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Reviewed, UniProtKB/Swiss-Prot Q8XDG9 (MTLD_ECO57)

Last modified November 4, 2008. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mannitol-1-phosphate 5-dehydrogenase
    EC=1.1.1.17
Gene names
Name: mtlD
Ordered Locus Names: Z5024, ECs4476
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

D-mannitol 1-phosphate + NAD(+) = D-fructose 6-phosphate + NADH.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the mannitol dehydrogenase family.

Ontologies

Keywords

   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmannitol-1-phosphate 5-dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Mannitol-1-phosphate 5-dehydrogenase
PRO_0000170705

Regions

Nucleotide binding3 – 1412NAD By similarity

Amino acid modifications

Modified residue2691N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XDG9-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: E38BB1867C53CA3C

FASTA38241,198
        10         20         30         40         50         60 
MKALHFGAGN IGRGFIGKLL ADAGIQLTFA DVNQVVLDAL NARHSYQVHV VGETEQVDTV 

        70         80         90        100        110        120 
SGVDAVSSIG DDVVDLIAQV DLVTTAVGPV VLERIAPAIA KGLVKRKEQG NESPLNIIAC 

       130        140        150        160        170        180 
ENMVRGTTQL KGHVMNALPE DAKAWVEEHV GFVDSAVDRI VPPSASATND PLEVTVETFS 

       190        200        210        220        230        240 
EWIVDKTQFK GALPNIPGME LTDNLMAFVE RKLFTLNTGH AITAYLGKLA GHQTIRDAIL 

       250        260        270        280        290        300 
DEKIRAVVKG AMEESGAVLI KRYGFDADKH AAYIQKILGR FENPYLKDDV ERVGRQPLRK 

       310        320        330        340        350        360 
LSAGDRLIKP LLGTLEYSLP HKNLIQGIAG AMHFRSEDDP QAQELAALIA DKGPQAALAQ 

       370        380 
ISDLDANSEV VSEAVTAYKA MQ 

« Hide

References

Cross-references

Sequence databases

AE005174 Genomic DNA. Translation: AAG58744.1.
BA000007 Genomic DNA. Translation: BAB37899.1.
PIRD86035.
D91188.
RefSeqNP_290180.1.
NP_312503.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID915582.
960952.
GenomeReviewsGene locus ECs4476 in contig BA000007_GR.
Gene locus Z5024 in contig AE005174_GR.
KEGGece:Z5024.
ecs:ECs4476.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8XDG9.

Enzyme and pathway databases

BioCycECOL83334:ECS4476-MON.

Family and domain databases

HAMAPMF_00196.
[Tree]
InterProIPR013328. DHase_multihelical.
IPR013118. Mannitol_DHase_C.
IPR000669. Mannitol_DHase_core.
IPR013131. Mannitol_DHase_N.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PfamPF01232. Mannitol_dh. 1 hit.
PF08125. Mannitol_dh_C. 1 hit.
[Graphical view]
PRINTSPR00084. MTLDHDRGNASE.
PROSITEPS00974. MANNITOL_DHGENASE. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Entry information

Entry nameMTLD_ECO57
AccessionPrimary (citable) accession number: Q8XDG9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: March 1, 2002
Last modified: November 4, 2008
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents