ARAE1_ARATH
ID ARAE1_ARATH Reviewed; 419 AA.
AC Q9SA77; Q570B0; Q8H7B9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=UDP-arabinose 4-epimerase 1 {ECO:0000305};
DE EC=5.1.3.5 {ECO:0000269|PubMed:12566589};
DE AltName: Full=UDP-D-xylose 4-epimerase 1 {ECO:0000305};
GN Name=MUR4 {ECO:0000303|PubMed:12566589};
GN OrderedLocusNames=At1g30620 {ECO:0000312|Araport:AT1G30620};
GN ORFNames=T5I8.7 {ECO:0000312|EMBL:AAD25749.1};
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, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTANTS MUR4-1 AND MUR4-3.
RX PubMed=12566589; DOI=10.1105/tpc.008425;
RA Burget E.G., Verma R., Moelhoej M., Reiter W.-D.;
RT "The biosynthesis of L-arabinose in plants: molecular cloning and
RT characterization of a Golgi-localized UDP-D-xylose 4-epimerase encoded by
RT the MUR4 gene of Arabidopsis.";
RL Plant Cell 15:523-531(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 175-419.
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., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a UDP-D-xylose 4-epimerase but lacks both UDP-D-
CC glucose and UDP-D-glucuronic acid 4-epimerase activities in vitro.
CC {ECO:0000269|PubMed:12566589}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-beta-L-arabinopyranose = UDP-alpha-D-xylose;
CC Xref=Rhea:RHEA:11320, ChEBI:CHEBI:57632, ChEBI:CHEBI:61457;
CC EC=5.1.3.5; Evidence={ECO:0000269|PubMed:12566589};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-L-arabinose biosynthesis;
CC UDP-L-arabinose from UDP-alpha-D-xylose: step 1/1.
CC {ECO:0000305|PubMed:12566589}.
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:12566589}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SA77-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: High expression in roots. Also found in leaves,
CC stems, flowers, and siliques. {ECO:0000269|PubMed:12566589}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94059.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY195742; AAO39213.1; -; mRNA.
DR EMBL; AF083751; AAN60309.1; -; mRNA.
DR EMBL; AC007060; AAD25749.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31251.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31252.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59489.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59490.1; -; Genomic_DNA.
DR EMBL; AY064973; AAL57628.1; -; mRNA.
DR EMBL; BT002614; AAO11530.1; -; mRNA.
DR EMBL; AF325108; AAK17176.1; -; mRNA.
DR EMBL; AK220800; BAD94059.1; ALT_INIT; mRNA.
DR PIR; E86431; E86431.
DR RefSeq; NP_001319115.1; NM_001332913.1. [Q9SA77-1]
DR RefSeq; NP_001321844.1; NM_001332916.1. [Q9SA77-1]
DR RefSeq; NP_001321845.1; NM_001332914.1. [Q9SA77-1]
DR RefSeq; NP_174350.2; NM_102799.6. [Q9SA77-1]
DR AlphaFoldDB; Q9SA77; -.
DR SMR; Q9SA77; -.
DR BioGRID; 25177; 2.
DR STRING; 3702.AT1G30620.1; -.
DR iPTMnet; Q9SA77; -.
DR PaxDb; Q9SA77; -.
DR PRIDE; Q9SA77; -.
DR ProteomicsDB; 244458; -. [Q9SA77-1]
DR EnsemblPlants; AT1G30620.1; AT1G30620.1; AT1G30620. [Q9SA77-1]
DR EnsemblPlants; AT1G30620.2; AT1G30620.2; AT1G30620. [Q9SA77-1]
DR EnsemblPlants; AT1G30620.4; AT1G30620.4; AT1G30620. [Q9SA77-1]
DR EnsemblPlants; AT1G30620.6; AT1G30620.6; AT1G30620. [Q9SA77-1]
DR GeneID; 839942; -.
DR Gramene; AT1G30620.1; AT1G30620.1; AT1G30620. [Q9SA77-1]
DR Gramene; AT1G30620.2; AT1G30620.2; AT1G30620. [Q9SA77-1]
DR Gramene; AT1G30620.4; AT1G30620.4; AT1G30620. [Q9SA77-1]
DR Gramene; AT1G30620.6; AT1G30620.6; AT1G30620. [Q9SA77-1]
DR KEGG; ath:AT1G30620; -.
DR Araport; AT1G30620; -.
DR TAIR; locus:2204639; AT1G30620.
DR eggNOG; KOG1371; Eukaryota.
DR InParanoid; Q9SA77; -.
DR OMA; DGELGEW; -.
DR PhylomeDB; Q9SA77; -.
DR BioCyc; ARA:AT1G30620-MON; -.
DR BioCyc; MetaCyc:AT1G30620-MON; -.
DR BRENDA; 5.1.3.5; 399.
DR UniPathway; UPA00797; UER00772.
DR UniPathway; UPA00963; -.
DR PRO; PR:Q9SA77; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA77; baseline and differential.
DR Genevisible; Q9SA77; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050373; F:UDP-arabinose 4-epimerase activity; IDA:TAIR.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:InterPro.
DR GO; GO:0019567; P:arabinose biosynthetic process; IMP:TAIR.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
DR GO; GO:0033358; P:UDP-L-arabinose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01179; galE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carbohydrate metabolism; Golgi apparatus; Isomerase;
KW Membrane; NAD; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..419
FT /note="UDP-arabinose 4-epimerase 1"
FT /id="PRO_0000183229"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..419
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 72..103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MUTAGEN 275
FT /note="G->D: In mur4-1; 50% reduction in L-Ara in cell wall
FT material."
FT /evidence="ECO:0000269|PubMed:12566589"
FT MUTAGEN 304
FT /note="R->Q: In mur4-3; 50% reduction in L-Ara in cell wall
FT material."
FT /evidence="ECO:0000269|PubMed:12566589"
FT CONFLICT 155
FT /note="V -> G (in Ref. 2; AAN60309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46311 MW; 0F44E4B43EB5314D CRC64;
MFSFGRARSQ GRQNRSMSLG GLDYADPKKK NNYLGKILLT ASLTALCIFM LKQSPTFNTP
SVFSRHEPGV THVLVTGGAG YIGSHAALRL LKESYRVTIV DNLSRGNLAA VRILQELFPE
PGRLQFIYAD LGDAKAVNKI FTENAFDAVM HFAAVAYVGE STQFPLKYYH NITSNTLVVL
ETMAAHGVKT LIYSSTCATY GEPDIMPITE ETPQVPINPY GKAKKMAEDI ILDFSKNSDM
AVMILRYFNV IGSDPEGRLG EAPRPELREH GRISGACFDA ARGIMPGLQI KGTDYKTADG
TCVRDYIDVT DLVDAHVKAL QKAKPRKVGI YNVGTGKGSS VKEFVEACKK ATGVEIKIDY
LPRRAGDYAE VYSDPSKIRK ELNWTAKHTN LKESLETAWR WQKLHRNGYG LTTSSVSVY
