ID C6LFJ5_9FIRM Unreviewed; 341 AA.
AC C6LFJ5;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=BRYFOR_07398 {ECO:0000313|EMBL:EET60580.1};
OS Marvinbryantia formatexigens DSM 14469.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Marvinbryantia.
OX NCBI_TaxID=478749 {ECO:0000313|EMBL:EET60580.1, ECO:0000313|Proteomes:UP000005561};
RN [1] {ECO:0000313|EMBL:EET60580.1, ECO:0000313|Proteomes:UP000005561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14469 {ECO:0000313|EMBL:EET60580.1,
RC ECO:0000313|Proteomes:UP000005561};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2009) 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:EET60580.1}.
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DR EMBL; ACCL02000010; EET60580.1; -; Genomic_DNA.
DR RefSeq; WP_006862189.1; NZ_CP102268.1.
DR AlphaFoldDB; C6LFJ5; -.
DR STRING; 168384.SAMN05660368_02093; -.
DR eggNOG; COG1063; Bacteria.
DR OrthoDB; 1700359at2; -.
DR Proteomes; UP000005561; 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 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 ECO:0000313|EMBL:EET60580.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005561};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02069}.
FT DOMAIN 27..123
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 219..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; 38121 MW; 918615794BBA08C2 CRC64;
MLNTVYQLKS ARQFEAVFKN IELDDMHVLV RPTHLSICHA DQRYYQGTRP EAVLRAKLPM
ALIHEGIGRV VYDPTGTFQV GDEVVMIPNH PSETDNVIAE NYLRSTKFCG SSKDGFMQEY
VSLLPDRVVL LPEGLDKITA AFTEIVTVSY HAITRFLRFS HERRAAVGVW GDGNLGYITS
LLLKKMLPET RVYVFGVNRS KLSDFSFADD TFLVSQVPEG LQVDHAFECV GSGAAAKAID
QIIDCIHPEG TISLMGVSED PVPVNTRMVL EKGLRIFGSS RSGRADYEGL MELYKENPDI
PSYLENIVGT RLKVSNIGDI VKAFETDIHK MIGKTVMIWN E
//
