ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q5EFU4

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CRD1_HORVU
Primary accession number Q5EFU4
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on March 15, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 20)
Name and origin of the protein
Protein name Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase, chloroplastic [Precursor]
Synonyms Mg-protoporphyrin IX monomethyl ester oxidative cyclase
EC 1.14.13.81
Protein Xantha-l
Gene name
Name: CRD1
From
Hordeum vulgare (Barley) [TaxID: 4513] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Pooideae; Triticeae; Hordeum.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY, PATHWAY, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-154 AND SER-180.
DOI=10.1073/pnas.0501784102; PubMed=15824317 [NCBI, ExPASy, EBI, Israel, Japan]
Rzeznicka K., Walker C.J., Westergren T., Kannangara C.G., von Wettstein D., Merchant S., Gough S.P., Hansson M.;
"Xantha-l encodes a membrane subunit of the aerobic Mg-protoporphyrin IX monomethyl ester cyclase involved in chlorophyll biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 102:5886-5891(2005).
Comments
  • FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. 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 metabolism; chlorophyll biosynthesis.
  • SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral membrane protein (Potential).
  • 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
AY887063; AAW80518.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase Q5EFU4.
Organism-specific databases
Gramene Q5EFU4; -.
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 Q5EFU4.
Other
ProtoNet Q5EFU4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chlorophyll biosynthesis; Chloroplast; Iron; Membrane; Metal-binding; NADP; Oxidoreductase; Photosynthesis; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    45  45     Chloroplast (Potential). 
CHAIN   46   417  372     Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase, chloroplastic. PRO_0000000603
MUTAGEN   154   154        G->E: In xantha-l(81); induces accumulation of MgPMME. 
MUTAGEN   180   180        S->F: In xantha-l(35); induces accumulation of MgPMME. 
Sequence information
Length: 417 AA [This is the length of the unprocessed precursor] Molecular weight: 48161 Da [This is the MW of the unprocessed precursor] CRC64: 83933398C325E77E [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MASAMELSLL NPAMHHYGIA AKTASHLPVV PARRASSGAV RFRVRAAAAA PPAPAAKPGS 

        70         80         90        100        110        120 
PKKRGKTEVN ESLLTPRFYT TDFDEMEQLF NAEINKQLNQ DEFDALLQEF KTDYNQTHFI 

       130        140        150        160        170        180 
RNPEFKEAAD KMQGPLRQIF VEFLERSCTA EFSGFLLYKE LGRRLKKTNP VVAEIFSLMS 

       190        200        210        220        230        240 
RDEARHAGFL NKGLSDFNLA LDLGFLTKAR KYTFFKPKFI FYATYLSEKI GYWRYITIFR 

       250        260        270        280        290        300 
HLKANPEYQV YPIFKYFENW CQDENRHGDF FSALLKAQPQ FLNDWKAKLW SRFFCLSVYI 

       310        320        330        340        350        360 
TMYLNDCQRS AFYEGIGLNT KEFDMHVIYE TNRTTARIFP AVPDVENPEF KRKLDRMVDI 

       370        380        390        400        410 
NLKIISIGES NDLPLVKNLK RVPLIAQLVS EIIAAYLMPP IESGSVDFAE FEPKLVY
Q5EFU4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!