MTLD_TALMQ
ID MTLD_TALMQ Reviewed; 389 AA.
AC B6QP49;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE Short=M1PDH;
DE Short=MPD;
DE Short=MPDH;
DE EC=1.1.1.17;
GN ORFNames=PMAA_048060;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- FUNCTION: Catalyzes the NAD(H)-dependent interconversion of D-fructose
CC 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic
CC pathway. {ECO:0000250}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEA21000.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS995904; EEA21000.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002152000.1; XM_002151964.1.
DR AlphaFoldDB; B6QP49; -.
DR SMR; B6QP49; -.
DR STRING; 441960.B6QP49; -.
DR EnsemblFungi; EEA21000; EEA21000; PMAA_048060.
DR GeneID; 7029423; -.
DR KEGG; tmf:PMAA_048060; -.
DR HOGENOM; CLU_385507_0_0_1; -.
DR OrthoDB; 1133390at2759; -.
DR Proteomes; UP000001294; 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; 1.10.1040.10; -; 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 Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..389
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000371533"
FT ACT_SITE 214
FT /evidence="ECO:0000250"
FT BINDING 5..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 389 AA; 43188 MW; A305A10CEFB3693E CRC64;
MGKKAIQFGG GNIGRGFVAE FLHESGYEVV FIDVVPQVIE SLNKNKSYEV TEISEEGEKT
KTITNYRALS SKTQEPEVVK EIATADVVTC AVGPNILKFI APVIAKGIDA REEGLPPIAV
IACENAINAT DALRGYIEEH LDKSRLDTLP KRARFANSAI DRIVPTQPEH AGLNVRIEKF
YEWAVEQTPF GEYGHPDISA IHWVDHLEPY IERKLFTVNT GHATAAYYGY KAGKKTIHEA
MAEETIHKAV HAALDETASL IISKHEITEQ EQKEYVKTII SRISNPYLED VVERVGRAPL
RKLSRKERFI GPAAQLAERG MKFDALLGSI EKALQFQNVK GDDESTELAK ILSEKTAAEA
TQQITGLETD HPLYQPVLKV VEKVQSVSK