ID   DRDI_BACCR              Reviewed;         347 AA.
AC   Q81IK7;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 101.
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=BC_0379;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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=AAP07419.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016877; AAP07419.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_830218.1; NC_004722.1.
DR   AlphaFoldDB; Q81IK7; -.
DR   SMR; Q81IK7; -.
DR   STRING; 226900.BC_0379; -.
DR   EnsemblBacteria; AAP07419; AAP07419; BC_0379.
DR   KEGG; bce:BC0379; -.
DR   PATRIC; fig|226900.8.peg.351; -.
DR   HOGENOM; CLU_016218_1_2_9; -.
DR   OMA; RLWVDET; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..347
FT                   /note="5-deoxyribose 1-phosphate isomerase"
FT                   /id="PRO_0000357144"
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;  38349 MW;  B0EE6EA4618AFD44 CRC64;
     MEEQLIPIQW KDDALVLLDQ TLLPNEIVYE SFKTAESVWD AIQVMKVRGA PAIGVSAAYG
     VYLGIKEFAE STEEGFMDEV RKVCTYLATS RPTAVNLFWA LERMESVATD NIHLSISQLK
     NRLLEEAKEI HREDEEINRQ IGEHALTLFH DGMGVLTHCN AGALATTKYG TATAPMYLAK
     EKGWDLKIYS DETRPRLQGS TLTALELQRA GIDVTVITDN MAAMVMSQGK IDAVIVGCDR
     VAANGDVANK IGTLGVSILA KYYNIPFYVA APTPTIDLKT STGKEIPIEE RDASEVINRF
     GKYSAPKESK VYNPAFDVTP HENVTAIITE KGIVKAPFTE NLKKLFQ