ID D9TSJ7_THETC Unreviewed; 538 AA.
AC D9TSJ7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Mannitol dehydrogenase domain {ECO:0000313|EMBL:ADL69852.1};
GN OrderedLocusNames=Tthe_2387 {ECO:0000313|EMBL:ADL69852.1};
OS Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 /
OS NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium
OS thermosaccharolyticum).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=580327 {ECO:0000313|EMBL:ADL69852.1, ECO:0000313|Proteomes:UP000001626};
RN [1] {ECO:0000313|EMBL:ADL69852.1, ECO:0000313|Proteomes:UP000001626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM
RC 00135 / 2032 {ECO:0000313|Proteomes:UP000001626};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM
RT 571.";
RL Submitted (AUG-2010) 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};
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DR EMBL; CP002171; ADL69852.1; -; Genomic_DNA.
DR RefSeq; WP_013298809.1; NC_014410.1.
DR AlphaFoldDB; D9TSJ7; -.
DR STRING; 580327.Tthe_2387; -.
DR KEGG; ttm:Tthe_2387; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_037833_0_0_9; -.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000001626; Chromosome.
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; PTHR43362:SF1; MANNITOL DEHYDROGENASE 2-RELATED; 1.
DR PANTHER; PTHR43362; MANNITOL DEHYDROGENASE DSF1-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000001626}.
FT DOMAIN 38..201
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 239..506
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 538 AA; 60916 MW; 9A9299789C94E409 CRC64;
MKLKRHELKD PKKWEEMGIK LPQFDIDKVI DETKKNPRWV HFGAGNIFRG FIAMLQQTLL
NKGLADSGII AVESYDFEVH DKIYVPYDNL GLLVIMNSDG TLEKEVVGSI SDILLADPSN
KENWDRLNEV FSNPSLQIAS MTITEKGYNL KDFAGNFIKE VMEDIEAGPE NPKNVVSKLV
SLVYSRYKKG EYPLALVSLD NFSGNGERLY SAVMTIAEEW ANKGFVDKGF TQYLNDPSKI
SFPLTMIDKI VPRPHELVKK SLEEKGLEDM NIITTSKNTV IAPFVNAEKA QYLVIEDKFP
NGRMKLEEAG VLLTDKETVE KVERMKVTTC LNPLHTALAI YGCLLDYKTI ADEMKDDCLR
KLVEKIGYVE GMPVVINPKV LDPEEFIKEV IEVRLPNPYM PDTPQRIATD TSQKMGIRFG
ETIKSYIHRS DLEVNDLKFI PLVIAGWCRY LMGIDDEGNH MDLSPDPLLN DLKSHVSNIR
LGDVDSVKDN LRPILSNKEI FGLDLYEVGL GEKVESYFKE LISGTGAVRN TLKKYLEC
//
