ID   ARAD_HALH5              Reviewed;         231 AA.
AC   Q9KBQ4;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-SEP-2026, entry version 122.
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; OrderedLocusNames=BH1871;
OS   Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Halalkalibacterium (ex Joshi et al. 2022).
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05590.1; -; Genomic_DNA.
DR   PIR; G83883; G83883.
DR   RefSeq; WP_010898032.1; NC_002570.2.
DR   AlphaFoldDB; Q9KBQ4; -.
DR   SMR; Q9KBQ4; -.
DR   STRING; 272558.gene:10727769; -.
DR   KEGG; bha:BH1871; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_006033_5_0_9; -.
DR   OrthoDB; 9786287at2; -.
DR   UniPathway; UPA00145; UER00567.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:TreeGrafter.
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 D-xylulose 5-phosphate; ISS:UniProtKB.
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   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   NCBIfam; TIGR00760; araD; 1.
DR   NCBIfam; NF006047; PRK08193.1; 1.
DR   NCBIfam; NF009003; PRK12348.1; 1.
DR   PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR22789:SF8; L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE SGBE; 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_0000162916"
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   231 AA;  25991 MW;  6CA570D2A6B4DB97 CRC64;
     MLEQLKETVF KANLYLPKYQ LVTFTWGNVS GIDREKGLVV IKPSGVEYFE MKSKDMVVVD
     LEGNIVEGDL KPSSDTPTHL ALYRAFDKVG GIVHTHSVWA TAWAQAGKEI PAYGTTHADY
     FHGTIPCTRP MTETEILGDY EKETGNVIVE TFRNKDPMSI PGVLVHSHAP FVWGKDPMEA
     VHHAVVLEEV AKMAQKTLSI SERTLPMDSV LLDRHFYRKH GQAAYYGQEK R
//