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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//