ID Q97JE5_CLOAB Unreviewed; 233 AA.
AC Q97JE5;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 100.
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:AAK79309.1};
GN OrderedLocusNames=CA_C1341 {ECO:0000313|EMBL:AAK79309.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK79309.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK79309.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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}.
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DR EMBL; AE001437; AAK79309.1; -; Genomic_DNA.
DR PIR; B97065; B97065.
DR RefSeq; NP_347969.1; NC_003030.1.
DR RefSeq; WP_010964650.1; NC_003030.1.
DR AlphaFoldDB; Q97JE5; -.
DR STRING; 272562.CA_C1341; -.
DR GeneID; 44997846; -.
DR KEGG; cac:CA_C1341; -.
DR PATRIC; fig|272562.8.peg.1546; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_5_0_9; -.
DR OrthoDB; 9786287at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019572; P:L-arabinose catabolic process; IEA:InterPro.
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 InterPro; IPR004661; AraD.
DR NCBIfam; TIGR00760; araD; 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 Reference proteome {ECO:0000313|Proteomes:UP000000814}.
FT DOMAIN 7..197
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 233 AA; 25923 MW; 675531875648AB90 CRC64;
MLEALKQEVL EANLMLPKYG LVVFTWGNVS GIDREKGLIV IKPSGVEYDQ MKASDMVVVD
LNGKVVEGDL NPSSDTPTHI VLYKEFSDIK GIVHTHSPWA TSFAQAGVSI PAAGTTHGDY
FYGNIPVTSR MTKEEIATDY EKQTGDVIVR TFRKENINPN DVPAVLVNDH APFTWGTDPK
NAVHNSVVLE EVAKMTYHSL QLNPHNIEMS QDLLDKHFKR KHGANAYYGQ KTK
//