ID A0A194VAP5_9PEZI Unreviewed; 514 AA.
AC A0A194VAP5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Mannitol 2-dehydrogenase {ECO:0000256|ARBA:ARBA00040250};
DE EC=1.1.1.67 {ECO:0000256|ARBA:ARBA00038970};
GN ORFNames=VP1G_08151 {ECO:0000313|EMBL:KUI60938.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI60938.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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; KN714763; KUI60938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VAP5; -.
DR STRING; 694573.A0A194VAP5; -.
DR OrthoDB; 211204at2759; -.
DR Proteomes; UP000078576; 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:UP000078576}.
FT DOMAIN 45..211
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 240..484
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 514 AA; 57450 MW; 39956468D2A622EC CRC64;
MGSSTTSAPL KLNNQNLPQI EAYGAENERK ASVTPSYSRD GLKEGIVHIG VGGFHRAHLA
VYVDNLLKKN VDDARQWAIC GVGLKPFDAG MRDALVPQDC LYTVIERSAS GSAARVIGSI
NSFLYAPDDV EAVIAKMAHP DTRIVSMTIT ESGYYYNENT HELEVEDPDI VADLASDLTA
PRTTFGYLFS ALARRYEAGL KPFTVLSCDN MQKNGTISRN MLLSFARLRD TKIADWIAEN
GAFPNSMVDR ITPRTSDSDK TDLAESFGIQ DDWPVVTEPF MQWVVEDTFA NGRPSFEKVG
VQVVKNVHEV EKFECHKLRL LNASHTSMAY MAYLAGFEYV HNVIENPLFN KYLYNMMQEE
VKPLLPEIEG VNIDNYIKQL MERFSNPTIM DQITRLTLNG SGKLPQFIMP SIAEQIWQVK
THNFRRLALC VAGWFRYLNG VDEQGKPIAI DDPMAESLQA KAREGGDQPG PLLNVRSLFG
DDLRGDKPFV DELTRALESL HREGAMATLA KYVD
//
