ID A0A1V6UXJ0_9EURO Unreviewed; 520 AA.
AC A0A1V6UXJ0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Mannitol 2-dehydrogenase {ECO:0000256|ARBA:ARBA00040250};
DE EC=1.1.1.67 {ECO:0000256|ARBA:ARBA00038970};
GN ORFNames=PENCOP_c003G04330 {ECO:0000313|EMBL:OQE43106.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE43106.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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 -!- 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:OQE43106.1}.
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DR EMBL; MDDG01000003; OQE43106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6UXJ0; -.
DR STRING; 36646.A0A1V6UXJ0; -.
DR OrthoDB; 211204at2759; -.
DR Proteomes; UP000191500; 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:UP000191500}.
FT DOMAIN 38..203
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 234..483
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 520 AA; 58864 MW; CEAADDB90294FB2B CRC64;
MTALRLNTKN LDLIGKAGRG KIQIPTHRAR NAGTVKEGIV HIGVGGFHRA HLAVYVDQLM
EKHGVKNFAI CGVGLQPFDS AMRDILREQD HLYTVMERSD KGSFAHVVGC INSYLYAPDN
REAVIAKMAH PDTHIVSLTI TESGYYYNEN THELQSEHPD IKYDATASNE NAPRTTFGFL
YAALARRHRQ GLNPFTVMSC DNMQKNGSIT RHMLESFARM RNPEVAEWIA EKGAFPNAMV
DRITPQTENV DKEALNENFG IEDSWPVVTE PFMQWVIEDQ FSDGRPPFEK VGVQVVNNVH
DVEQFEMHKL RLLNGSHSAI GYPGQLAGFK YVHEVMQNAK MRKLVWEMMQ EEVKPLLPQI
PGVDIDQYCK TLMKRFSNST IQDQLPRICL NASGKIPQFI MPSIAEVIMK SNADKREYPF
RRLCFVAAAW FTYIRGVDDK KVPFNVNDPM LDELRAAAKA DPGGPLGLLQ IKNLFGDDLR
TDKRFIAEMT QAMKDIAEKG VLATLDEYFP DSKEDRNDVD
//
