ID E3ZP69_LISSE Unreviewed; 341 AA.
AC E3ZP69;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 ORFNames=NT03LS_1248 {ECO:0000313|EMBL:EFS00578.1};
OS Listeria seeligeri FSL N1-067.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=702453 {ECO:0000313|EMBL:EFS00578.1};
RN [1] {ECO:0000313|EMBL:EFS00578.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL N1-067 {ECO:0000313|EMBL:EFS00578.1};
RX PubMed=21126366; DOI=10.1186/1471-2164-11-688;
RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H.,
RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.;
RT "Comparative genomics of the bacterial genus Listeria: Genome evolution is
RT characterized by limited gene acquisition and limited gene loss.";
RL BMC Genomics 11:688-688(2010).
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:EFS00578.1}.
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DR EMBL; ADXJ01000513; EFS00578.1; -; Genomic_DNA.
DR RefSeq; WP_003746843.1; NZ_CM001051.1.
DR AlphaFoldDB; E3ZP69; -.
DR GeneID; 32490423; -.
DR PATRIC; fig|702453.3.peg.1008; -.
DR HOGENOM; CLU_823603_0_0_9; -.
DR OrthoDB; 1700359at2; -.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000004302; 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:SF19; D-GULOSIDE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 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 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 Teichoic acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02069};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02069}.
FT DOMAIN 27..129
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 220..295
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
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; 38525 MW; 44B127276B433273 CRC64;
MINQVYRLVS ERQFEEANVE EALTEDVVVV RPTYLSICAA DQRYYTGSRG KEMLSKKLPM
ALIHEGVGQV TYDATGEFEI GTKVVMIPNT PVEDDPVIAE NYRRSSLFRS SGYDGLMQEN
VFMRRDRVVR LPENMDMEVA AYSELISVAF HAITRFKKKA NDNQSVFGVW GDGNLGFITC
LLLKTIYPES KVIIFGKTQY KLDFFSFVDE AYLVDELPAG VVIDNAFECA GGRGSQYAVE
QIIDLIKPEG TISLLGVSEN PIEFNSRMVL EKGLTVFGSS RSGREDFQNT VNFLSENERA
VEYLSSLIGQ RKVVRNLQDI IEAFETDLRN PFGKTVMEWK V
//