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Database: UniProt
Entry: A0A3S3V8T8_9SPHI
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Original site: A0A3S3V8T8_9SPHI 
ID   A0A3S3V8T8_9SPHI        Unreviewed;       232 AA.
AC   A0A3S3V8T8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   08-OCT-2025, entry version 25.
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=EPL05_21430 {ECO:0000313|EMBL:RWY48142.1};
OS   Mucilaginibacter gilvus.
OC   Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC   Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=2305909 {ECO:0000313|EMBL:RWY48142.1, ECO:0000313|Proteomes:UP000286701};
RN   [1] {ECO:0000313|EMBL:RWY48142.1, ECO:0000313|Proteomes:UP000286701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F01003 {ECO:0000313|EMBL:RWY48142.1,
RC   ECO:0000313|Proteomes:UP000286701};
RA   Yan Y.-Q., Du Z.-J.;
RT   "Mucilaginibacter antarcticum sp. nov., isolated from antarctic soil.";
RL   Submitted (JAN-2019) 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}.
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:RWY48142.1}.
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DR   EMBL; SBIW01000012; RWY48142.1; -; Genomic_DNA.
DR   RefSeq; WP_128536035.1; NZ_SBIW01000012.1.
DR   AlphaFoldDB; A0A3S3V8T8; -.
DR   OrthoDB; 9786287at2; -.
DR   Proteomes; UP000286701; 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: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:UP000286701};
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;  25812 MW;  FB13585F4EB081D7 CRC64;
     MSQYQHIKQK AYEANMQLPK LGLVLFTFGN VSAADHDLGV FAIKPSGVPY EELSPEKMVI
     VDFDGNTVEG SHRPSSDTKT HAVLYKNWPK IGGIVHTHST YATAWAQSQR CIPIFGTTHA
     DHLTADIPCA PPMSDEMIQG DYEYQTGFQI IDHFTELGLS YEEVEMVLVG NHAPFTWGKT
     ADKAVYNSAV LESVAQMALL TEQINANAPR LKDALIKKHF ERKHGPDSYY GQ
//
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