ID K6YB68_9ALTE Unreviewed; 500 AA.
AC K6YB68;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Mannitol 2-dehydrogenase {ECO:0000313|EMBL:GAC13878.1};
DE EC=1.1.1.67 {ECO:0000313|EMBL:GAC13878.1};
GN Name=mtlK {ECO:0000313|EMBL:GAC13878.1};
GN ORFNames=GLIP_1237 {ECO:0000313|EMBL:GAC13878.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC13878.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC13878.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC13878.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC13878.1}.
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DR EMBL; BAEN01000023; GAC13878.1; -; Genomic_DNA.
DR RefSeq; WP_008843695.1; NZ_BAEN01000023.1.
DR AlphaFoldDB; K6YB68; -.
DR STRING; 1127673.GLIP_1237; -.
DR eggNOG; COG0246; Bacteria.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000006334; Unassembled WGS sequence.
DR GO; GO:0050086; F:mannitol 2-dehydrogenase activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:GAC13878.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006334}.
FT DOMAIN 34..198
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 227..468
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 500 AA; 56016 MW; 5EC432856A46759D CRC64;
MNTQSTVRLA NKTLSQVPKS IVVPTYDRSK LKSGIVHVGV GGFHRSHEAF YTDAYIQQSG
DLDWGICGVG LRDSDRKMQA ILEAQDYLYT LIVKHPNGSI ENQVIGCLTG FMLGCDEPNA
VIQKMADAET KIVSLTITEG GYNFNPATNE FDFSNPDVIH DLANPLEPRL VFGFLAAALK
LRMERGLPAF TVQSCDNIQH NGDVTRKMLL AYCHKVDSEL AKWIDAHVQF PNAMVDRITP
ATTEKDVAYL QDQFGISDQW PVTCEPFHQW IIEDKFSLGR PQWQTVGAQF VDDVTPYENM
KIRLLNAGHS VLGILGSIHG FGTIDESMQD AVFSQFLQLF MDSEVTPILP EVSGIDLTQY
KQTLLERFAN PNIKDSLSRI CSESSSKLAT FLLPTLVENL QRNGDIQCAS LVLAAWCYYS
DKGVDRFGNS LNIIDAMSER LHNTAAQTAN NADAFLRLTS IFGKLIENQR FLKAYQGYVE
AIYNDTNVKN HMQLMLMMRR
//
