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UniProtKB/Swiss-Prot entry P21218


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

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Entry information
Entry name PORB_ARATH
Primary accession number P21218
Secondary accession number Q42537
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on November 1, 1997 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 84)
Name and origin of the protein
Protein name Protochlorophyllide reductase B, chloroplastic [Precursor]
Synonyms PCR B
EC 1.3.1.33
NADPH-protochlorophyllide oxidoreductase B
POR B
Gene name
Name: PORB
OrderedLocusNames: At4g27440
ORFNames: F27G19.40
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1104/pp.108.4.1505; PubMed=7659751 [NCBI, ExPASy, EBI, Israel, Japan]
Armstrong G.A., Runge S., Frick G., Sperling U., Apel K.;
"Identification of NADPH:protochlorophyllide oxidoreductases A and B: a branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana.";
Plant Physiol. 108:1505-1517(1995).
[2]
NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
STRAIN=cv. An-2;
TISSUE=Leaf;
DOI=10.1007/BF00023426; PubMed=1714319 [NCBI, ExPASy, EBI, Israel, Japan]
Benli M., Schuelz R., Apel K.;
"Effect of light on the NADPH-protochlorophyllide oxidoreductase of Arabidopsis thaliana.";
Plant Mol. Biol. 16:615-625(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M300030-MCP200; PubMed=12766230 [NCBI, ExPASy, EBI, Israel, Japan]
Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.;
"Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana.";
Mol. Cell. Proteomics 2:325-345(2003).
Comments
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
U29785; AAC49044.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL078467; CAB43876.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161571; CAB81394.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY042883; AAK68823.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY054206; AAL06867.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY081465; AAM10027.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T08936; T08936.
RefSeq NP_001031731.1; -.
NP_194474.1; -.
UniGene At.23416
3D structure databases
HSSP P14061; 1FDS. [HSSP ENTRY / PDB]
ModBase P21218.
Organism-specific databases
TAIR At4g27440; -.
Gene expression databases
ArrayExpress P21218; -.
GermOnline AT4G27440; Arabidopsis thaliana.
Ontologies
GO
GO:0009527; Cellular component: plastid outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
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.
PRINTS PR00081; GDHRDH.
TIGRFAMs TIGR01289; LPOR; 1.
BLOCKS P21218.
ProtoNet P21218.
Genome annotation databases
GeneID 828853; -.
GenomeReviews CT486007_GR; AT4G27440.
KEGG ath:AT4G27440; -.
NMPDR fig|3702.1.peg.20681; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chlorophyll biosynthesis; Chloroplast; Complete proteome; Direct protein sequencing; Membrane; NADP; Oxidoreductase; Photosynthesis; Plastid; Plastid outer membrane; Polymorphism; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    66  66     Chloroplast (Potential). 
CHAIN   67   401  335     Protochlorophyllide reductase B, chloroplastic. PRO_0000023288
VARIANT   395   395  1     E -> D (in strain: cv. An-2). 
Sequence information
Length: 401 AA [This is the length of the unprocessed precursor] Molecular weight: 43359 Da [This is the MW of the unprocessed precursor] CRC64: 0C2132F980AF6CA3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALQAASLVS SAFSVRKDAK LNASSSSFKD SSLFGASITD QIKSEHGSSS LRFKREQSLR 

        70         80         90        100        110        120 
NLAIRAQTAA TSSPTVTKSV DGKKTLRKGN VVVTGASSGL GLATAKALAE TGKWNVIMAC 

       130        140        150        160        170        180 
RDFLKAERAA KSVGMPKDSY TVMHLDLASL DSVRQFVDNF RRTETPLDVL VCNAAVYFPT 

       190        200        210        220        230        240 
AKEPTYSAEG FELSVATNHL GHFLLARLLL DDLKKSDYPS KRLIIVGSIT GNTNTLAGNV 

       250        260        270        280        290        300 
PPKANLGDLR GLAGGLNGLN SSAMIDGGDF DGAKAYKDSK VCNMLTMQEF HRRFHEETGV 

       310        320        330        340        350        360 
TFASLYPGCI ASTGLFREHI PLFRALFPPF QKYITKGYVS ETESGKRLAQ VVSDPSLTKS 

       370        380        390        400 
GVYWSWNNAS ASFENQLSEE ASDVEKARKV WEISEKLVGL A 

P21218 in FASTA format

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