ID ARAD_SALTY Reviewed; 231 AA. AC P06190; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 3. DT 28-JAN-2026, entry version 150. DE RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000255|HAMAP-Rule:MF_00989}; DE EC=5.1.3.4 {ECO:0000255|HAMAP-Rule:MF_00989}; DE AltName: Full=Phosphoribulose isomerase {ECO:0000255|HAMAP-Rule:MF_00989}; GN Name=araD {ECO:0000255|HAMAP-Rule:MF_00989}; GN OrderedLocusNames=STM0101; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2; RX PubMed=3891514; DOI=10.1016/0378-1119(85)90303-8; RA Lin H.-C., Lei S.-P., Studnicka G., Wilcox G.; RT "The araBAD operon of Salmonella typhimurium LT2. III. Nucleotide sequence RT of araD and its flanking regions, and primary structure of its product, L- RT ribulose-5-phosphate 4-epimerase."; RL Gene 34:129-134(1985). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). CC -!- FUNCTION: Involved in the degradation of L-arabinose. Catalyzes the CC interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5- CC phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond CC cleavage analogous to a class II aldolase reaction). CC {ECO:0000255|HAMAP-Rule:MF_00989}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate; CC Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226; CC EC=5.1.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00989}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00989}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00989}; CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L- CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): CC step 3/3. {ECO:0000255|HAMAP-Rule:MF_00989}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00989}. CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00989}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA27025.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M11047; AAA27025.1; ALT_FRAME; Genomic_DNA. DR EMBL; AE006468; AAL19065.1; -; Genomic_DNA. DR PIR; A24986; ISEB4T. DR RefSeq; NP_459106.1; NC_003197.2. DR RefSeq; WP_000888683.1; NC_003197.2. DR AlphaFoldDB; P06190; -. DR SMR; P06190; -. DR STRING; 99287.STM0101; -. DR PaxDb; 99287-STM0101; -. DR GeneID; 1251619; -. DR KEGG; stm:STM0101; -. DR PATRIC; fig|99287.12.peg.104; -. DR HOGENOM; CLU_006033_5_0_6; -. DR OMA; PCVLTMM; -. DR PhylomeDB; P06190; -. DR BioCyc; SENT99287:STM0101-MONOMER; -. DR UniPathway; UPA00145; UER00567. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central. DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0019569; P:L-arabinose catabolic process to D-xylulose 5-phosphate; IEA:UniProtKB-UniRule. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR CDD; cd00398; Aldolase_II; 1. DR FunFam; 3.40.225.10:FF:000001; L-ribulose-5-phosphate 4-epimerase UlaF; 1. DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1. DR HAMAP; MF_00989; AraD_entero; 1. DR InterPro; IPR050197; Aldolase_class_II_sugar_metab. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR036409; Aldolase_II/adducin_N_sf. DR InterPro; IPR004661; AraD. DR InterPro; IPR033748; AraD_entero. DR NCBIfam; TIGR00760; araD; 1. DR NCBIfam; NF006047; PRK08193.1; 1. DR NCBIfam; NF009002; PRK12347.1; 1. DR NCBIfam; NF009003; PRK12348.1; 1. DR PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR22789:SF15; L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE ARAD; 1. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1. PE 3: Inferred from homology; KW Arabinose catabolism; Carbohydrate metabolism; Isomerase; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1..231 FT /note="L-ribulose-5-phosphate 4-epimerase" FT /id="PRO_0000162920" FT ACT_SITE 120 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989" FT ACT_SITE 229 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989" FT BINDING 27..28 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989" FT BINDING 44..45 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989" FT BINDING 74..75 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989" FT BINDING 76 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989" FT BINDING 171 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989" SQ SEQUENCE 231 AA; 25531 MW; DA473505739284F9 CRC64; MLEDLKRQVL EANLALPKHN LVTLTWGNVS AVDRERGVLV IKPSGVDYSV MTADDMVVVS LESGEVVEGH KKPSSDTPTH RLLYQAFPTI GGIVHTHSRH ATIWAQAGQP IPATGTTHAD YFYGTIPCTR KMTEAEINGE YEWETGNVIV ETFEKQGIDA AQMPGVLVHS HGPFAWGKNA EDAVHNAIVL EEVAYMGIFC RQLAPQLPDM QQSLLDKHYL RKHGAKAYYG Q //