ARAE4_ARATH
ID ARAE4_ARATH Reviewed; 436 AA.
AC Q9FI17;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative UDP-arabinose 4-epimerase 4;
DE EC=5.1.3.5;
DE AltName: Full=UDP-D-xylose 4-epimerase 4;
GN OrderedLocusNames=At5g44480; ORFNames=MFC16.15;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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).
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;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-L-arabinose biosynthesis;
CC UDP-L-arabinose from UDP-alpha-D-xylose: step 1/1.
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AB017065; BAB09155.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95113.1; -; Genomic_DNA.
DR RefSeq; NP_199261.1; NM_123815.1.
DR AlphaFoldDB; Q9FI17; -.
DR SMR; Q9FI17; -.
DR STRING; 3702.AT5G44480.1; -.
DR PaxDb; Q9FI17; -.
DR PRIDE; Q9FI17; -.
DR EnsemblPlants; AT5G44480.1; AT5G44480.1; AT5G44480.
DR GeneID; 834475; -.
DR Gramene; AT5G44480.1; AT5G44480.1; AT5G44480.
DR KEGG; ath:AT5G44480; -.
DR Araport; AT5G44480; -.
DR TAIR; locus:2163401; AT5G44480.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_1_10_1; -.
DR InParanoid; Q9FI17; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; Q9FI17; -.
DR BioCyc; ARA:AT5G44480-MON; -.
DR BRENDA; 5.1.3.5; 399.
DR UniPathway; UPA00797; UER00772.
DR UniPathway; UPA00963; -.
DR PRO; PR:Q9FI17; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI17; baseline and differential.
DR Genevisible; Q9FI17; AT.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050373; F:UDP-arabinose 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:InterPro.
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: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 3: Inferred from homology;
KW Carbohydrate metabolism; Golgi apparatus; Isomerase; Membrane; NAD;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..436
FT /note="Putative UDP-arabinose 4-epimerase 4"
FT /id="PRO_0000183232"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..436
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 96..127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 436 AA; 48345 MW; E8CCF469F31C9DF6 CRC64;
MLNSSGVRTQ RRSPRPLSLG GRKIITPTKF AYDHHNPDKV LDFVEMDCLE PKTKNNLTGK
LLLVASLLIL AIIVISQSSS FTSPSAFSQR EEGVTHVLVT GGAGYIGSHA ALRLLRDSYR
VTIVDNLSRG NLGAVKTLQQ LFPQTGRLQF IYADLGDPLA VEKIFSENAF DAVMHFAAVA
YVGESTLYPL KYYHNITSNT LGVLEAMARH KVKKLIYSST CATYGEPEKM PITEDTPQVP
INPYGKAKKM AEDMILDFSK NSDMAVMILR YFNVIGSDPG GRLGEAPRPE LREQGRISGA
CFDAARGFIP GLQVKGTDYK TSDGTCIRDY IDVTDLVDAH VKALEKAQPR KVGIYNVGTG
KGRSVKEFVE ACKKATGVEI KVDFLPRRPG DYAEVYSDPT KILKDLNWTA RFTNLQDSLQ
VAWRWQKIHP HGYNSY