DRDI_BACAN
ID DRDI_BACAN Reviewed; 347 AA.
AC Q81ZC2; Q6I468; Q6KXX4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=BA_0347, GBAA_0347, BAS0332;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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=AAT52663.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016879; AAP24380.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29438.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT52663.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_842894.1; NC_003997.3.
DR RefSeq; WP_000392493.1; NZ_WXXJ01000007.1.
DR RefSeq; YP_026612.1; NC_005945.1.
DR AlphaFoldDB; Q81ZC2; -.
DR SMR; Q81ZC2; -.
DR STRING; 261594.GBAA_0347; -.
DR DNASU; 1087308; -.
DR EnsemblBacteria; AAP24380; AAP24380; BA_0347.
DR EnsemblBacteria; AAT29438; AAT29438; GBAA_0347.
DR GeneID; 45020403; -.
DR KEGG; ban:BA_0347; -.
DR KEGG; bar:GBAA_0347; -.
DR KEGG; bat:BAS0332; -.
DR PATRIC; fig|198094.11.peg.338; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_9; -.
DR OMA; RLWVDET; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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; Reference proteome.
FT CHAIN 1..347
FT /note="5-deoxyribose 1-phosphate isomerase"
FT /id="PRO_0000357141"
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
