ID R9MIM0_9FIRM Unreviewed; 484 AA.
AC R9MIM0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Tagaturonate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=C818_00927 {ECO:0000313|EMBL:EOS70919.1};
OS Lachnospiraceae bacterium MD308.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235799 {ECO:0000313|EMBL:EOS70919.1, ECO:0000313|Proteomes:UP000014117};
RN [1] {ECO:0000313|EMBL:EOS70919.1, ECO:0000313|Proteomes:UP000014117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-2 {ECO:0000313|EMBL:EOS70919.1,
RC ECO:0000313|Proteomes:UP000014117};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 3-2.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61381; EC=1.1.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000292};
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:EOS70919.1}.
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DR EMBL; ASTE01000011; EOS70919.1; -; Genomic_DNA.
DR AlphaFoldDB; R9MIM0; -.
DR STRING; 1235799.C818_00927; -.
DR PATRIC; fig|1235799.3.peg.991; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_027324_1_0_9; -.
DR OrthoDB; 9768714at2; -.
DR Proteomes; UP000014117; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000014117}.
FT DOMAIN 25..182
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 216..417
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 484 AA; 55885 MW; E45E4E2153A35967 CRC64;
MEKLNYRTLE KLKYKGYILK DAPERVLQFG EGNFLRAFVE HFIDIMNEKA EFNGKVVMVQ
PSPNNSATYA DKINEQDGLY TLYLRGLKKG GKVQEKRIIS CVSRCLNVNR DYSEVIACAD
NPELRYIVCN TTEAGIVHDS RDDFKDFPPV SYPAKLTQFL YRRFQRFGEK NGKGFIILPC
ELIDDNGKEL KRCVLKYAVQ WRLGEEFIQW IERENLFCST LVDRIVTGYP KDEAVALNEE
NGYEDSFIDT GEMYGMWVIE APEWLSKELP FDEAGLPVQI TNDYKPYRQR KVCILNGAHT
SMAPGAYLAG KRTVGECMDD KGISEFIKRL INNEIIPALS LCEEECKQFA DAVEERFENP
FIHHELLSIS LNSTSKWKAR VLPVIEDYQR KYGVLPRRLV ASFAFYIAFY IMFAQGSCND
ERKVLEFFCN HRDDSEEELV HAVCCNAGFW GKNLAKFPGL EEETVRILRN VRKDGIYETI
VNLI
//
