ID A0A136Q6J9_9FIRM Unreviewed; 229 AA.
AC A0A136Q6J9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 08-OCT-2025, entry version 29.
DE RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000256|ARBA:ARBA00074961};
DE EC=5.1.3.4 {ECO:0000256|ARBA:ARBA00013186};
DE AltName: Full=Phosphoribulose isomerase {ECO:0000256|ARBA:ARBA00032206};
GN ORFNames=HMPREF3293_00986 {ECO:0000313|EMBL:KXK66249.1};
OS Christensenella minuta.
OC Bacteria; Bacillati; Bacillota; Clostridia; Christensenellales;
OC Christensenellaceae; Christensenella.
OX NCBI_TaxID=626937 {ECO:0000313|EMBL:KXK66249.1, ECO:0000313|Proteomes:UP000070366};
RN [1] {ECO:0000313|EMBL:KXK66249.1, ECO:0000313|Proteomes:UP000070366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22607 {ECO:0000313|EMBL:KXK66249.1,
RC ECO:0000313|Proteomes:UP000070366};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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: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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXK66249.1}.
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DR EMBL; LSZW01000047; KXK66249.1; -; Genomic_DNA.
DR RefSeq; WP_066520464.1; NZ_CABMOF010000003.1.
DR AlphaFoldDB; A0A136Q6J9; -.
DR STRING; 626937.HMPREF3293_00986; -.
DR KEGG; cmiu:B1H56_01870; -.
DR PATRIC; fig|626937.4.peg.973; -.
DR OrthoDB; 9786287at2; -.
DR Proteomes; UP000070366; Unassembled WGS sequence.
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-ARBA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019568; P:arabinose catabolic process; IEA:UniProtKB-KW.
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 NCBIfam; NF006047; PRK08193.1; 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:UP000070366};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 7..193
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 229 AA; 25061 MW; D3B86DC0C5F488F1 CRC64;
MKDELKRRVY EANMLLPKYG LITFTWGNVS EREGDVVAIK PSGVEYDALR PEDIVLVGMD
GSILEDGLNP SSDLETHLEL YRNFEGVAGI THTHSEWATS WAQAGMDIPA AGTTHADYIY
GDVPCTRGLT PGEIRGAYEL NTGKVIVETF AGLDPLAVPC VLVKNHGPFT WGASAAESVR
NAVVLEQIAK MAFVGRTLQG GGPERMPQSL LDKHYLRKHG KNAYYGQKK
//
