ID W3XIP4_PESFW Unreviewed; 504 AA.
AC W3XIP4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Mannitol 2-dehydrogenase {ECO:0000256|ARBA:ARBA00040250};
DE EC=1.1.1.67 {ECO:0000256|ARBA:ARBA00038970};
GN ORFNames=PFICI_03322 {ECO:0000313|EMBL:ETS85297.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS85297.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol + NAD(+) = D-fructose + H(+) + NADH;
CC Xref=Rhea:RHEA:12084, ChEBI:CHEBI:15378, ChEBI:CHEBI:16899,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.67;
CC Evidence={ECO:0000256|ARBA:ARBA00036174};
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006541}.
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DR EMBL; KI912110; ETS85297.1; -; Genomic_DNA.
DR RefSeq; XP_007830094.1; XM_007831903.1.
DR AlphaFoldDB; W3XIP4; -.
DR STRING; 1229662.W3XIP4; -.
DR GeneID; 19268335; -.
DR KEGG; pfy:PFICI_03322; -.
DR eggNOG; ENOG502QT30; Eukaryota.
DR HOGENOM; CLU_027324_0_1_1; -.
DR InParanoid; W3XIP4; -.
DR OMA; IVASWAR; -.
DR OrthoDB; 211204at2759; -.
DR Proteomes; UP000030651; 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; IPR000669; Mannitol_DH.
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 PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030651}.
FT DOMAIN 40..203
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 234..477
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 504 AA; 56844 MW; CCE2B0918BAB3DE8 CRC64;
MAISTERFKL TSKNLSPISS QQGEHRVEIP TYNRDDVKEG IVHVGVGGFH RAHLAVYVDK
LLQHHNERDW AICGVGLRPN DAAMRDVLAA QDHLYTVIER SAKGSFANVV GSINSFLFAP
DDREAVIAKM AHPDTHIVSL TITESGYYYN ENTHQLTSEH PDIQHDLANE NSPVSTFGFL
YAALARRHAA GLKPFTVLSC DNMQKNGSIT RHMLESFARL RNPELAKWIA EEGAFPNAMV
DRITPSTSPN DIKSLSEDFG IDDEWPVVTE PFMQWVVEDK FSDGRPPFEK VGVQVVNNVH
DVEQFEKHKL RLLNASHSAM AYPGQLAGFK YIHEVMEHPV YRKFVWQMMQ EEVKPLLPDI
PGVNIDQYCE TLMERFSNPT IMDQIPRVAL NASGKIPQFI MPSIAEQIWV TGPFKRLCFV
LAGWFHYIRG VDNAGNAFEI DDPMREQLQA LAKQGGNDPR PLLSIKVLFG DDLRNDKRFI
DELTSAMELI DKEGVMAALP KLVN
//
