ID TARJ1_STAA8 Reviewed; 341 AA.
AC Q2G1B9;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Ribulose-5-phosphate reductase 1 {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000305};
DE Short=Ribulose-5-P reductase 1 {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000305};
DE EC=1.1.1.405 {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000269|PubMed:15362865};
DE AltName: Full=Ribitol-5-phosphate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_02069, ECO:0000305};
GN Name=tarJ {ECO:0000303|PubMed:15362865};
GN OrderedLocusNames=SAOUHSC_00226 {ECO:0000312|EMBL:ABD29401.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; 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, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP ENZYME KINETICS, AND PATHWAY.
RX PubMed=15362865; DOI=10.1021/bi048866v;
RA Pereira M.P., Brown E.D.;
RT "Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of
RT reductase and cytidylyltransferase activities in Haemophilus influenzae and
RT Staphylococcus aureus.";
RL Biochemistry 43:11802-11812(2004).
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:15362865}.
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:15362865};
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=6.74 uM for NADPH {ECO:0000269|PubMed:15362865};
CC KM=28.5 uM for D-ribulose 5-phosphate {ECO:0000269|PubMed:15362865};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02069,
CC ECO:0000305|PubMed:15362865}.
CC -!- SUBUNIT: Heterodimer together with TarI. Can also form a dimer of
CC heterodimers. {ECO:0000269|PubMed:15362865}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000255|HAMAP-Rule:MF_02069}.
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DR EMBL; CP000253; ABD29401.1; -; Genomic_DNA.
DR RefSeq; WP_000610203.1; NZ_LS483365.1.
DR RefSeq; YP_498821.1; NC_007795.1.
DR PDB; 6XH9; X-ray; 3.20 A; A=1-341.
DR PDB; 6XHK; X-ray; 3.00 A; A=1-341.
DR PDBsum; 6XH9; -.
DR PDBsum; 6XHK; -.
DR AlphaFoldDB; Q2G1B9; -.
DR SMR; Q2G1B9; -.
DR STRING; 93061.SAOUHSC_00226; -.
DR PaxDb; 1280-SAXN108_0236; -.
DR GeneID; 3920301; -.
DR KEGG; sao:SAOUHSC_00226; -.
DR PATRIC; fig|93061.5.peg.207; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_823603_0_0_9; -.
DR OrthoDB; 1700359at2; -.
DR BioCyc; MetaCyc:MONOMER-19986; -.
DR UniPathway; UPA00790; -.
DR PRO; PR:Q2G1B9; -.
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 CDD; cd08237; ribitol-5-phosphate_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_02069; TarJ; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR034710; TarJ.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF19; RIBULOSE-5-PHOSPHATE REDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome; Teichoic acid biosynthesis; Zinc.
FT CHAIN 1..341
FT /note="Ribulose-5-phosphate reductase 1"
FT /id="PRO_0000437487"
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"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:6XHK"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:6XHK"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:6XHK"
SQ SEQUENCE 341 AA; 38452 MW; 99DF1294677CF9C0 CRC64;
MINQVYQLVA PRQFEVTYNN VDIYSDYVIV RPLYMSICAA DQRYYTGSRD ENVLSQKLPM
SLIHEGVGEV VFDSKGVFNK GTKVVMVPNT PTEKDDVIAE NYLKSSYFRS SGHDGFMQDF
VLLNHDRAVP LPDDIDLSII SYTELVTVSL HAIRRFEKKS ISNKNTFGIW GDGNLGYITA
ILLRKLYPES KIYVFGKTDY KLSHFSFVDD VFFINKIPEG LTFDHAFECV GGRGSQSAIN
QMIDYISPEG SIALLGVSEF PVEVNTRLVL EKGLTLIGSS RSGSKDFQDV VDLYIQYPDI
VDKLALLKGQ EFEIATINDL TEAFEADLST SWGKTVLKWI M
//
