Q4X1A4 (MTLD_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mannitol-1-phosphate 5-dehydrogenase
Short name=M1PDH
Short name=MPD
Short name=MPDH
EC=1.1.1.17

Gene names

Name:	mpdA
ORF Names:	AFUA_2G10660

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway. Has a strong preference for NADH over NADPH. Ref.2
Catalytic activity	D-mannitol 1-phosphate + NAD+ = D-fructose 6-phosphate + NADH.
Subunit structure	Monomer. Ref.2
Sequence similarities	Belongs to the mannitol dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=0.23 mM for D-mannitol 1-phosphate Ref.2 Ref.3 KM=2.1 mM for D-fructose 6-phosphate KM=0.016 mM for NADH KM=0.75 mM for NAD+

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mannitol metabolic process Inferred by curator Ref.2Ref.3. Source: UniProtKB
Molecular function	NAD binding Inferred from direct assay Ref.2Ref.3. Source: UniProtKB mannitol-1-phosphate 5-dehydrogenase activity Inferred from direct assay Ref.2Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 388	388	Mannitol-1-phosphate 5-dehydrogenase		PRO_0000371520
Regions
	Nucleotide binding	5 – 16	12	NAD By similarity
Sites
	Active site	213	1
Experimental info
	Mutagenesis	213	1	K → A: Loss of catalytic activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q4X1A4 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: EE8F7B90FAFC3B3F	FASTA	388	43,004
	10 20 30 40 50 60 MGKKAIQFGG GNIGRGFVAE FLHEAGYEVV FIDVVDKIID ALKSTPSYEV TEVSEEGEKT 70 80 90 100 110 120 KTITNYRAIN SKTNEEDVVK EIGTADVVTC AVGPNVLKFI APVIAKGIDA RTASKPVAVI 130 140 150 160 170 180 ACENAIGATD TLRGFIEQNT DKDRLSSMSE RARFANSAID RIVPNQPPNA GLNVRIEKFY 190 200 210 220 230 240 EWTVEQTPFG EFGHPDIPAI HWVDDLKPYI ERKLFTVNTG HATTAYYGHM RGKKMIADAL 250 260 270 280 290 300 ADAEIRQIVH KVLEQTAKLI TTKHEITEQE QNEYVDTIVK RMSNPFLEDN VERVGRAPLR 310 320 330 340 350 360 KLSRNERFIG PASQLAEKGL PFDALLGSIE MALRFQNVPG DEESAELAKI LKEMSAEEAT 370 380 GKLTGLEKHH PLYEPVQNVI AKVQKDSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[2]	"Characterization of recombinant Aspergillus fumigatus mannitol-1-phosphate 5-dehydrogenase and its application for the stereoselective synthesis of protio and deuterio forms of D-mannitol 1-phosphate." Krahulec S., Armao G.C., Weber H., Klimacek M., Nidetzky B. Carbohydr. Res. 343:1414-1423(2008) [PubMed: 18452897] [Abstract] Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[3]	"Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies of mannitol 2-dehydrogenase and mannitol-1-phosphate 5-dehydrogenase." Krahulec S., Armao G.C., Bubner P., Klimacek M., Nidetzky B. Chem. Biol. Interact. 178:274-282(2009) [PubMed: 18983992] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-213.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000001 Genomic DNA. Translation: EAL93361.1.
RefSeq	XP_755399.1. XM_750306.1.
3D structure databases
ProteinModelPortal	Q4X1A4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4X1A4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00004609; CADAFUAP00004609; CADAFUAG00004609.
GeneID	3513687.
GenomeReviews	Gene locus mpdA in contig CM000170_GR.
KEGG	afm:AFUA_2G10660.
Phylogenomic databases
eggNOG	fuNOG06426.
GeneTree	EFGT00050000004394.
HOGENOM	HBG568825.
OMA	FANTAVD.
OrthoDB	EOG469V3C.
Family and domain databases
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR013328. DH_multihelical. IPR023028. Mannitol_1_phos_5_DH. IPR000669. Mannitol_DH. IPR013118. Mannitol_DH_C. IPR013131. Mannitol_DH_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
KO	K00009.
Pfam	PF01232. Mannitol_dh. 1 hit. PF08125. Mannitol_dh_C. 1 hit. [Graphical view]
PRINTS	PR00084. MTLDHDRGNASE.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
PROSITE	PS00974. MANNITOL_DHGENASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MTLD_ASPFU

Accession

Primary (citable) accession number: Q4X1A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	July 5, 2005
Last modified:	December 14, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program