M2DH_PHANO
ID M2DH_PHANO Reviewed; 568 AA.
AC Q0UEB6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Mannitol 2-dehydrogenase;
DE Short=M2DH;
DE Short=MDH;
DE EC=1.1.1.67;
GN ORFNames=SNOG_09898;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: Catalyzes the NAD(H)-dependent interconversion of D-fructose
CC and D-mannitol in the mannitol metabolic pathway. {ECO:0000250}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CH445339; EAT83163.1; -; Genomic_DNA.
DR RefSeq; XP_001800184.1; XM_001800132.1.
DR AlphaFoldDB; Q0UEB6; -.
DR SMR; Q0UEB6; -.
DR STRING; 13684.SNOT_09898; -.
DR PRIDE; Q0UEB6; -.
DR EnsemblFungi; SNOT_09898; SNOT_09898; SNOG_09898.
DR GeneID; 5977089; -.
DR KEGG; pno:SNOG_09898; -.
DR eggNOG; ENOG502QT30; Eukaryota.
DR HOGENOM; CLU_027324_0_1_1; -.
DR InParanoid; Q0UEB6; -.
DR OMA; YKPYDNL; -.
DR OrthoDB; 1095102at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0050086; F:mannitol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046029; F:mannitol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 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 Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..568
FT /note="Mannitol 2-dehydrogenase"
FT /id="PRO_0000371547"
FT BINDING 109..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 568 AA; 63495 MW; BF3CECA2C4156C92 CRC64;
MFSYLPRYPL RAASARALVR ATRPSYRSAL LRYQSSEAVG RTQEIVPGAY QIPPRDFSRQ
HEEKLAPKNA ARAPRRIEPA TLKLNSKNLS QLQNVTVPTY QREGVKQGIV HVGVGGFHRA
HLAAYVDTLL EQFNSQDWSI CGVDLQPFAA PMRDALGSQD NLYTMIECDT EGTSARVIGS
ITDYLFAPDN CEAVIAKMAH PDTHIVSMTV TESGYYMNEN THELQIDHPD IAADLAGQQP
PRTVFAYLYA ALARRHAAGL RPFTVMSCDN MQKNGDISRN MLLAFARQQN PEVADWIAEN
GAFPNSMVDR ITPRTSDENK AQLAQEFGVE DSWPVVTEVF HQWVLEDKFA DGRPPFEKAG
VQVVPNVHKV EEYELIKLRL LNASHSAMGY AGYLGGFTYI HEVIADPTFR KYIRNMMQEE
VQPLLPRIPG VSVDDYCNTL LGRFSNPTLK DELPRICLGG SGKIPQFIMP SIAEQIQAGG
PLRRLTLCAA AWFRYLRGIN EQGQAFKLDD PMAEELQAKA LESPFSVLEV KSLFGDDLRD
DKRFVAELKN ALESLERDGA RATIAQYA