ID   DRDI_PETMO              Reviewed;         347 AA.
AC   A9BJF6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 78.
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=Pmob_0639;
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX   NCBI_TaxID=403833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-2007) 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=ABX31370.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000879; ABX31370.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041534034.1; NC_010003.1.
DR   AlphaFoldDB; A9BJF6; -.
DR   SMR; A9BJF6; -.
DR   STRING; 403833.Pmob_0639; -.
DR   EnsemblBacteria; ABX31370; ABX31370; Pmob_0639.
DR   KEGG; pmo:Pmob_0639; -.
DR   eggNOG; COG0182; Bacteria.
DR   HOGENOM; CLU_016218_1_2_0; -.
DR   OrthoDB; 1290468at2; -.
DR   Proteomes; UP000000789; 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_0000357218"
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;  38270 MW;  789762B453252045 CRC64;
     MTVVPVKLNE LKNKLVIIDQ TLLPNEEKFL ELDNPEEIWE AIKKLRVRGA PAIGIAAAFG
     LYVSTLKSKA ANVAQFKKEF EEVRDYFATS RPTAVNLFWA LKRMTRRFEQ EEDKTVDKIK
     QALLDESEKI FAEDQEMSKA IGKHGLSLLK PGMGLLTHCN AGGLASSGYG TALAPIYLGH
     EKGYNFKVYA DETRPLLQGA RLTTYELYKA GIDVTLICDD MASLVMKEGK IDAVLVGCDR
     VAANGDTANK IGTSGLAVLA KEYGIPMYIL GPTSTIDLDA STGEDIKIEL RDEEEVVNGF
     GRRTALKGVK AYNPAFDVTD AKYITAIITE KGIVMQPYKE SLKKLFE