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Database: UniProt
Entry: E3C5P0_9LACO
LinkDB: E3C5P0_9LACO
Original site: E3C5P0_9LACO 
ID   E3C5P0_9LACO            Unreviewed;       243 AA.
AC   E3C5P0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
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:EFQ53953.1};
GN   ORFNames=HMPREF9265_1949 {ECO:0000313|EMBL:EFQ53953.1};
OS   Limosilactobacillus oris PB013-T2-3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=908339 {ECO:0000313|EMBL:EFQ53953.1, ECO:0000313|Proteomes:UP000003070};
RN   [1] {ECO:0000313|EMBL:EFQ53953.1, ECO:0000313|Proteomes:UP000003070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB013-T2-3 {ECO:0000313|EMBL:EFQ53953.1,
RC   ECO:0000313|Proteomes:UP000003070};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) 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:EFQ53953.1}.
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DR   EMBL; AEKL01000007; EFQ53953.1; -; Genomic_DNA.
DR   RefSeq; WP_003711408.1; NZ_AEKL01000007.1.
DR   AlphaFoldDB; E3C5P0; -.
DR   GeneID; 78173951; -.
DR   eggNOG; COG0235; Bacteria.
DR   OrthoDB; 9786287at2; -.
DR   Proteomes; UP000003070; Unassembled WGS sequence.
DR   GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-EC.
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   Isomerase {ECO:0000313|EMBL:EFQ53953.1}.
FT   DOMAIN          7..197
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   243 AA;  27256 MW;  963B0030C126741F CRC64;
     MLEELKQEVY EANMKLPKLG LVTFTWGNVS GIDREKGLFV IKPSGVPYEE LKPSDMVVVN
     LDGEVVEGDL NPSSDTPTHT YLYNHFPKIG GIVHTHSPWA VSFAAAHMDI PAMNTTHADT
     FYTDVPAADA LTKEEIEEDY EGNTGKVIVR SFKERGLDYE ATPAALVMQH GPFAWGPTPD
     KAVYNAKVLE VVAEEDYHTL QLTRADNHLP QYLLDKHYYR KHGANAYYGQ NNAHSKDHAK
     REN
//
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