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Database: UniProt
Entry: A0A1M4TXW3_9CLOT
LinkDB: A0A1M4TXW3_9CLOT
Original site: A0A1M4TXW3_9CLOT 
ID   A0A1M4TXW3_9CLOT        Unreviewed;       537 AA.
AC   A0A1M4TXW3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Fructuronate reductase {ECO:0000313|EMBL:SHE49329.1};
GN   ORFNames=SAMN02745158_00630 {ECO:0000313|EMBL:SHE49329.1};
OS   Lactonifactor longoviformis DSM 17459.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Lactonifactor.
OX   NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHE49329.1, ECO:0000313|Proteomes:UP000184245};
RN   [1] {ECO:0000313|EMBL:SHE49329.1, ECO:0000313|Proteomes:UP000184245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17459 {ECO:0000313|EMBL:SHE49329.1,
RC   ECO:0000313|Proteomes:UP000184245};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQVI01000002; SHE49329.1; -; Genomic_DNA.
DR   RefSeq; WP_072848927.1; NZ_FQVI01000002.1.
DR   AlphaFoldDB; A0A1M4TXW3; -.
DR   STRING; 1122155.SAMN02745158_00630; -.
DR   OrthoDB; 271711at2; -.
DR   Proteomes; UP000184245; 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; 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:UP000184245}.
FT   DOMAIN          38..201
FT                   /note="Mannitol dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01232"
FT   DOMAIN          240..474
FT                   /note="Mannitol dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08125"
SQ   SEQUENCE   537 AA;  58841 MW;  B946236A7B8A1403 CRC64;
     MKLSQEALNN KNMWEEAGFA LPQYDREAVA AKTKEAPAWI HFGAGNIFRA FTANLQQTLL
     NAGKADTGII VAEGFDYEII EKMYRPNDNL SVLVTLKSDG TIEKTVVGSI VESVIVDSSN
     AAEWARLKEI FTAPTLQMVS FTITEKGYNL FAADGSYFPP VKADFENGPK APVSYIGKLT
     ALVYERYLAG RLPLALVSMD NCSHNGTRLH DAVIAYAKAW SEHGLVPKEF LAYAEDPACI
     SFPWSMIDKI TPRPDDSVKE MLKKDGFDDV EAIVTSKNTY VAAFVNSEEP QYLVIENAFP
     NGRPNLDEAG VIFADKETVD KVEKMKVCTC LNPLHTALAV YGCLLDYTLI ADEMKDPELK
     KLVEIIGYQE GLPVVVDPGI INPREFIDEV LQVRIPNPFM PDTPQRIATD TSQKLGIRFG
     ETIKAYAASD TLDVKDLKLI PLVLAGWCRY LLAVDDNGNA FAPSSDPLLE SSMACVKDIK
     LGEKGDFHEA LQPILSNAAI FGVDLYQAGL GETVEALFAE LAAGPGAVRA TLKKYTA
//
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