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UniProtKB/Swiss-Prot entry Q9LD46


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

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Entry information
Entry name CRD1_CHLRE
Primary accession number Q9LD46
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 35)
Name and origin of the protein
Protein name Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 1, chloroplastic [Precursor]
Synonyms Mg-protoporphyrin IX monomethyl ester oxidative cyclase 1
EC 1.14.13.81
Copper response defect 1 protein
Copper-response target 1 protein
Gene name
Name: CRD1
From
Chlamydomonas reinhardtii [TaxID: 3055] 
Taxonomy Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
DOI=10.1093/emboj/19.10.2139; PubMed=10811605 [NCBI, ExPASy, EBI, Israel, Japan]
Moseley J.L., Quinn J., Eriksson M., Merchant S.;
"The Crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii.";
EMBO J. 19:2139-2151(2000).
[2]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1093/emboj/cdf666; PubMed=12485992 [NCBI, ExPASy, EBI, Israel, Japan]
Moseley J.L., Allinger T., Herzog S., Hoerth P., Wehinger E., Merchant S., Hippler M.;
"Adaptation to Fe-deficiency requires remodeling of the photosynthetic apparatus.";
EMBO J. 21:6709-6720(2002).
[3]
SUBCELLULAR LOCATION, AND INDUCTION.
DOI=10.1105/tpc.010420; PubMed=11910013 [NCBI, ExPASy, EBI, Israel, Japan]
Moseley J.L., Page M.D., Alder N.P., Eriksson M., Quinn J., Soto F., Theg S.M., Hippler M., Merchant S.;
"Reciprocal expression of two candidate di-iron enzymes affecting photosystem I and light-harvesting complex accumulation.";
Plant Cell 14:673-688(2002).
[4]
INDUCTION.
DOI=10.1104/pp.010694; PubMed=11842150 [NCBI, ExPASy, EBI, Israel, Japan]
Quinn J.M., Eriksson M., Moseley J.L., Merchant S.;
"Oxygen deficiency responsive gene expression in Chlamydomonas reinhardtii through a copper-sensing signal transduction pathway.";
Plant Physiol. 128:463-471(2002).
Comments
  • FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis under oxygen- and copper-deficient conditions. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME).
  • CATALYTIC ACTIVITY: Magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + O2 = 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + NADP+ + H2O.
  • CATALYTIC ACTIVITY: 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + O2 = 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADP+ + 2 H2O.
  • CATALYTIC ACTIVITY: 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + O2 = divinylprotochlorophyllide + NADP+ + 2 H2O.
  • COFACTOR: Iron (By similarity).
  • PATHWAY: Porphyrin biosynthesis; chlorophyll biosynthesis.
  • SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane.
  • INDUCTION: Induced in absence of copper and oxygen. Regulated by CRR1 protein, which activates its transcription in absence of copper.
  • SIMILARITY: Belongs to the acsF family.
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
AF226628; AAF65221.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237671; AAF63477.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_001692557.1; -.
UniGene Cre.5891
3D structure databases
ModBase Q9LD46.
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:0009579; Cellular component: thylakoid (inferred from electronic annotation from UniProtKB-KW).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0048529; Molecular function: magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase activity (inferred from electronic annotation from EC).
GO:0015995; Biological process: chlorophyll biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0015979; Biological process: photosynthesis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR008434; AcsF.
IPR003251; Rubrerythrin.
Graphical view of domain structure.
Pfam PF02915; Rubrerythrin; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02029; AcsF; 1.
BLOCKS Q9LD46.
ProtoNet Q9LD46.
Genome annotation databases
GeneID 5718021; -.
KEGG cre:CHLREDRAFT_183476; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chlorophyll biosynthesis; Chloroplast; Iron; Membrane; Metal-binding; NADP; Oxidoreductase; Photosynthesis; Plastid; Thylakoid; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
TRANSIT   1     ?        Chloroplast (Potential). 
CHAIN   ?   407        Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 1, chloroplastic. PRO_0000000599
Sequence information
Length: 407 AA [This is the length of the unprocessed precursor] Molecular weight: 47212 Da [This is the MW of the unprocessed precursor] CRC64: FD13EE5AC9C55CFE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQTTLKQQRA SGRVSARQPF RSAAVARPRR STVRVQASAA PLNDGLGFET MRDGIKVAAK 

        70         80         90        100        110        120 
ETLLTPRFYT TDFDEMEQLF SKEINPNLDM EELNACLNEF RNDYNKVHFV RNETFKAAAD 

       130        140        150        160        170        180 
KVTGETRRIF IEFLERSCTA EFSGFLLYKE LARRMKASSP EVAEMFLLMS RDEARHAGFL 

       190        200        210        220        230        240 
NKALSDFNLA LDLGFLTKNR TYTYFKPKFI IYATFLSEKI GYWRYITIYR HLQRNPDNQF 

       250        260        270        280        290        300 
YPLFEYFENW CQDENRHGDF LAACLKAKPE LLNTFEAKLW SKFFCLSVYI TMYLNDHQRT 

       310        320        330        340        350        360 
KFYESLGLNT RQFNQHVIIE TNRATERLFP VVPDVEDPRF FEILNKMVDV NAKLVELSAS 

       370        380        390        400 
SSPLAGLQKL PLLERMASYC LQLLFFKEKD VGSVDIAGSG ASRNLAY 

Q9LD46 in FASTA format

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