ID A0A2B7Y6C8_9EURO Unreviewed; 388 AA.
AC A0A2B7Y6C8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000256|ARBA:ARBA00016219};
DE EC=1.1.1.17 {ECO:0000256|ARBA:ARBA00012939};
GN ORFNames=AJ79_01531 {ECO:0000313|EMBL:PGH16659.1};
OS Helicocarpus griseus UAMH5409.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH16659.1, ECO:0000313|Proteomes:UP000223968};
RN [1] {ECO:0000313|EMBL:PGH16659.1, ECO:0000313|Proteomes:UP000223968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH16659.1,
RC ECO:0000313|Proteomes:UP000223968};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH16659.1}.
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DR EMBL; PDNB01000015; PGH16659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7Y6C8; -.
DR STRING; 1447875.A0A2B7Y6C8; -.
DR OrthoDB; 1700931at2759; -.
DR Proteomes; UP000223968; 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:UP000223968}.
FT DOMAIN 4..124
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 153..370
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 388 AA; 43221 MW; A17D447E539890A2 CRC64;
MGKKAVHFGG GNIGRGFVAE FLHESGYEVV FVDVMEKVID SLNAASSYTV TEISEEGEQQ
KTIKNYRAIN SKTDLPKVIN EIATADVVTC AVGPNILKFI APNIAQGIDA RTESKPLAVI
ACENAIGATD TLHNFIKENT PESRRESLPK RAQFANSAID RIVPTQDPDA GLNVKIEKFY
EWVVEQTPFG DVGHPDIKAI HWVDNLEPYI ERKLFTVNTG HATAAYYGYA LGKKTIHDAL
SDEKIRGEVN AALLETSKLI IEKHGIPEEE QRDYVNKIVT RISNPYLEDV VQRVGRAPLR
KLSRKERFIG PAAQLAERGQ KVDALMGAVE QALRFQNVPE DDESTELYKI LKEKSAEEAT
TQLTGLEKNH PLYPRVLEKV DKVQKETK
//
