ARAD_SALTY
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 03-AUG-2022, entry version 138.
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}; OrderedLocusNames=STM0101;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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;
CC Evidence={ECO:0000255|HAMAP-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};
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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; P06190; -.
DR EnsemblBacteria; AAL19065; AAL19065; STM0101.
DR GeneID; 1251619; -.
DR KEGG; stm:STM0101; -.
DR PATRIC; fig|99287.12.peg.104; -.
DR HOGENOM; CLU_006033_5_0_6; -.
DR OMA; PIFGTTH; -.
DR PhylomeDB; P06190; -.
DR BioCyc; SENT99287:STM0101-MON; -.
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 xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.225.10; -; 1.
DR HAMAP; MF_00989; AraD_entero; 1.
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 Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR00760; araD; 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
