ID A0A1Q5U768_9EURO Unreviewed; 502 AA.
AC A0A1Q5U768;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Mannitol 2-dehydrogenase {ECO:0000256|ARBA:ARBA00040250};
DE EC=1.1.1.67 {ECO:0000256|ARBA:ARBA00038970};
GN ORFNames=PENSUB_5690 {ECO:0000313|EMBL:OKP08323.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP08323.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP08323.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP08323.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) 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 -!- 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:OKP08323.1}.
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DR EMBL; MNBE01000569; OKP08323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5U768; -.
DR STRING; 1316194.A0A1Q5U768; -.
DR OrthoDB; 211204at2759; -.
DR Proteomes; UP000186955; 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:UP000186955}.
FT DOMAIN 36..201
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 231..475
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 502 AA; 56410 MW; 831775F069CA9C71 CRC64;
MAPLKLNNKN LAQIATAGET QVKVPTYQRG GAVKEGIVHV GVGGFHRAHL AVYVDQLMQK
HGVTDYAICG VGLQPFDASM RDALGSQDYL YTVIERSAKG SFANVVGSIN SYLFAPDNRE
AVIAKMAHSD THIVSLTITE SGYYYNENTH ELQSENPDIQ HDLNPANENA PRTTFGFLYA
ALVRRRKQGL KPFTVMSCDN MLKNGSITRH MLESFARLRD PEMAKWISEQ GGFPNAMVDR
ITPQTAPSDK TALADNFGIE DSWPVVTEPF MQWVIEDKFS DGRPPFEKVG AQVVKDVHDV
EQFEKHKLRL LNGSHSAIGY PGQLAGFKYV HEVMENPLFR KFIWQYMQEE VKPLLPEIPG
VNIDQYCNTL MERFSNPTIM DQLPRVALNA SGKIPQFIMP SIAEQIWVSG PFRRLCFIAA
AWFHYINGVD DNGNKFEIDD PMREELQAKA RAGGTNPTEL LSITNLFGDD LRSDKRFLQE
MTTAMEDIAR DGILKTIPKY ID
//
