ID D7V167_LISGR Unreviewed; 341 AA.
AC D7V167;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Ribulose-5-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_02069};
DE Short=Ribulose-5-P reductase {ECO:0000256|HAMAP-Rule:MF_02069};
DE EC=1.1.1.405 {ECO:0000256|HAMAP-Rule:MF_02069};
DE AltName: Full=Ribitol-5-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02069};
GN Name=tarJ {ECO:0000256|HAMAP-Rule:MF_02069,
GN ECO:0000313|EMBL:EFI83299.1};
GN ORFNames=HMPREF0556_11984 {ECO:0000313|EMBL:EFI83299.1};
OS Listeria grayi DSM 20601.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI83299.1, ECO:0000313|Proteomes:UP000010119};
RN [1] {ECO:0000313|EMBL:EFI83299.1, ECO:0000313|Proteomes:UP000010119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI83299.1,
RC ECO:0000313|Proteomes:UP000010119};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH dependent reduction of D-ribulose 5-
CC phosphate to D-ribitol 5-phosphate. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_02069};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|HAMAP-Rule:MF_02069};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02069}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|HAMAP-Rule:MF_02069}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFI83299.1}.
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DR EMBL; ACCR02000005; EFI83299.1; -; Genomic_DNA.
DR RefSeq; WP_003755130.1; NZ_GL538352.1.
DR AlphaFoldDB; D7V167; -.
DR STRING; 525367.HMPREF0556_11984; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_823603_0_0_9; -.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000010119; Unassembled WGS sequence.
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; IPR013154; ADH-like_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 PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF19; RIBULOSE-5-PHOSPHATE REDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF16912; Glu_dehyd_C; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02069};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02069};
KW NADP {ECO:0000256|HAMAP-Rule:MF_02069};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02069,
KW ECO:0000313|EMBL:EFI83299.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010119};
KW Teichoic acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02069};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02069}.
FT DOMAIN 26..131
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 146..327
FT /note="Glucose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16912"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02069"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02069"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02069"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02069"
SQ SEQUENCE 341 AA; 38572 MW; AE3E676C1FC42332 CRC64;
MINQVFRLVS ERQFEETNIE EKLTPETVVV RPTYLSICAA DQRYYTGSRG KEVLSRKLPM
ALIHEGVGEV VYDAEGEFPV GTKVVMIPNT PFEENDVIAE NYLRTSKFRS SGYDGLMQEN
VYMRRDRVVP LPEGMDLEVA AYSELISVAY HAISRFQNKG NRNRESFGVW GDGNLGFITC
LLLKTIYPES KVYIFGKTQY KLDFFSFVDE AFLIDEIPAD LVIDNAFECA GGRGSEHAVE
QIIDLIVPEG TVALLGVSEM PIEFNSRMVL EKGLTVFGSS RSGRVDFENT VKFLSENEGA
VEYLSNLIGL RKVVRNLQDI TEAFEDDLRN PFGKTVMEWR V
//
