NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=cv. Carina;
TISSUE=Leaf;
DOI=10.1007/BF02464904; PubMed=2671659 [NCBI, ExPASy, EBI, Israel, Japan]
Schuelz R., Steinmueller K., Klaas M., Forreiter C., Rasmussen S., Hiller C., Apel K.;
"Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli.";
Mol. Gen. Genet. 217:355-361(1989).

Comments

FUNCTION: Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
CATALYTIC ACTIVITY: Chlorophyllide a + NADP⁺ = protochlorophyllide + NADPH.
PATHWAY: Porphyrin metabolism; chlorophyll biosynthesis .
SUBCELLULAR LOCATION: Plastid, chloroplast.
DEVELOPMENTAL STAGE: Active only transiently in etiolated seedlings at the beginning of illumination.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. POR subfamily.

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

X15869; CAA33879.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S04783; S04783.

3D structure databases

HSSP

P14061; 1FDS. [HSSP ENTRY / PDB]

ModBase

P13653.

Organism-specific databases

Gramene

P13653; -.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
IPR005979; Prochl_reduct.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PR00081; GDHRDH.

TIGR01289; LPOR; 1.

Other

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

Keywords

Chlorophyll biosynthesis; Chloroplast; Direct protein sequencing; NADP; Oxidoreductase; Photosynthesis; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 74`	`74`	`Chloroplast.`
`CHAIN`	`75 388`	`314`	`Protochlorophyllide reductase A, chloroplastic.`	`PRO_0000023293`

Sequence information

Length: 388 AA [This is the length of the unprocessed precursor]

Molecular weight: 41181 Da [This is the MW of the unprocessed precursor]

CRC64: EBD3EF153D96C129 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALQLLPSTL SVPKKGSSMG AVAVKDTAAF LGVSSKAKKA SLAVRTQVAT APSPVTTSPG 

        70         80         90        100        110        120 
STASSPSGKK TLRQGVVVIT GASSGLGLAA AKALAETGKW HVVMACRDFL KASKAAKAAG 

       130        140        150        160        170        180 
MADGSYTVMH LDLASLDSVR QFVDAFRRAE MPLDVLVCNA AIYRPTARTP TFTADGHEMS 

       190        200        210        220        230        240 
VGVNHLGHFL LARLLMEDLQ KSDYPSRRMV IVGSITGNSN TLAGNVPPKA SLGDLRGLAG 

       250        260        270        280        290        300 
GLSGASGSAM IDGDESFDGA KAYKDSKVCN MLTMQEFHRR YHEETGITFS SLYPGCIATT 

       310        320        330        340        350        360 
GLFREHIPLF RTLFPPFQKF VTKGFVSEAE SGKRLAQVVA EPVLTKSGVY WSWNKDSASF 

       370        380 
ENQLSQEASD PEKARKVWEL SEKLVGLA

P13653 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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