TARJ2_STAA8
ID TARJ2_STAA8 Reviewed; 341 AA.
AC Q2G1C4;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Ribulose-5-phosphate reductase 2 {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000305};
DE Short=Ribulose-5-P reductase 2 {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000305};
DE EC=1.1.1.405 {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000269|PubMed:18556787};
DE AltName: Full=Ribitol-5-phosphate dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000305};
GN Name=tarJ' {ECO:0000303|PubMed:18556787};
GN OrderedLocusNames=SAOUHSC_00221 {ECO:0000312|EMBL:ABD29397.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
RC STRAIN=RN4220;
RX PubMed=18556787; DOI=10.1128/jb.00526-08;
RA Pereira M.P., D'Elia M.A., Troczynska J., Brown E.D.;
RT "Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus
RT leads to functionally redundant poly(ribitol phosphate) polymerases.";
RL J. Bacteriol. 190:5642-5649(2008).
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:18556787}.
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:18556787};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02069};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.21 uM for NADPH {ECO:0000269|PubMed:18556787};
CC KM=11.0 uM for ribulose 5-phosphate {ECO:0000269|PubMed:18556787};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02069,
CC ECO:0000269|PubMed:18556787}.
CC -!- SUBUNIT: Heterodimer together with TarI. {ECO:0000269|PubMed:18556787}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000255|HAMAP-Rule:MF_02069}.
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DR EMBL; CP000253; ABD29397.1; -; Genomic_DNA.
DR RefSeq; WP_000610189.1; NZ_LS483365.1.
DR RefSeq; YP_498816.1; NC_007795.1.
DR AlphaFoldDB; Q2G1C4; -.
DR SMR; Q2G1C4; -.
DR STRING; 1280.SAXN108_0231; -.
DR EnsemblBacteria; ABD29397; ABD29397; SAOUHSC_00221.
DR GeneID; 3920297; -.
DR KEGG; sao:SAOUHSC_00221; -.
DR PATRIC; fig|93061.5.peg.203; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_823603_0_0_9; -.
DR OMA; MVIMSSX; -.
DR SABIO-RK; Q2G1C4; -.
DR UniPathway; UPA00790; -.
DR PRO; PR:Q2G1C4; -.
DR Proteomes; UP000008816; 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; IPR013149; ADH-like_C.
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 Pfam; PF00107; ADH_zinc_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..341
FT /note="Ribulose-5-phosphate reductase 2"
FT /id="PRO_0000437488"
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; 38558 MW; E51D93579A70C2F6 CRC64;
MINQVYQLVA PRQFDVTYNN VDIYGNHVIV RPLYLSICAA DQRYYTGRRD ENVLRKKLPM
SLVHEAVGEV VFDSKGVFEK GTKVVMVPNT PTEQHHIIAE NYLASSYFRS SGYDGFMQDY
VVMAHDRIVP LPNDIDLSTI SYTELVSVSY HAIQRFERKS IPLKTSFGIW GDGNLGYITA
ILLRKLYPEA KTYVFGKTDY KLSHFSFVDD IFTVNQIPDD LKIDHAFECV GGKGSQVALQ
QIVEHISPEG SIALLGVSEL PVEVNTRLVL EKGLTLIGSS RSGSKDFEQV VDLYRKYPDI
VEKLALLKGH EINVCTMQDI VQAFEMDLST SWGKTVLKWT I
