ID R6QCU0_9FIRM Unreviewed; 341 AA.
AC R6QCU0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=BN563_01578 {ECO:0000313|EMBL:CDC33610.1};
OS Eubacterium sp. CAG:251.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262886 {ECO:0000313|EMBL:CDC33610.1, ECO:0000313|Proteomes:UP000018414};
RN [1] {ECO:0000313|EMBL:CDC33610.1, ECO:0000313|Proteomes:UP000018414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:251 {ECO:0000313|Proteomes:UP000018414};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- 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:CDC33610.1}.
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DR EMBL; CBFD010000083; CDC33610.1; -; Genomic_DNA.
DR AlphaFoldDB; R6QCU0; -.
DR STRING; 1262886.BN563_01578; -.
DR Proteomes; UP000018414; 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 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000018414};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02069}.
FT DOMAIN 27..131
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 212..294
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; 38074 MW; 4ADCFA4C410478AE CRC64;
MINTVYRLVA PRRFEIAFED INLFGENAIV RPTYLSICNA DMRYYLGTRD AKVLAEKLPM
ALIHEGVGEV FLDPTGTFKT GDKVVMVPNA PVEKDEFIAE NYLRSSKFCG SSMDGFLQEF
VEISPKRLVK LPDDIDMTVA AFTEIVSVSV HAISRFDKIA HARRNTISVW GDGNLGYITS
LFLKYHFPKS KIVVFGTSSD KLADFTFADE THLVNEVPDG FTTDHAFECV GGNGSPIAIE
QIIGLIKPEG TISILGVSEY PVPINTRMIL EKGLRVFGSS RSGVKDFAKT VDMYKKHPEI
IDYLGNLINS VNVVRTTTDI KNAFEKDTQK SFGKTIMKWE E
//
