TARJ_STRR6
ID TARJ_STRR6 Reviewed; 346 AA.
AC Q8DPI3;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ribulose-5-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000303|PubMed:19074383};
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, ECO:0000269|PubMed:19074383};
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:19074383};
GN OrderedLocusNames=spr1148 {ECO:0000312|EMBL:AAK99951.1};
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=R36A;
RX PubMed=19074383; DOI=10.1128/jb.01120-08;
RA Baur S., Marles-Wright J., Buckenmaier S., Lewis R.J., Vollmer W.;
RT "Synthesis of CDP-activated ribitol for teichoic acid precursors in
RT Streptococcus pneumoniae.";
RL J. Bacteriol. 191:1200-1210(2009).
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 ECO:0000269|PubMed:19074383}.
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, ECO:0000269|PubMed:19074383};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P25984,
CC ECO:0000255|HAMAP-Rule:MF_02069};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=61 uM for D-ribulose 5-phosphate {ECO:0000269|PubMed:19074383};
CC Note=kcat is 0.5 sec(-1). {ECO:0000269|PubMed:19074383};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02069,
CC ECO:0000269|PubMed:19074383}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000305}.
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DR EMBL; AE007317; AAK99951.1; -; Genomic_DNA.
DR PIR; C98015; C98015.
DR RefSeq; NP_358741.1; NC_003098.1.
DR AlphaFoldDB; Q8DPI3; -.
DR SMR; Q8DPI3; -.
DR STRING; 171101.spr1148; -.
DR EnsemblBacteria; AAK99951; AAK99951; spr1148.
DR KEGG; spr:spr1148; -.
DR PATRIC; fig|171101.6.peg.1246; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_823603_0_0_9; -.
DR OMA; HADQRYF; -.
DR BioCyc; MetaCyc:MON-20026; -.
DR BRENDA; 1.1.1.405; 1960.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000000586; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR034710; TarJ.
DR Pfam; PF08240; ADH_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome; Teichoic acid biosynthesis; Zinc.
FT CHAIN 1..346
FT /note="Ribulose-5-phosphate reductase"
FT /id="PRO_0000437489"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25984, ECO:0000255|HAMAP-
FT Rule:MF_02069"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25984, ECO:0000255|HAMAP-
FT Rule:MF_02069"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25984, ECO:0000255|HAMAP-
FT Rule:MF_02069"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P25984, ECO:0000255|HAMAP-
FT Rule:MF_02069"
SQ SEQUENCE 346 AA; 39503 MW; 6194B3155396F079 CRC64;
MRKTSKMINQ IYQLTKPKFI NVKYQEEAID QENHILIRPN YMAVCHADQR YYQGKRDPKI
LNKKLPMAMI HESCGTVISD PTGTYEVGQK VVMIPNQSPM QSDEEFYENY MTGTHFLSSG
FDGFMREFVS LPKDRVVAYD AIEDTVAAIT EFVSVGMHAM NRLLTLAHSK RERIAVIGDG
SLAFVVANII NYTLPEAEIV VIGRHWEKLE LFSFAKECYI TDNIPEDLAF DHAFECCGGD
GTGPAINDLI RYIRPQGTIL MMGVSEYKVN LNTRDALEKG LILVGSSRSG RIDFENAIQM
MEVKKFANRL KNILYLEEPV REIKDIHRVF ATDLNTAFKT VFKWEV
