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Database: UniProt
Entry: A0A1I4HW90_9FIRM
LinkDB: A0A1I4HW90_9FIRM
Original site: A0A1I4HW90_9FIRM 
ID   A0A1I4HW90_9FIRM        Unreviewed;       512 AA.
AC   A0A1I4HW90;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Tagaturonate reductase {ECO:0000313|EMBL:SFL46469.1};
GN   ORFNames=SAMN02983006_01219 {ECO:0000313|EMBL:SFL46469.1};
OS   Halanaerobium salsuginis.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=29563 {ECO:0000313|EMBL:SFL46469.1, ECO:0000313|Proteomes:UP000199006};
RN   [1] {ECO:0000313|EMBL:SFL46469.1, ECO:0000313|Proteomes:UP000199006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51327 {ECO:0000313|EMBL:SFL46469.1,
RC   ECO:0000313|Proteomes:UP000199006};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOTI01000013; SFL46469.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4HW90; -.
DR   STRING; 29563.SAMN02983006_01219; -.
DR   OrthoDB; 9768714at2; -.
DR   Proteomes; UP000199006; 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:UP000199006}.
FT   DOMAIN          36..187
FT                   /note="Mannitol dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01232"
FT   DOMAIN          222..423
FT                   /note="Mannitol dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08125"
SQ   SEQUENCE   512 AA;  58398 MW;  ACA5C8F641FF0686 CRC64;
     MSEDNLPMLN REYLESELMG TELADFSAEI LDYPEKVVQI GEGNFLRAFV DWMFHTMNKK
     GIFKGRAVVV QPIAEGRVAN LNQQDGLYTL YLRGIENGKE VNKKEIMTAI SRGLNSYTEW
     EQFLKLAEDP AVEFVVSNTT EAGISYNETD QLTDTPPESY PGKLTAYLYR RYQSFNGDPG
     KGMVIIPVEL IDRNGDNLKR IILQLAEDWN LEAEFSSWIK ESNHFLNTLV DRIVTGYPFN
     EIDKLEKELA YHDQNLDTGE IFHLWVIEGD ESLKEKLPFH KAGLNVKWVD DLTPYRTTKV
     RILNGAHTST VPVSYLAGID LVRDAVNDEL VGEFIKQAVF EDIIPTLAAD PAELDDFAHK
     IFERFKNPYI DHKWLDISLN STSKFKTRVL PSLVQHIEQL SKVPARLSFS LAALITFYQG
     TELENGKLVA YRGEDKYLIR DDKSALEYFA QLWSEFKAAE ITLAELGRDV LANQDFWDRD
     LNQLPGLTES VVSNLKMIKK AGMKASLEKL IK
//
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