ID R9LC12_9FIRM Unreviewed; 496 AA.
AC R9LC12;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Tagaturonate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=C814_02914 {ECO:0000313|EMBL:EOS55921.1};
OS Anaerotruncus sp. G3(2012).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=1235835 {ECO:0000313|EMBL:EOS55921.1, ECO:0000313|Proteomes:UP000014129};
RN [1] {ECO:0000313|EMBL:EOS55921.1, ECO:0000313|Proteomes:UP000014129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G3(2012) {ECO:0000313|Proteomes:UP000014129};
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 Anaerotruncus bacterium G3.";
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:EOS55921.1}.
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DR EMBL; ASTA01000093; EOS55921.1; -; Genomic_DNA.
DR RefSeq; WP_016317529.1; NZ_KE159680.1.
DR AlphaFoldDB; R9LC12; -.
DR STRING; 1235835.C814_02914; -.
DR PATRIC; fig|1235835.3.peg.3070; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_027324_1_0_9; -.
DR OrthoDB; 9768714at2; -.
DR Proteomes; UP000014129; 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; IPR000669; Mannitol_DH.
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 PRINTS; PR00084; MTLDHDRGNASE.
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:UP000014129}.
FT DOMAIN 18..171
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 203..460
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 496 AA; 55905 MW; 4F17503C118B9B24 CRC64;
MKTLNKEMAA VRQRPLRLMQ FGEGNFLRAF VDYMVDISNE KGVSDIGIAV VKPIPFGNLE
RFRQQDNLYT VILRGQMDGK VVNDARIVTS IQKTIDAYES YGELVETACL ESLQIIISNT
TEAGIVFDAD DRFESEPPST YPGKLTKLLF ERFQKFEGDA GKGLAIIPCE LIEHNGDRLH
DCVNQYISLW GLGETFRNWV EESCTFCCTL VDRIVTGYPR DNLEETTAQL GYIDELVDTA
EPFGLWVIES RRDISDILPL EKAGLPVIFT DDQTPYRERK VRILNGAHTS TVLAGYLAGF
EIVGEIMKDP DLRTFMNTVV MEEIVPGVRL PREEVLAFAN SVFERFENPF IKHRLLDISL
NSVSKWKSRI LPSLRDYYNT SGRLPHLLTF SFAALMAFYT SDKLENGVLQ GNRDGQPYEI
KDDAAALVFF AEHSTRLSSN EFVQALASQT GFWGEDLTRY DGFVPMAAGY LDEIKTKGMK
AAIHALVEQK EGLTVG
//
