AXS2_ARATH
ID AXS2_ARATH Reviewed; 389 AA.
AC Q9SGE0; Q8L9F5; Q94B32;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=UDP-D-apiose/UDP-D-xylose synthase 2;
GN Name=AXS2; OrderedLocusNames=At1g08200; ORFNames=T23G18.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA 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].
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.
CC -!- FUNCTION: Catalyzes the conversion of UDP-D-glucuronate to a mixture of
CC UDP-D-apiose and UDP-D-xylose. D-Apiose (3-C-hydroxymethyl-d-erythrose)
CC is the only plant cell wall monosaccharide with a branched carbon
CC skeleton and is found in rhamnogalacturonan II (RG-II),
CC apiogalacturonan, and several apioglycosides (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AC011438; AAF18254.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28260.1; -; Genomic_DNA.
DR EMBL; AY042880; AAK68820.1; -; mRNA.
DR EMBL; BT001220; AAN65107.1; -; mRNA.
DR EMBL; AY088462; AAM65998.1; -; mRNA.
DR PIR; C86216; C86216.
DR RefSeq; NP_563807.1; NM_100694.5.
DR AlphaFoldDB; Q9SGE0; -.
DR SMR; Q9SGE0; -.
DR BioGRID; 22582; 11.
DR STRING; 3702.AT1G08200.1; -.
DR iPTMnet; Q9SGE0; -.
DR PaxDb; Q9SGE0; -.
DR PRIDE; Q9SGE0; -.
DR ProteomicsDB; 240943; -.
DR EnsemblPlants; AT1G08200.1; AT1G08200.1; AT1G08200.
DR GeneID; 837341; -.
DR Gramene; AT1G08200.1; AT1G08200.1; AT1G08200.
DR KEGG; ath:AT1G08200; -.
DR Araport; AT1G08200; -.
DR TAIR; locus:2200018; AT1G08200.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_7_0_1; -.
DR InParanoid; Q9SGE0; -.
DR OMA; WIYSCAK; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q9SGE0; -.
DR BioCyc; ARA:AT1G08200-MON; -.
DR PRO; PR:Q9SGE0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGE0; baseline and differential.
DR Genevisible; Q9SGE0; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR CDD; cd05257; Arna_like_SDR_e; 1.
DR InterPro; IPR045869; Arna-like_SDR_e.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Cytoplasm; NAD; Reference proteome.
FT CHAIN 1..389
FT /note="UDP-D-apiose/UDP-D-xylose synthase 2"
FT /id="PRO_0000423718"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 49..80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185..189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 236..240
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253..260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 337..341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 319
FT /note="E -> D (in Ref. 4; AAM65998)"
FT /evidence="ECO:0000305"
FT CONFLICT 354..355
FT /note="WN -> CT (in Ref. 3; AAK68820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43790 MW; A3865CBEA04517E2 CRC64;
MANGADRLDL DGKPIKPMTI CMIGAGGFIG SHLCEKLMTE TPHKVLALDV YNDKIKHLLE
PDTVQWAGRI QFHRINIKHD SRLEGLIKMA DLTINLAAIC TPADYNTRPL DTIYSNFIDA
LPVVKYCSEN NKRLIHFSTC EVYGKTIGSF LPKDHPLRQD PEFYVLKEDI SPCIFGSIEK
QRWSYACAKQ LIERLVYAEG AENGLEFTIV RPFNWIGPRM DFIPGIDGPS EGVPRVLACF
SNNLLRREPL KLVDGGESQR TFIYIKDAIE AVLLMIENPE RANGHIFNVG NPNNEVTVRQ
LAEMMTEVYA KVSGETAIES PTIDVSSKEF YGEGYDDSDK RIPDMTIINR QLGWNPKTSL
WDLLESTLTY QHTTYAEAIK KATSKPVAS
