ID   PDX12_ARATH             Reviewed;         314 AA.
AC   Q9ZNR6; Q0WS48;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   22-JUL-2008, entry version 56.
DE   RecName: Full=Probable pyridoxal biosynthesis protein PDX1.2;
DE            Short=AtPDX1.2;
DE            Short=AtPDX1;3;
GN   Name=PDX12; Synonyms=A37, PDX1L2; OrderedLocusNames=At3g16050;
GN   ORFNames=MSL1.3;
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   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RA   Oekresz L., Mathe C., Horvath E., Schell J., Koncz C., Szabados L.;
RT   "T-DNA trapping of a cryptic promoter identifies an ortholog of highly
RT   conserved SNZ growth arrest response genes in Arabidopsis.";
RL   Plant Sci. 138:217-228(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20277480; PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [3]
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   [4]
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   [5]
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).
RN   [6]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH PDX1.1 AND PDX1.3.
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).
CC   -!- FUNCTION: May be involved in the production of pyridoxal (vitamin
CC       B6) and indirect resistance to singlet oxygen-generating
CC       photosensitizers.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer or heterodimer with PDX1.1 or PDX1.3. No
CC       interaction with PDX2.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-1545987, EBI-1545987;
CC       O80448:PDX11; NbExp=1; IntAct=EBI-1545987, EBI-1545972;
CC       Q8L940:PDX13; NbExp=1; IntAct=EBI-1545987, EBI-1545956;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in callus tissues, flowers and
CC       roots. Weakly expressed in leaves and stems.
CC   -!- MISCELLANEOUS: Unlike PDX1.1 or PDX1.3, PDX1.2 is unable to
CC       interact with PDX2 and restore prototrophy in yeast snz1 mutants.
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; AF029980; AAD01897.1; -; mRNA.
DR   EMBL; AF029981; AAD01898.1; -; Genomic_DNA.
DR   EMBL; AB012247; BAB02670.1; -; Genomic_DNA.
DR   EMBL; BT003136; AAO24568.1; -; mRNA.
DR   EMBL; AK228092; BAF00051.1; -; mRNA.
DR   RefSeq; NP_188226.1; -.
DR   UniGene; At.7601; -.
DR   IntAct; Q9ZNR6; -.
DR   GeneID; 820850; -.
DR   GenomeReviews; BA000014_GR; AT3G16050.
DR   KEGG; ath:AT3G16050; -.
DR   NMPDR; fig|3702.1.peg.13774; -.
DR   GeneFarm; 3240; -.
DR   TAIR; At3g16050; -.
DR   ArrayExpress; Q9ZNR6; -.
DR   GermOnline; AT3G16050; Arabidopsis thaliana.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR   InterPro; IPR001852; Snz1p/Sor1.
DR   Pfam; PF01680; SOR_SNZ; 1.
DR   PIRSF; PIRSF029271; Pdx1; 1.
DR   ProDom; PD004958; Snz1p/Sor1; 1.
DR   PROSITE; PS01235; PDXS_SNZ_1; 1.
DR   PROSITE; PS51129; PDXS_SNZ_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Pyridoxine biosynthesis.
FT   CHAIN         1    314       Probable pyridoxal biosynthesis protein
FT                                PDX1.2.
FT                                /FTId=PRO_0000109367.
SQ   SEQUENCE   314 AA;  33836 MW;  D894BC393CBBBA6A CRC64;
     MADQAMTDQD QGAVTLYSGT AITDAKKNHP FSVKVGLAQV LRGGAIVEVS SVNQAKLAES
     AGACSVIVSD PVRSRGGVRR MPDPVLIKEV KRAVSVPVMA RARVGHFVEA QILESLAVDY
     IDESEIISVA DDDHFINKHN FRSPFICGCR DTGEALRRIR EGAAMIRIQG DLTATGNIAE
     TVKNVRSLMG EVRVLNNMDD DEVFTFAKKI SAPYDLVAQT KQMGRVPVVQ FASGGITTPA
     DAALMMQLGC DGVFVGSEVF DGPDPFKKLR SIVQAVQHYN DPHVLAEMSS GLENAMESLN
     VRGDRIQDFG QGSV
//