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Protein

Protochlorophyllide reductase

Gene
N/A
Organism
Avena sativa (Oat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).

Catalytic activityi

Chlorophyllide a + NADP+ = protochlorophyllide + NADPH.

Pathway:ichlorophyll biosynthesis

This protein is involved in the pathway chlorophyll biosynthesis, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway chlorophyll biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Photosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.3.1.33. 588.
UniPathwayiUPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Protochlorophyllide reductase (EC:1.3.1.33)
Short name:
PCR
Alternative name(s):
NADPH-protochlorophyllide oxidoreductase
Short name:
POR
OrganismiAvena sativa (Oat)
Taxonomic identifieri4498 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaePoodaePoeaeAveninaeAvena

Organism-specific databases

GrameneiP15904.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 313›313Protochlorophyllide reductasePRO_0000219915Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP15904.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR005979. Prochl_reduct.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
TIGRFAMsiTIGR01289. LPOR. 1 hit.

Sequencei

Sequence statusi: Fragment.

P15904-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VVVITGASSG LGLAAAKALA ETGKWHVVMA CRDFLKASKA AKAAGMADGS
60 70 80 90 100
YTVMHLDLAS LDSVRQFVDA FRRAEMPLDV LVCNAAIYRP TARKPTFTAE
110 120 130 140 150
GVEMSVGVNH LGHFLLARLL LEDLQKSDYP SRRLVIVGSI TGNDNTLAGN
160 170 180 190 200
VPPKANLGDL RGLAGGLTGA SGSAMIDGDE SFDGAKAYKD SKVCNMLTMQ
210 220 230 240 250
EFHRRYHEDT GITFSSLYPG CIATTGLFRE HIPLFRTLFP PFQKFVTKGF
260 270 280 290 300
VSEAESGKRL AQVVGEPSLT KSGVYWSWNK DSASFENQLS QEASDPEKAR
310
KVWELSEKLV GLA
Length:313
Mass (Da):33,797
Last modified:April 1, 1990 - v1
Checksum:i4F81BA5DC8D1487C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17067 mRNA. Translation: CAA34913.1.
PIRiS08406.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17067 mRNA. Translation: CAA34913.1.
PIRiS08406.

3D structure databases

ProteinModelPortaliP15904.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiP15904.

Enzyme and pathway databases

UniPathwayiUPA00668.
BRENDAi1.3.1.33. 588.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR005979. Prochl_reduct.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
TIGRFAMsiTIGR01289. LPOR. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of protochlorophyllide reductase."
    Darrah P.M., Kay S.A., Teakle G.R., Griffiths W.T.
    Biochem. J. 265:789-798(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Peniarth.
    Tissue: Etiolated leaf.

Entry informationi

Entry nameiPOR_AVESA
AccessioniPrimary (citable) accession number: P15904
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 22, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.