ID   B0RIE2_CLASE            Unreviewed;       236 AA.
AC   B0RIE2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 88.
DE   RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000256|ARBA:ARBA00013186};
DE            EC=5.1.3.4 {ECO:0000256|ARBA:ARBA00013186};
GN   OrderedLocusNames=CMS0132 {ECO:0000313|EMBL:CAQ00256.1};
OS   Clavibacter sepedonicus (Clavibacter michiganensis subsp. sepedonicus).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ00256.1, ECO:0000313|Proteomes:UP000001318};
RN   [1] {ECO:0000313|EMBL:CAQ00256.1, ECO:0000313|Proteomes:UP000001318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / ICMP 2535 / C-1
RC   {ECO:0000313|Proteomes:UP000001318};
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
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   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC       subfamily. {ECO:0000256|ARBA:ARBA00010037}.
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DR   EMBL; AM849034; CAQ00256.1; -; Genomic_DNA.
DR   RefSeq; WP_012297614.1; NC_010407.1.
DR   AlphaFoldDB; B0RIE2; -.
DR   STRING; 31964.CMS0132; -.
DR   GeneID; 29472744; -.
DR   KEGG; cms:CMS0132; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_006033_3_0_11; -.
DR   OrthoDB; 9786287at2; -.
DR   Proteomes; UP000001318; 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-EC.
DR   GO; GO:0019323; P:pentose catabolic process; IEA:TreeGrafter.
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   NCBIfam; NF005123; PRK06557.1; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001318};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   236 AA;  25030 MW;  8048D192DFFD0350 CRC64;
     MSTYAPEIEV AVARVRSEVS RLHAELVRYG LVVWTGGNVS GRVPGADLFV IKPSGVSYDD
     LSPENMILCD LDGNVIPDTP GSRNAPSSDT AAHAYVYRNM PEVGGVVHTH STYAVAWAAR
     REPIPCVITA MADEFGGEIP VGPFAIIGDD SIGRGIVETL TGHRSRAVLM AGHGPFTIGK
     DAKDAVKAAV MVEDVARTVH ISRQLGEPAP LPADAVDALF DRYQNVYGQA PQGALK
//