ID A0A7D4UDQ9_9SPHI Unreviewed; 232 AA.
AC A0A7D4UDQ9;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 08-OCT-2025, entry version 16.
DE RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000256|ARBA:ARBA00013186};
DE EC=5.1.3.4 {ECO:0000256|ARBA:ARBA00013186};
GN ORFNames=HQ865_14350 {ECO:0000313|EMBL:QKJ30879.1};
OS Mucilaginibacter mali.
OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=2740462 {ECO:0000313|EMBL:QKJ30879.1, ECO:0000313|Proteomes:UP000505355};
RN [1] {ECO:0000313|EMBL:QKJ30879.1, ECO:0000313|Proteomes:UP000505355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G2-14 {ECO:0000313|EMBL:QKJ30879.1,
RC ECO:0000313|Proteomes:UP000505355};
RA Kim H.S., Lee K.C., Suh M.K., Kim J.-S., Han K.-I., Eom M.K., Shin Y.K.,
RA Lee J.-S.;
RT "Mucilaginibacter mali sp. nov.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
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; CP054139; QKJ30879.1; -; Genomic_DNA.
DR RefSeq; WP_173415549.1; NZ_CP054139.1.
DR AlphaFoldDB; A0A7D4UDQ9; -.
DR KEGG; mmab:HQ865_14350; -.
DR Proteomes; UP000505355; 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-ARBA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019323; P:pentose catabolic process; IEA:TreeGrafter.
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 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:UP000505355};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 9..199
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 232 AA; 26069 MW; 15BC6090FFF06E3B CRC64;
MSIYKRIQEE AYEANMQLPK LGLVLFTFGN VSAVDREREV FAIKPSGVAY DDLTPEKMVI
VDFDANVIQG ELRPSSDTKT HAVLYKHMPS IGGIVHTHST YATAWAQSQR DIPIYGTTHA
DYNTVNIPCA PPMSDEMIAG NYEYQTGFQI LNCLQEKGMD YREVEMILVG NHAPFTWGKS
ADKAVHNSAV LECVAKMALL TEQINPQAPR LQDSLIRKHF ERKHGPDSYY GQ
//
