ID   TARJ_BACSH              Reviewed;         341 AA.
AC   Q8RKJ0; B7ZDK6; E0U4X8;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Ribulose-5-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000305};
DE            Short=Ribulose-5-P reductase {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000305};
DE            EC=1.1.1.405 {ECO:0000255|HAMAP-Rule:MF_02069};
DE   AltName: Full=Ribitol-5-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000305};
GN   Name=tarJ {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000303|PubMed:11882717};
GN   OrderedLocusNames=BSUW23_17570;
OS   Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS   subtilis subsp. spizizenii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PUTATIVE FUNCTION.
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=11882717; DOI=10.1099/00221287-148-3-815;
RA   Lazarevic V., Abellan F.-X., Beggah Moeller S., Karamata D., Maueel C.;
RT   "Comparison of ribitol and glycerol teichoic acid genes in Bacillus
RT   subtilis W23 and 168: identical function, similar divergent organization,
RT   but different regulation.";
RL   Microbiology 148:815-824(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RA   Soldo B., Freymond P.P., Karamata D., Lazarevic V.;
RT   "Minor teichoic acid of Bacillus subtilis W23.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA   Zeigler D.R.;
RT   "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT   into speciation within the B. subtilis complex and into the history of B.
RT   subtilis genetics.";
RL   Microbiology 157:2033-2041(2011).
CC   -!- FUNCTION: Catalyzes the NADPH dependent reduction of D-ribulose 5-
CC       phosphate to D-ribitol 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_02069}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribitol 5-phosphate + NADP(+) = D-ribulose 5-phosphate +
CC         H(+) + NADPH; Xref=Rhea:RHEA:19921, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57695, ChEBI:CHEBI:57783, ChEBI:CHEBI:58121,
CC         ChEBI:CHEBI:58349; EC=1.1.1.405; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02069};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02069};
CC   -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02069,
CC       ECO:0000305|PubMed:11882717}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000255|HAMAP-Rule:MF_02069}.
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DR   EMBL; AJ313428; CAC86108.1; -; Genomic_DNA.
DR   EMBL; AM260209; CAJ97395.1; -; Genomic_DNA.
DR   EMBL; CP002183; ADM39549.1; -; Genomic_DNA.
DR   RefSeq; WP_003219623.1; NC_014479.1.
DR   AlphaFoldDB; Q8RKJ0; -.
DR   SMR; Q8RKJ0; -.
DR   EnsemblBacteria; ADM39549; ADM39549; BSUW23_17570.
DR   GeneID; 64305340; -.
DR   KEGG; bss:BSUW23_17570; -.
DR   HOGENOM; CLU_823603_0_0_9; -.
DR   OMA; HADQRYF; -.
DR   BioCyc; MetaCyc:MON-19970; -.
DR   UniPathway; UPA00790; -.
DR   Proteomes; UP000002233; Chromosome.
DR   GO; GO:0050256; F:ribitol-5-phosphate 2-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:1902012; P:poly(ribitol phosphate) teichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02069; TarJ; 1.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR031640; Glu_dehyd_C.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR034710; TarJ.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF16912; Glu_dehyd_C; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Metal-binding; NADP; Oxidoreductase;
KW   Teichoic acid biosynthesis; Zinc.
FT   CHAIN           1..341
FT                   /note="Ribulose-5-phosphate reductase"
FT                   /id="PRO_0000160829"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02069"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02069"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02069"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02069"
SQ   SEQUENCE   341 AA;  38559 MW;  DFC4549735BD19F5 CRC64;
     MINQTYRLVS ARQFEVTYKD KVVHSDKVVV RPTHLSICAA DQRYYTGSRG KEAMDKKLPM
     ALIHEGIGKV MFDPTGTFKV GTRVVMVPNT PVEEHEVIAE NYLRSSRFRS SGYDGFMQDY
     MFMAPDRLVE LPDSINPHVA AFTELITIAV HALSRFERMA HKKRDTFGVW GDGNLGFIMT
     LLLKKKYPDS KVFIFGKTPY KLDHFSFVDA AYQINDIPED VRLDHAFECV GGRGSESAIE
     QIIAHVHPEA CVALLGVSEY PVEIETRMVL EKGITLIGSS RSGREDFART VDFLAQYPEV
     VDYLETLVGG RFPVRSIEEI TNAFEADLTS SWGKTVIEWE I