ID   Q9A1N4_STRP1            Unreviewed;       234 AA.
AC   Q9A1N4; Q491E6;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 130.
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:AAK33279.1};
GN   OrderedLocusNames=SPy_0179 {ECO:0000313|EMBL:AAK33279.1};
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447 {ECO:0000313|EMBL:AAK33279.1, ECO:0000313|Proteomes:UP000000750};
RN   [1] {ECO:0000313|EMBL:AAK33279.1, ECO:0000313|Proteomes:UP000000750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1
RC   {ECO:0000313|Proteomes:UP000000750};
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Adjic D., Savic D., Savic G., Lyon K.,
RA   Primeaux C., Sezate S.S., Surorov A.N., Kenton S., Lai H., Lin S., Qian Y.,
RA   Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(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; AE004092; AAK33279.1; -; Genomic_DNA.
DR   RefSeq; NP_268558.1; NC_002737.2.
DR   AlphaFoldDB; Q9A1N4; -.
DR   PaxDb; 1314-HKU360_00198; -.
DR   KEGG; spy:SPy_0179; -.
DR   PATRIC; fig|160490.10.peg.157; -.
DR   HOGENOM; CLU_006033_5_0_9; -.
DR   OMA; PCVLTMM; -.
DR   Proteomes; UP000000750; Chromosome.
DR   GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-EC.
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:AAK33279.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000750}.
FT   DOMAIN          10..200
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   234 AA;  26158 MW;  8E17505DFE5EBB4B CRC64;
     MAKNLQEMRE RVCAANKSLP QHGLVKFTWG NVSEVCRELG RIVIKPSGVD YDLLTPENMV
     VTDLDGNVVE GDLNPSSDLP THVELYKAWP EVGGIVHTHS TEAVGWAQAG RDIPFYGTTH
     ADYFYGPVPC ARSLTKAEVD GAYEQETGNV ILEEFSKRGL DPMAVPGIVV RNHGPFTWGK
     TPEQAVYHSV VLEEVARMNR LTEQINPRVE PAPRYIMDKH YLRKHGPNAY YGQK
//