ID   Q65GC2_BACLD            Unreviewed;       228 AA.
AC   Q65GC2; Q62RS7;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 124.
DE   RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000256|ARBA:ARBA00074961, ECO:0000256|NCBIfam:TIGR00760};
DE            EC=5.1.3.4 {ECO:0000256|ARBA:ARBA00013186, ECO:0000256|NCBIfam:TIGR00760};
GN   Name=araD {ECO:0000313|EMBL:AAU24533.1};
GN   OrderedLocusNames=BL00350 {ECO:0000313|EMBL:AAU24533.1};
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU24533.1, ECO:0000313|Proteomes:UP000000606};
RN   [1] {ECO:0000313|EMBL:AAU24533.1, ECO:0000313|Proteomes:UP000000606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC   9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC   {ECO:0000313|Proteomes:UP000000606};
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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:0000256|ARBA:ARBA00053542}.
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:0000256|ARBA:ARBA00001726};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:0000256|ARBA:ARBA00060520}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC       subfamily. {ECO:0000256|ARBA:ARBA00010037}.
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DR   EMBL; CP000002; AAU24533.1; -; Genomic_DNA.
DR   RefSeq; WP_011198185.1; NC_006270.3.
DR   AlphaFoldDB; Q65GC2; -.
DR   STRING; 279010.BL00350; -.
DR   GeneID; 92860380; -.
DR   KEGG; bld:BLi03026; -.
DR   KEGG; bli:BL00350; -.
DR   PATRIC; fig|279010.13.peg.3088; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_006033_5_0_9; -.
DR   Proteomes; UP000000606; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0019572; P:L-arabinose catabolic process; IEA:InterPro.
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 {ECO:0000256|ARBA:ARBA00022935};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000606};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          7..195
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   228 AA;  25682 MW;  7D11CF3BD832E200 CRC64;
     MLESLKEQVL KANLQLEEYR LVTFTWGNVS GIDRENKLVV IKPSGVKYSD LKAEDLVVLN
     MDGEIVEGDL KPSSDTPTHL YLYRQFQSIG GIVHTHSPWA TSWAQSGKDI PSLGTTHADY
     YHGDIPCTRE MDPDEIRSQY ELNTGKVIVE TFRHLDPLAV PAVLVNNHGP FCWGKDALTA
     VHNAVVLEEV AKMAYRSLML NPSLKRIKSA LQDKHYFRKH GADAYYGQ
//