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UniProtKB/Swiss-Prot entry Q8L940


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

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Entry information
Entry name PDX13_ARATH
Primary accession number Q8L940
Secondary accession numbers Q3KRU4 Q9M032
Integrated into Swiss-Prot on March 15, 2004
Sequence was last modified on March 15, 2004 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 45)
Name and origin of the protein
Protein name Pyridoxal biosynthesis protein PDX1.3
Synonyms AtPDX1.3
AtPDX1;1
Gene name
Name: PDX13
Synonyms: GIP2, PDX1L3, RSR4
OrderedLocusNames: At5g01410
ORFNames: T10O8.120
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]
FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
DOI=10.1111/j.1365-313X.2005.02538.x; PubMed=16236150 [NCBI, ExPASy, EBI, Israel, Japan]
Chen H., Xiong L.;
"Pyridoxine is required for post-embryonic root development and tolerance to osmotic and oxidative stresses.";
Plant J. 44:396-408(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-54, TISSUE SPECIFICITY, AND INTERACTION WITH PDX1.1, PDX1.2 AND PDX2.
STRAIN=cv. C24;
DOI=10.1105/tpc.105.036269; PubMed=16766694 [NCBI, ExPASy, EBI, Israel, Japan]
Wagner S., Bernhardt A., Leuendorf J.E., Drewke C., Lytovchenko A., Mujahed N., Gurgui C., Frommer W.B., Leistner E., Fernie A.R., Hellmann H.;
"Analysis of the Arabidopsis rsr4-1/pdx1-3 mutant reveals the critical function of the PDX1 protein family in metabolism, development, and vitamin B6 biosynthesis.";
Plant Cell 18:1722-1735(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1073/pnas.0506228102; PubMed=16157873 [NCBI, ExPASy, EBI, Israel, Japan]
Tambasco-Studart M., Titiz O., Raschle T., Forster G., Amrhein N., Fitzpatrick T.B.;
"Vitamin B6 biosynthesis in higher plants.";
Proc. Natl. Acad. Sci. U.S.A. 102:13687-13692(2005).
Comments
  • FUNCTION: Involved in the production of pyridoxal (vitamin B6). Also plays an indirect role in osmotic or salt tolerance, and in resistance to singlet oxygen-generating photosensitizers.
  • PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
  • SUBUNIT: Homodimer or heterodimer with PDX1.1 or PDX1.2. Interacts with PDX2.
  • INTERACTION:
    Q9ZNR6:PDX12; NbExp=1; IntAct=EBI-1545956, EBI-1545987;
  • SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Membrane.
  • TISSUE SPECIFICITY: Expressed in cotyledons, rapidly dividing root stele tissues, stems, leaves, flowers, mature pollen, and siliques.
  • INDUCTION: Not induced by cold, salt, drought or UV stress, or by abscisic acid or jasmonic acid.
  • MISCELLANEOUS: Loss-of-function mutants (T-DNA insertion) have a lower leaf carotenoid and chlorophyll a and b content, and are impaired both in root cell division and in root cell elongation. Mutant rsr4-1 can be complemented by the addition of any of the vitamin B6 vitamers, except pyridoxal 5'-phosphate.
  • MISCELLANEOUS: In plants, synthesis of vitamin B6 does not involve deoxyxylulose 5-phosphate but utilizes intermediates from the pentose phosphate pathway and from glycolysis.
  • MISCELLANEOUS: Vitamin B6 is an essential quencher of singlet oxygen in plants, that can protect cellular membranes from lipid peroxidation.
  • SIMILARITY: Belongs to the pdxS/SNZ 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
AY972813; AAY42123.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161746; CAB81924.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF428298; AAL16130.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF446352; AAL48227.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY097428; AAM19944.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY088650; AAM66972.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK227197; BAE99236.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T48163; T48163.
RefSeq NP_195761.1; -.
UniGene At.23386
3D structure databases
ModBase Q8L940.
Protein-protein interaction databases
IntAct Q8L940; -.
Organism-specific databases
TAIR At5g01410; -.
Gene expression databases
ArrayExpress Q8L940; -.
GermOnline AT5G01410; Arabidopsis thaliana.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR001852; Snz1p/Sor1.
Graphical view of domain structure.
Pfam PF01680; SOR_SNZ; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF029271; Pdx1; 1.
ProDom PD004958; Snz1p/Sor1; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00343; Snz1p/Sor1; 1.
PROSITE PS01235; PDXS_SNZ_1; 1.
PS51129; PDXS_SNZ_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q8L940.
Proteomic databases
ProMEX Q8L940; -.
Genome annotation databases
GeneID 831738; -.
GenomeReviews BA000015_GR; AT5G01410.
KEGG ath:AT5G01410; -.
NMPDR fig|3702.1.peg.22207; -.
Other
ProtoNet Q8L940.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; Cytoplasm; Membrane; Pyridoxine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   309  309     Pyridoxal biosynthesis protein PDX1.3. PRO_0000109368
MUTAGEN   54    54        G->S: In rsr4-1; strongly reduced oligomerization and 63% reduction in pyridoxal biosynthesis. 
CONFLICT   226   226        F -> S (in Ref. 5; AAM66972). 
Sequence information
Length: 309 AA [This is the length of the unprocessed precursor] Molecular weight: 33216 Da [This is the MW of the unprocessed precursor] CRC64: E74EBBCD4F124456 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEGTGVVAVY GNGAITEAKK SPFSVKVGLA QMLRGGVIMD VVNAEQARIA EEAGACAVMA 

        70         80         90        100        110        120 
LERVPADIRA QGGVARMSDP QMIKEIKQAV TIPVMAKARI GHFVEAQILE AIGIDYIDES 

       130        140        150        160        170        180 
EVLTLADEDH HINKHNFRIP FVCGCRNLGE ALRRIREGAA MIRTKGEAGT GNIIEAVRHV 

       190        200        210        220        230        240 
RSVNGDIRVL RNMDDDEVFT FAKKLAAPYD LVMQTKQLGR LPVVQFAAGG VATPADAALM 

       250        260        270        280        290        300 
MQLGCDGVFV GSGIFKSGDP ARRARAIVQA VTHYSDPEML VEVSCGLGEA MVGINLNDEK 


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