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Database: UniProt
Entry: A0A1G1BWP3_9BACT
LinkDB: A0A1G1BWP3_9BACT
Original site: A0A1G1BWP3_9BACT 
ID   A0A1G1BWP3_9BACT        Unreviewed;       243 AA.
AC   A0A1G1BWP3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-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   Name=araD {ECO:0000313|EMBL:OGV87204.1};
GN   ORFNames=A3K19_12870 {ECO:0000313|EMBL:OGV87204.1};
OS   Lentisphaerae bacterium RIFOXYB12_FULL_65_16.
OC   Bacteria; Lentisphaerota.
OX   NCBI_TaxID=1798581 {ECO:0000313|EMBL:OGV87204.1, ECO:0000313|Proteomes:UP000179250};
RN   [1] {ECO:0000313|EMBL:OGV87204.1, ECO:0000313|Proteomes:UP000179250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGV87204.1}.
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DR   EMBL; MHBP01000274; OGV87204.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1BWP3; -.
DR   Proteomes; UP000179250; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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;
FT   DOMAIN          12..201
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   243 AA;  25876 MW;  CCE353B3B547F394 CRC64;
     MKTPPELQAL RKDVLAAHRF LCEQGLAVLT WGNVSGIHRA SGVVAIKPSG VAYDELTVDN
     IVLVELDGGR VLTDDLRPSS DLPTHLALYR AFPQIGGVAH THSRHATAFA QACRSLPCLG
     TTHADHFCGT IPVTRPLRSA ETAKDYESNT GQVIIETFRD KNPVALPAVL VAHHAPFTWG
     DSPAAAVCNS VVLEAVAGMA LETWQLDPAK AGIPADLQRC HFLRKHGPAA HYGQPQGPAA
     AIS
//
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