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Database: UniProt
Entry: A0A1Y4TTS2_9FIRM
LinkDB: A0A1Y4TTS2_9FIRM
Original site: A0A1Y4TTS2_9FIRM 
ID   A0A1Y4TTS2_9FIRM        Unreviewed;       231 AA.
AC   A0A1Y4TTS2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000256|ARBA:ARBA00013186};
DE            EC=5.1.3.4 {ECO:0000256|ARBA:ARBA00013186};
DE   AltName: Full=Phosphoribulose isomerase {ECO:0000256|ARBA:ARBA00032206};
GN   ORFNames=B5E62_14905 {ECO:0000313|EMBL:OUQ47966.1};
OS   Lachnoclostridium sp. An118.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1965547 {ECO:0000313|EMBL:OUQ47966.1, ECO:0000313|Proteomes:UP000199786};
RN   [1] {ECO:0000313|Proteomes:UP000199786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An118 {ECO:0000313|Proteomes:UP000199786};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUQ47966.1}.
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DR   EMBL; NFLQ01000023; OUQ47966.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4TTS2; -.
DR   OrthoDB; 9786287at2; -.
DR   Proteomes; UP000199786; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   CDD; cd00398; Aldolase_II; 1.
DR   Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
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   Reference proteome {ECO:0000313|Proteomes:UP000199786}.
FT   DOMAIN          7..197
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   231 AA;  26006 MW;  A4C082BF208D2C2E CRC64;
     MLEELKKEVY EANMLLPKYE LVTFTWGNVS GIDREKGLFV IKPSGVDYDK LTPDDMVVVD
     LDGNKVEGRY NPSSDTATHV VLYNRFPNIG GIVHTHSPWA TSWAQAGRDI PCYGTTHADY
     IYGEVPCVRN LTKEEIEEAY EKNTGVLIAD EFEKRGKDYI AVPAVLCKNH GPFTWGKDAH
     EAVHNAVVLE EVAKMAARCE MINPENGPAP QELQDKHYYR KHGANAYYGQ K
//
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