ID   PDX13_ARATH             Reviewed;         309 AA.
AC   Q8L940; Q3KRU4; Q9M032;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   25-NOV-2008, entry version 46.
DE   RecName: Full=Pyridoxal biosynthesis protein PDX1.3;
DE            Short=AtPDX1.3;
DE            Short=AtPDX1;1;
GN   Name=PDX13; Synonyms=GIP2, PDX1L3, RSR4; OrderedLocusNames=At5g01410;
GN   ORFNames=T10O8.120;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16236150; DOI=10.1111/j.1365-313X.2005.02538.x;
RA   Chen H., Xiong L.;
RT   "Pyridoxine is required for post-embryonic root development and
RT   tolerance to osmotic and oxidative stresses.";
RL   Plant J. 44:396-408(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-54, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH PDX1.1, PDX1.2 AND PDX2.
RC   STRAIN=cv. C24;
RX   PubMed=16766694; DOI=10.1105/tpc.105.036269;
RA   Wagner S., Bernhardt A., Leuendorf J.E., Drewke C., Lytovchenko A.,
RA   Mujahed N., Gurgui C., Frommer W.B., Leistner E., Fernie A.R.,
RA   Hellmann H.;
RT   "Analysis of the Arabidopsis rsr4-1/pdx1-3 mutant reveals the critical
RT   function of the PDX1 protein family in metabolism, development, and
RT   vitamin B6 biosynthesis.";
RL   Plant Cell 18:1722-1735(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016721; PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16157873; DOI=10.1073/pnas.0506228102;
RA   Tambasco-Studart M., Titiz O., Raschle T., Forster G., Amrhein N.,
RA   Fitzpatrick T.B.;
RT   "Vitamin B6 biosynthesis in higher plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13687-13692(2005).
CC   -!- FUNCTION: Involved in the production of pyridoxal (vitamin B6).
CC       Also plays an indirect role in osmotic or salt tolerance, and in
CC       resistance to singlet oxygen-generating photosensitizers.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer or heterodimer with PDX1.1 or PDX1.2. Interacts
CC       with PDX2.
CC   -!- INTERACTION:
CC       Q9ZNR6:PDX12; NbExp=1; IntAct=EBI-1545956, EBI-1545987;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in cotyledons, rapidly dividing root
CC       stele tissues, stems, leaves, flowers, mature pollen, and
CC       siliques.
CC   -!- INDUCTION: Not induced by cold, salt, drought or UV stress, or by
CC       abscisic acid or jasmonic acid.
CC   -!- MISCELLANEOUS: Loss-of-function mutants (T-DNA insertion) have a
CC       lower leaf carotenoid and chlorophyll a and b content, and are
CC       impaired both in root cell division and in root cell elongation.
CC       Mutant rsr4-1 can be complemented by the addition of any of the
CC       vitamin B6 vitamers, except pyridoxal 5'-phosphate.
CC   -!- MISCELLANEOUS: In plants, synthesis of vitamin B6 does not involve
CC       deoxyxylulose 5-phosphate but utilizes intermediates from the
CC       pentose phosphate pathway and from glycolysis.
CC   -!- MISCELLANEOUS: Vitamin B6 is an essential quencher of singlet
CC       oxygen in plants, that can protect cellular membranes from lipid
CC       peroxidation.
CC   -!- SIMILARITY: Belongs to the pdxS/SNZ family.
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DR   EMBL; AY972813; AAY42123.1; -; mRNA.
DR   EMBL; AL161746; CAB81924.1; -; Genomic_DNA.
DR   EMBL; AF428298; AAL16130.1; -; mRNA.
DR   EMBL; AF446352; AAL48227.1; -; mRNA.
DR   EMBL; AY097428; AAM19944.1; -; mRNA.
DR   EMBL; AY088650; AAM66972.1; -; mRNA.
DR   EMBL; AK227197; BAE99236.1; -; mRNA.
DR   PIR; T48163; T48163.
DR   RefSeq; NP_195761.1; -.
DR   UniGene; At.23386; -.
DR   IntAct; Q8L940; -.
DR   ProMEX; Q8L940; -.
DR   GeneID; 831738; -.
DR   GenomeReviews; BA000015_GR; AT5G01410.
DR   KEGG; ath:AT5G01410; -.
DR   NMPDR; fig|3702.1.peg.22207; -.
DR   TAIR; At5g01410; -.
DR   ArrayExpress; Q8L940; -.
DR   GermOnline; AT5G01410; Arabidopsis thaliana.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001852; Snz1p/Sor1.
DR   Pfam; PF01680; SOR_SNZ; 1.
DR   PIRSF; PIRSF029271; Pdx1; 1.
DR   ProDom; PD004958; Snz1p/Sor1; 1.
DR   TIGRFAMs; TIGR00343; Snz1p/Sor1; 1.
DR   PROSITE; PS01235; PDXS_SNZ_1; 1.
DR   PROSITE; PS51129; PDXS_SNZ_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Cytoplasm; Membrane;
KW   Pyridoxine biosynthesis.
FT   CHAIN         1    309       Pyridoxal biosynthesis protein PDX1.3.
FT                                /FTId=PRO_0000109368.
FT   MUTAGEN      54     54       G->S: In rsr4-1; strongly reduced
FT                                oligomerization and 63% reduction in
FT                                pyridoxal biosynthesis.
FT   CONFLICT    226    226       F -> S (in Ref. 5; AAM66972).
SQ   SEQUENCE   309 AA;  33216 MW;  E74EBBCD4F124456 CRC64;
     MEGTGVVAVY GNGAITEAKK SPFSVKVGLA QMLRGGVIMD VVNAEQARIA EEAGACAVMA
     LERVPADIRA QGGVARMSDP QMIKEIKQAV TIPVMAKARI GHFVEAQILE AIGIDYIDES
     EVLTLADEDH HINKHNFRIP FVCGCRNLGE ALRRIREGAA MIRTKGEAGT GNIIEAVRHV
     RSVNGDIRVL RNMDDDEVFT FAKKLAAPYD LVMQTKQLGR LPVVQFAAGG VATPADAALM
     MQLGCDGVFV GSGIFKSGDP ARRARAIVQA VTHYSDPEML VEVSCGLGEA MVGINLNDEK
     VERFANRSE
//