ID R9LKD1_9FIRM Unreviewed; 538 AA.
AC R9LKD1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=Fructuronate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=C814_02038 {ECO:0000313|EMBL:EOS59195.1};
OS Anaerotruncus sp. G3(2012).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=1235835 {ECO:0000313|EMBL:EOS59195.1, ECO:0000313|Proteomes:UP000014129};
RN [1] {ECO:0000313|EMBL:EOS59195.1, 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:EOS59195.1}.
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DR EMBL; ASTA01000050; EOS59195.1; -; Genomic_DNA.
DR RefSeq; WP_016316706.1; NZ_KE159676.1.
DR AlphaFoldDB; R9LKD1; -.
DR STRING; 1235835.C814_02038; -.
DR PATRIC; fig|1235835.3.peg.2133; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_037833_0_0_9; -.
DR OrthoDB; 271711at2; -.
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; 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:UP000014129}.
FT DOMAIN 38..201
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 239..479
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 538 AA; 59114 MW; EC5EC7CFF68A0950 CRC64;
MKLCYEGLKD RAAWEAAGVA LPQFDWKEMC AATAAEPTWV HFGAGNIFRG FIALLQQSLL
EQGLVKGGIV AADTFDYDII EKIYTPFDHM TLMVSLLPDG SMEKEVVASI AEGLRAGNAF
PEDMDALKRI FRNPSLQMAS FTITEKGYAL KNIQGDFFPF VEADFKNGPS NCSHAMSMVA
SLLLERFNAC AAPVAMVSMD NCSHNGEKLR SSVMTVVEKW LENGFVSQEF VAWVQDETKV
SFPWSMIDKI TPRPAKVVEE SLAAAGIENM APIVTSKNTF IAPFVNAEQP QYLVVEDRFP
NGRPPLEKAG VYMTDRDTVN NTEKMKVTTC LNPLHTALAV YGCLLGYDSI AAEMKDPELK
ALVERIGYDE GIPVVVDPKI LSPMDFIHEV IDQRLPNPFI PDMPQRIATD TSQKVAIRFG
ETIKSYLARP DLNAADLTYI PLAIAGWLRY LLAVDDNGNP MECSSDPMLE TLQQQLSGAT
LGNPDSLDGK LPAILSNTSL FATDLNAAGL GGKIETMLRE LMAGPGAVRD TLKKYLRN
//
