NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Express;
TISSUE=Leaf;
PubMed=10743659 [NCBI, ExPASy, EBI, Israel, Japan]
Wuethrich K.L., Bovet L., Hunziker P.E., Donnison I.S., Hoertensteiner S.;
"Molecular cloning, functional expression and characterization of RCC reductase, involved in chlorophyll catabolism.";
Plant J. 21:189-198(2000).

Comments

FUNCTION: Catalyzes the key reaction of chlorophyll catabolism, porphyrin macrocycle cleavage of pheophorbide a (pheide a) to a primary fluorescent catabolite (pFCC). Works in a two-step reaction with pheophorbide a oxygenase (PaO) by reducing the C20/C1 double bond of the intermediate, RCC.
CATALYTIC ACTIVITY: Primary fluorescent chlorophyll catabolite + NADP⁺ = red chlorophyll catabolite + NADPH.
PATHWAY: Porphyrin metabolism; chlorophyll degradation .
SUBUNIT: Homodimer (Probable).
SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
TISSUE SPECIFICITY: In etiolated and green primary leaves. Low amount in roots.
DEVELOPMENTAL STAGE: Decreases during leaf senescence, but still present after 8 days of dark-induced senescence.
PTM: The N-terminus is blocked.

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

AJ243066; CAB77705.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q9MTQ6.

Organism-specific databases

Gramene

Q9MTQ6; -.

Family and domain databases

InterPro

IPR009439; RCC_reductase.
Graphical view of domain structure.

Pfam

PF06405; RCC_reductase; 1.
Pfam graphical view of domain structure.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Chlorophyll catabolism; Chloroplast; NADP; Oxidoreductase; Plastid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 205`	`>205`	`Red chlorophyll catabolite reductase.`	`PRO_0000097198`
`NON_TER`	`1 1`

Sequence information

Length: 205 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 22868 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 835DC48C813D5AD7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
IDFMLQSSLH CKVPNGAIDI TSLFINLNAS TDAPHFIMEF IQGSPTSMVV LLDLLPRKDL 

        70         80         90        100        110        120 
ALHPEYIEKY YEDTEVDKQR KIIEQLPQAR PYLSPSLFVR SAFSPTAVFF TIDCGKGGEG 

       130        140        150        160        170        180 
TLEEIVHGHL ASVVKGILQI WLDTCASDAS EMEEGEREIM VKRDRTVRSK SIEVDLTANL 

       190        200 
PRMFGPDVSG RIIAEIRKAF GVQEG

Q9MTQ6 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools