DRDI_BACMK
ID DRDI_BACMK Reviewed; 347 AA.
AC A9VRK3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 81.
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};
GN OrderedLocusNames=BcerKBAB4_0327;
OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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=ABY41593.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000903; ABY41593.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_016103220.1; NC_010184.1.
DR AlphaFoldDB; A9VRK3; -.
DR SMR; A9VRK3; -.
DR STRING; 315730.BcerKBAB4_0327; -.
DR EnsemblBacteria; ABY41593; ABY41593; BcerKBAB4_0327.
DR KEGG; bwe:BcerKBAB4_0327; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_9; -.
DR OMA; RLWVDET; -.
DR Proteomes; UP000002154; 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_0000357155"
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; 38129 MW; 9FACF0126D560CD7 CRC64;
MAEQLIPIQW KDDALVLLDQ TVLPNEVVYE SFKTAEGVWD AIQVMKVRGA PAIGVSAAYG
VYLGVKEVAE SSAEEFIAEV KKVCAYLATS RPTAVNLFWA LERMESVAKE NAHLSIAQLK
DRLLEEAKEI HREDEEINRQ IGEHALTLFH DGMGVLTHCN AGALATTKYG TATAPMYLAK
EKGWDLKIYS DETRPRLQGS TLTALELQRA GIDVTVITDN MAAMVMSQGK IDAVIVGCDR
VAANGDVANK IGTLGVSILA KYYNIPFYVA APTPTIDLKT PTGKEIPIEE RDASEVINRF
GQYSAPKESK VYNPAFDVTP YENVTAIITE KGIVRAPFME NLKKLFQ