ID A0A229YI70_9EURO Unreviewed; 388 AA.
AC A0A229YI70;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000256|ARBA:ARBA00016219};
DE EC=1.1.1.17 {ECO:0000256|ARBA:ARBA00012939};
GN ORFNames=CDV55_100992 {ECO:0000313|EMBL:RHZ50608.1}, CFD26_101076
GN {ECO:0000313|EMBL:RLL93797.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ50608.1, ECO:0000313|Proteomes:UP000215394};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL93797.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ50608.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61381; EC=1.1.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000292};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006541}.
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:RHZ50608.1}.
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DR EMBL; NKHV02000244; RHZ50608.1; -; Genomic_DNA.
DR EMBL; NIDN02000262; RLL93797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229YI70; -.
DR STRING; 1245748.A0A229YI70; -.
DR OrthoDB; 1700931at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; Unassembled WGS sequence.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-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 HAMAP; MF_00196; Mannitol_dehydrog; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR023028; Mannitol_1_phos_5_DH.
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; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000215289}.
FT DOMAIN 4..124
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 153..364
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 388 AA; 43049 MW; B4E3EB424AF1B18F CRC64;
MGKKAIQFGG GNIGRGFVAE FLHEAGYEVV FIDVVDKIID ALKSTPSYQV TEVSEEGENT
KTITNYRAIN SKTNESDVVK EIATADVVTC AVGPNVLKFI APVIAKGIDA RTASKPVAVI
ACENAIGATD TLRGFIEQQT DKDRLSTMSE RARFANSAID RIVPNQPPNA GLDVRIEKFY
EWTVEQTPFG KFGHPDIPAI HWVDHLEPYI ERKLFTVNTG HATTAYYGRV RGKKMIADAL
ADPEIRETVH KVLEQTADLI TAKHEITEQE QKEYVDIIIK RMSNPFLEDN VERVGRAPLR
KLSRNERFIG PASQLAEKGK PFDKLLGSIE MALRFQNVPG DEESTELAKI LKEMSADEAT
AKLTGLEKSH PLYEPVQNVV AKVQKDSK
//
