ID A0A0A2KFI2_PENIT Unreviewed; 513 AA.
AC A0A0A2KFI2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Mannitol 2-dehydrogenase {ECO:0000256|ARBA:ARBA00040250};
DE EC=1.1.1.67 {ECO:0000256|ARBA:ARBA00038970};
GN ORFNames=PITC_007640 {ECO:0000313|EMBL:KGO65646.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO65646.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO65646.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO65646.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO65646.1}.
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DR EMBL; JQGA01001488; KGO65646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KFI2; -.
DR STRING; 40296.A0A0A2KFI2; -.
DR HOGENOM; CLU_027324_0_1_1; -.
DR OMA; IVASWAR; -.
DR OrthoDB; 211204at2759; -.
DR PhylomeDB; A0A0A2KFI2; -.
DR Proteomes; UP000030104; 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:UP000030104}.
FT DOMAIN 37..202
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 233..479
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 513 AA; 58001 MW; 9E4FAD269FD03D90 CRC64;
MAPLKLNSKN LELIGKAGKG PIQIPSHRFL RRPVKEGIVH VGVGGFHRAH LAVYVDQLME
KHGENKYAIC GVGLQPFDAT MRDVLREQDH LYTVMERSDK GSFAHVVGSI NSYLFAPDNR
QAVIDKMAHP DTRIVSLTIT ESGYYYNENT HELISEHPDI KNDLKESNAK APCTTFGFLY
AALAQRYANK QDPFTVMSCD NMQKNGSITR NMLVSFARLR NPKIADWIAE KGAFPNAMVD
RITPQTSEND KKVLAEDFGI QDAWPVVTEP FMQWVIEDDF SNGRPEFEKV GVQVVKNVHD
VEQFEKHKLR LLNGSHSAIG YPGQLAGFEY VHEVMQNPQL RKLVWEMMQE EVKPLLPEIP
GVDIDDYCKT LMKRFSNSTI MDQLPRVCLN ASGKIPQFIM PSIAEAIMQS KKEQREYPFR
RLCFVAAAWF LYIKGVDDHG KTFAVVDPML DELLAAAKAD DGGPSGLLEI KNLFGDDLRG
YPRFTTEIKQ AMKDIAEKGV LETLKEYFPE DAN
//
