ID   ARAD_GEOSE              Reviewed;         228 AA.
AC   Q9S469;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000250|UniProtKB:P08203};
DE            EC=5.1.3.4 {ECO:0000250|UniProtKB:P08203};
DE   AltName: Full=Phosphoribulose isomerase {ECO:0000250|UniProtKB:P08203};
GN   Name=araD;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T-6;
RA   Gilead-Gropper S., Shoham Y.;
RT   "The L-arabinose utilization gene cluster from Bacillus stearothermophilus
RT   T-6.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P08203}.
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:0000250|UniProtKB:P08203};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P08203};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08203};
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:0000250|UniProtKB:P08203}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC       subfamily. {ECO:0000250|UniProtKB:P08203}.
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DR   EMBL; AF160811; AAD45716.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S469; -.
DR   SMR; Q9S469; -.
DR   UniPathway; UPA00145; UER00567.
DR   GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; ISS:UniProtKB.
DR   Gene3D; 3.40.225.10; -; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   InterPro; IPR004661; AraD.
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   Zinc.
FT   CHAIN           1..228
FT                   /note="L-ribulose-5-phosphate 4-epimerase"
FT                   /id="PRO_0000162917"
FT   ACT_SITE        119
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
FT   ACT_SITE        226
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
FT   BINDING         27..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         44..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         73..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P08203"
SQ   SEQUENCE   228 AA;  25227 MW;  66EEC1746D950C84 CRC64;
     MLEELKQAVL EANLQLPQYR LVTFTWGNVS GIDRERGLVV IKPSGVAYDK LTIDDMVVVD
     LTGNVVEGDL KPSSDTPTHL WLYKQFPGIG GIVHTHSTWA TVWAQAGKGI PALGTTHADY
     FYGEIPCTRP MTNEEIQGAY ELETGKVITE TFRFLDPLQM PGVLVHGHGP FAWGKDPANA
     VHNAVVLEEV AKMAARTYML NPNAKPISQT LLDRHYLRKH GANAYYGQ