ID Q1GMX0_RUEST Unreviewed; 471 AA.
AC Q1GMX0;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Fructuronate reductase {ECO:0000313|EMBL:ABF61996.1};
GN OrderedLocusNames=TM1040_3866 {ECO:0000313|EMBL:ABF61996.1};
OS Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OG Plasmid pTM1040 {ECO:0000313|Proteomes:UP000000636}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=292414 {ECO:0000313|EMBL:ABF61996.1, ECO:0000313|Proteomes:UP000000636};
RN [1] {ECO:0000313|Proteomes:UP000000636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040 {ECO:0000313|Proteomes:UP000000636};
RC PLASMID=pTM1040 {ECO:0000313|Proteomes:UP000000636};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA Richardson P.;
RT "Complete sequence of plasmid of Silicibacter sp. TM1040.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABF61996.1, ECO:0000313|Proteomes:UP000000636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040 {ECO:0000313|EMBL:ABF61996.1,
RC ECO:0000313|Proteomes:UP000000636};
RC PLASMID=pTM1040 {ECO:0000313|Proteomes:UP000000636};
RX PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA Saunders E., Buchan A.;
RT "Ecological genomics of marine Roseobacters.";
RL Appl. Environ. Microbiol. 73:4559-4569(2007).
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DR EMBL; CP000375; ABF61996.1; -; Genomic_DNA.
DR RefSeq; WP_011536642.1; NC_008042.1.
DR AlphaFoldDB; Q1GMX0; -.
DR KEGG; sit:TM1040_3866; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_027324_0_0_5; -.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000000636; Plasmid pTM1040.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0019594; P:mannitol metabolic process; 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; IPR023027; Mannitol_DH_CS.
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 PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE 4: Predicted;
KW Plasmid {ECO:0000313|EMBL:ABF61996.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000636}.
FT DOMAIN 18..176
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 206..397
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 471 AA; 50927 MW; 1DE1A26373A80D86 CRC64;
MTNSLIPCSY EQTLLKPRIL HIGFGAFARA HPMVYLHHGL VAEGGDWGVV AARLNSGVDA
LDSLDAVQGR YHIAEADGDT ITLREIGLLC GTCHPARDGV DAIPALIASP DMSVILLTIT
EKGYCTKDGQ LDLTQAAIQA ELDGGLPTTA IGVLVSGLER RRAADLGGIT ILSCDNQPDN
GALTRAAVLG FAEELDLNLA EWIRTHVRFP SSMVDRIVPA MTDDSHTAVA SALGRDDPNA
VLCEPFRQWV IEDDFANERP PFAEGGAMLV ADVQPFEEMK LRLLNGAHTT LAWLGQLLGY
QTVADCMADK ELRALIRHLM LAEQAATLRP LEGIDLAAYA DELLKRFENT RLRHRLDQIA
SDSSQKMPQR LFAPIAINLE AKREWSVSAL AVAAWIKGLG SLPPVPDPRQ DELRRAALCN
DPVAAVLSLP SLVPDALRPL AEFQAAISVA FERLQGGAKA TVTTTAKELR R
//
