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Database: UniProt
Entry: A0A0A1DPS2_NOCSI
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ID   A0A0A1DPS2_NOCSI        Unreviewed;       168 AA.
AC   A0A0A1DPS2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Ribose-5-phosphate isomerase B {ECO:0000256|ARBA:ARBA00014007};
DE            EC=5.3.1.6 {ECO:0000256|ARBA:ARBA00011959};
DE   AltName: Full=Phosphoriboisomerase B {ECO:0000256|ARBA:ARBA00032117};
GN   ORFNames=F9L07_08220 {ECO:0000313|EMBL:KAB2811820.1}, KR76_20280
GN   {ECO:0000313|EMBL:AIY18513.1}, NSI01_24480
GN   {ECO:0000313|EMBL:GEB14133.1};
OS   Nocardioides simplex (Arthrobacter simplex).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Pimelobacter.
OX   NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY18513.1, ECO:0000313|Proteomes:UP000030300};
RN   [1] {ECO:0000313|EMBL:AIY18513.1, ECO:0000313|Proteomes:UP000030300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY18513.1,
RC   ECO:0000313|Proteomes:UP000030300};
RX   PubMed=25573942;
RA   Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA   Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT   "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT   Ac-2033D.";
RL   Genome Announc. 3:0-0(2015).
RN   [2] {ECO:0000313|EMBL:GEB14133.1, ECO:0000313|Proteomes:UP000318936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12069 {ECO:0000313|EMBL:GEB14133.1,
RC   ECO:0000313|Proteomes:UP000318936};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Pimelobacter simplex NBRC 12069.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAB2811820.1, ECO:0000313|Proteomes:UP000449906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pch-N {ECO:0000313|EMBL:KAB2811820.1,
RC   ECO:0000313|Proteomes:UP000449906};
RA   Jeong S.E.;
RT   "Pimelobacter sp. isolated from Paulinella.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC         EC=5.3.1.6; Evidence={ECO:0000256|ARBA:ARBA00001713};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC       5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC       1/1. {ECO:0000256|ARBA:ARBA00004988}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the LacAB/RpiB family.
CC       {ECO:0000256|ARBA:ARBA00008754}.
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DR   EMBL; CP009896; AIY18513.1; -; Genomic_DNA.
DR   EMBL; BJMC01000010; GEB14133.1; -; Genomic_DNA.
DR   EMBL; WBVM01000001; KAB2811820.1; -; Genomic_DNA.
DR   RefSeq; WP_038680820.1; NZ_WBVM01000001.1.
DR   AlphaFoldDB; A0A0A1DPS2; -.
DR   STRING; 2045.KR76_20280; -.
DR   KEGG; psim:KR76_20280; -.
DR   eggNOG; COG0698; Bacteria.
DR   HOGENOM; CLU_091396_4_0_11; -.
DR   OrthoDB; 1778624at2; -.
DR   Proteomes; UP000030300; Chromosome.
DR   Proteomes; UP000318936; Unassembled WGS sequence.
DR   Proteomes; UP000449906; Unassembled WGS sequence.
DR   GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1400.10; Sugar-phosphate isomerase, RpiB/LacA/LacB; 1.
DR   InterPro; IPR011860; Rib-5-P_Isoase_Actino.
DR   InterPro; IPR003500; RpiB_LacA_LacB.
DR   InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR   NCBIfam; TIGR02133; RPI_actino; 1.
DR   NCBIfam; TIGR00689; rpiB_lacA_lacB; 1.
DR   PANTHER; PTHR30345:SF0; DNA DAMAGE-REPAIR_TOLERATION PROTEIN DRT102; 1.
DR   PANTHER; PTHR30345; RIBOSE-5-PHOSPHATE ISOMERASE B; 1.
DR   Pfam; PF02502; LacAB_rpiB; 1.
DR   PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR   SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AIY18513.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030300}.
FT   BINDING         8..9
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         71..75
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         104
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         114
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         138
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         142
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
SQ   SEQUENCE   168 AA;  18210 MW;  8691238355FEEED7 CRC64;
     MRVHLGCDHA GLELKSHLIG WLTEHGYEPV DHGPFVYDAL DDYPVFCLRA AEGVRADREQ
     GLDSLGVVIG GSGNGEQIAA NKVQGVRAAL AWSEQTASLA REHNDAWVVA VGGRMHSLDE
     MTRLVEVFLT TPYTGEERHA RRIAQLSAYE TTGDLPPLPE SALGHGEA
//
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