AXS1_ARATH
ID AXS1_ARATH Reviewed; 389 AA.
AC Q9ZUY6;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=UDP-D-apiose/UDP-D-xylose synthase 1;
GN Name=AXS1; OrderedLocusNames=At2g27860; ORFNames=F15K20.4;
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 [MRNA], FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=12969423; DOI=10.1046/j.1365-313x.2003.01841.x;
RA Molhoj M., Verma R., Reiter W.D.;
RT "The biosynthesis of the branched-chain sugar d-apiose in plants:
RT functional cloning and characterization of a UDP-d-apiose/UDP-d-xylose
RT synthase from Arabidopsis.";
RL Plant J. 35:693-703(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Xiao Y.-L., Underwood B.A., Moskal W.A. Jr., Wang W., Redman J.C., Wu H.C.,
RA Utterback T., Town C.D.;
RT "Reconstruction of cDNA sequences for hypothetical genes in Arabidopsis
RT thaliana from 5' and 3' RACE products.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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.
CC {ECO:0000269|PubMed:12969423}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:12969423};
CC -!- ACTIVITY REGULATION: Inhibited by UDP-D-galacturonate.
CC {ECO:0000269|PubMed:12969423}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for UDP-D-glucuronate {ECO:0000269|PubMed:12969423};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:12969423};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12969423}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12969423}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AY442191; AAR14687.1; -; mRNA.
DR EMBL; AC005824; AAC73015.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08054.1; -; Genomic_DNA.
DR EMBL; AF361574; AAK32742.1; -; mRNA.
DR EMBL; BT001016; AAN46770.1; -; mRNA.
DR EMBL; AY735589; AAU44459.1; -; mRNA.
DR EMBL; AY924751; AAX23826.1; -; mRNA.
DR EMBL; AY086830; AAM63878.1; -; mRNA.
DR PIR; G84677; G84677.
DR RefSeq; NP_180353.1; NM_128345.4.
DR PDB; 6H0N; X-ray; 3.02 A; A/B=1-389.
DR PDB; 6H0P; X-ray; 3.47 A; A/B=1-389.
DR PDBsum; 6H0N; -.
DR PDBsum; 6H0P; -.
DR AlphaFoldDB; Q9ZUY6; -.
DR SMR; Q9ZUY6; -.
DR BioGRID; 2682; 14.
DR STRING; 3702.AT2G27860.1; -.
DR iPTMnet; Q9ZUY6; -.
DR PaxDb; Q9ZUY6; -.
DR PRIDE; Q9ZUY6; -.
DR ProteomicsDB; 241163; -.
DR EnsemblPlants; AT2G27860.1; AT2G27860.1; AT2G27860.
DR GeneID; 817332; -.
DR Gramene; AT2G27860.1; AT2G27860.1; AT2G27860.
DR KEGG; ath:AT2G27860; -.
DR Araport; AT2G27860; -.
DR TAIR; locus:2041974; AT2G27860.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_7_0_1; -.
DR InParanoid; Q9ZUY6; -.
DR OMA; ISAMTIC; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q9ZUY6; -.
DR BioCyc; ARA:AT2G27860-MON; -.
DR BioCyc; MetaCyc:AT2G27860-MON; -.
DR PRO; PR:Q9ZUY6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUY6; baseline and differential.
DR Genevisible; Q9ZUY6; AT.
DR GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0051287; F:NAD binding; IDA:TAIR.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IDA:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009226; P:nucleotide-sugar biosynthetic process; IDA:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Cytoplasm; NAD;
KW Reference proteome.
FT CHAIN 1..389
FT /note="UDP-D-apiose/UDP-D-xylose synthase 1"
FT /id="PRO_0000423717"
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 STRAND 10..12
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:6H0N"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:6H0N"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:6H0N"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6H0N"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 183..202
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:6H0N"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 298..313
FT /evidence="ECO:0007829|PDB:6H0N"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 346..352
FT /evidence="ECO:0007829|PDB:6H0N"
FT HELIX 360..381
FT /evidence="ECO:0007829|PDB:6H0N"
SQ SEQUENCE 389 AA; 43638 MW; DE0D661A3BD2C359 CRC64;
MANGANRVDL DGKPIQPLTI CMIGAGGFIG SHLCEKLLTE TPHKVLALDV YNDKIKHLLE
PDTVEWSGRI QFHRINIKHD SRLEGLVKMA DLIINLAAIC TPADYNTRPL DTIYSNFIDA
LPVVKYCSEN NKRLIHFSTC EVYGKTIGSF LPKDHPLRDD PAFYVLKEDI SPCIFGSIEK
QRWSYACAKQ LIERLVYAEG AENGLEFTIV RPFNWIGPRM DFIPGIDGPS EGVPRVLACF
SNNLLRREPL KLVDGGESQR TFVYINDAIE AVLLMIENPE RANGHIFNVG NPNNEVTVRQ
LAEMMTEVYA KVSGEGAIES PTVDVSSKEF YGEGYDDSDK RIPDMTIINR QLGWNPKTSL
WDLLESTLTY QHRTYAEAVK KATSKPVAS
