  28     Potential. 
METAL   262   262        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   264   264        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
METAL   281   281        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   284   284        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
METAL   360   360        Iron (By similarity). 
METAL   364   364        Iron (By similarity). 
METAL   367   367        Iron (By similarity). 
METAL   372   372        Iron (By similarity). 
VAR_SEQ   384   433        SLVKFLTPTSGLQGYWDPYPIDMEFKPPCIVLSTIGISKP GKLEGKSTQQ -> RFLLTLITLFSAKMKLGLSFLFLVLQFGEVFNTYLGSPRI LGSISNRYGI (in isoform 3). VSP_017071
VAR_SEQ   434   536        Missing (in isoform 3). VSP_017072
VAR_SEQ   484   511        LNEDLRLVLGQQERMLNGANIWNLPVAY -> KVHHKWIDHLQPSSQSCFLSYRFYISRS (in isoform 2). VSP_017073
VAR_SEQ   512   536        Missing (in isoform 2). VSP_017074
MUTAGEN   274   274        V->E: In chl-2; reduced level of chlorophyll b. 
MUTAGEN   334   335        SL->VA: In chl-3; reduced level of chlorophyll b. 
MUTAGEN   336   375        Missing: In chl-3; absence of chlorophyll b. 
CONFLICT   115   115        P -> R (in Ref. 2; AAD54323). 
CONFLICT   438   438        L -> F (in Ref. 1; BAA82484). 
CONFLICT   456   456        Y -> C (in Ref. 1; BAA82484). 
Sequence information
Length: 536 AA [This is the length of the unprocessed precursor] Molecular weight: 60331 Da [This is the MW of the unprocessed precursor] CRC64: E28640DB19F8C3FB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNAAVFSPSA LSLPISFSKT RSSFLSRKKG VKGEFRVFAV FGDESGLVEK KSQWRPLFDV 

        70         80         90        100        110        120 
EDPRSKAPPY KGKFLDVNQA IEVARFDIQY LDWRARQDLL TIMILHDKVV DVLNPLAREY 

       130        140        150        160        170        180 
KSIGTVKKEL AGLQEELSKA HQQVHISEAR VSTALDKLAH MEELVNDRLL PGRVVTELDK 

       190        200        210        220        230        240 
PSSSTTASAV ELDREKTNTG AKSLNVSGPV PPYSPHLKNF WYPVAFTADL KHDTMVPIEC 

       250        260        270        280        290        300 
FEQPWVIFRG EDGKPGCVRN TCAHRACPLD LGTVNEGRIQ CPYHGWEYST DGECKKMPST 

       310        320        330        340        350        360 
KLLKVKIKSL PCLEQEGMIW IWPGDEPPAP ILPSLQPPSG FLIHAELVMD LPVEHGLLLD 

       370        380        390        400        410        420 
NLLDLAHAPF THTSTFAKGW SVPSLVKFLT PTSGLQGYWD PYPIDMEFKP PCIVLSTIGI 

       430        440        450        460        470        480 
SKPGKLEGKS TQQCATHLHQ LHVCLPSSKN KTRLLYRMSL DFAPILKNLP FMEHLWRHFA 

       490        500        510        520        530 
EQVLNEDLRL VLGQQERMLN GANIWNLPVA YDKLGVRYRL WRNAVDRGDD KLPFSG 

Q9MBA1 in FASTA format

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