ID   DRDI_BACAH              Reviewed;         347 AA.
AC   A0R946;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=5-deoxyribose 1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_02229};
DE            EC=5.3.1.- {ECO:0000255|HAMAP-Rule:MF_02229};
GN   Name=drdI {ECO:0000255|HAMAP-Rule:MF_02229}; OrderedLocusNames=BALH_0338;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam;
RX   PubMed=17337577; DOI=10.1128/jb.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA   McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
CC   -!- FUNCTION: Catalyzes the isomerization of 5-deoxy-alpha-D-ribose 1-
CC       phosphate to 5-deoxy-D-ribulose 1-phosphate, as part of a 5-deoxyribose
CC       salvage pathway that recycles this toxic radical SAM enzyme by-product
CC       to mainstream metabolites. {ECO:0000255|HAMAP-Rule:MF_02229}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-deoxy-alpha-D-ribose 1-phosphate = 5-deoxy-D-ribulose 1-
CC         phosphate; Xref=Rhea:RHEA:61296, ChEBI:CHEBI:58749,
CC         ChEBI:CHEBI:144504; Evidence={ECO:0000255|HAMAP-Rule:MF_02229};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61297;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02229};
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02229}.
CC   -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family.
CC       DrdI subfamily. {ECO:0000255|HAMAP-Rule:MF_02229}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK83739.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000485; ABK83739.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000392493.1; NC_008600.1.
DR   AlphaFoldDB; A0R946; -.
DR   SMR; A0R946; -.
DR   EnsemblBacteria; ABK83739; ABK83739; BALH_0338.
DR   GeneID; 45020403; -.
DR   KEGG; btl:BALH_0338; -.
DR   HOGENOM; CLU_016218_1_2_9; -.
DR   OMA; RLWVDET; -.
DR   Proteomes; UP000000761; Chromosome.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:InterPro.
DR   GO; GO:0019323; P:pentose catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.420; -; 1.
DR   Gene3D; 3.40.50.10470; -; 1.
DR   HAMAP; MF_02229; Deoxyribose1P_isomerase; 1.
DR   HAMAP; MF_01678; Salvage_MtnA; 1.
DR   InterPro; IPR043679; Deoxyribose1P_isomerase_DrdI.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR005251; IF-M1Pi.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR   InterPro; IPR027363; M1Pi_N.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR   TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase.
FT   CHAIN           1..347
FT                   /note="5-deoxyribose 1-phosphate isomerase"
FT                   /id="PRO_0000357151"
FT   ACT_SITE        239
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT   BINDING         48..50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT   BINDING         249..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
FT   SITE            159
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02229"
SQ   SEQUENCE   347 AA;  38307 MW;  B232E7BBBC5E031F CRC64;
     MEEQLIPIQW KDDALVLLDQ TLLPNEVVYE SFNTAEGVWD AIQVMKVRGA PAIGVSAAYG
     VYLGVKEFVE STEAEFIDEV KRVCAYLATS RPTAVNLFWA LERMESVATD HTHLSITQLK
     DRLLEEAKEI HREDEEINRQ IGEHALTLFH DGMGVLTHCN AGALATTKYG TATAPMYLAK
     EKGWDLKIYS DETRPRLQGS TLTALELQRA GIDVTVITDN MAAMVMSQGK IDAVIVGCDR
     VAANGDVANK IGTLGVSILA KYYNIPFYVA APTPTIDLKT PTGKEIPIEE RDASEVINRF
     GQYSAPKESK VYNPAFDVTP HENVTAIITE KGIVKAPFTE NLKKLFQ