Mannitol dehydrogenase - Pseudomonas fluorescens

Preferred order of sections

Names and origin

Protein names

Submitted name:
Mannitol dehydrogenase EMBL AAC04472.1
EC=1.1.1.67 EMBL AAC04472.1

Gene names

Name:

mtlD EMBL AAC04472.1

Organism

Pseudomonas fluorescens EMBL AAC04472.1

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	NAD SAAS SAAS023027 PDB 1LJ8 PDB 1M2W Nucleotide-binding PDB 1LJ8 PDB 1M2W
Molecular function	Oxidoreductase SAAS SAAS023027 EMBL AAC04472.1
Technical term	3D-structure PDB 1LJ8 PDB 1M2W
Gene Ontology (GO)
Molecular function	coenzyme binding Inferred from electronic annotation. Source: InterPro mannitol 2-dehydrogenase activity Inferred from electronic annotation. Source: EC mannitol-1-phosphate 5-dehydrogenase activity Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Nucleotide binding

34 – 37

4

NAD PDB 1LJ8 PDB 1M2W

Nucleotide binding

66 – 69

4

NAD PDB 1LJ8 PDB 1M2W

Nucleotide binding

130 – 133

4

NAD PDB 1LJ8 PDB 1M2W

Nucleotide binding

190 – 191

2

NAD PDB 1LJ8 PDB 1M2W

Nucleotide binding

231 – 233

3

NAD PDB 1LJ8 PDB 1M2W

Sites

Binding site

373

1

NAD PDB 1LJ8 PDB 1M2W

Sequences

Sequence

Length

Mass (Da)

Tools

O08355 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 7C12DFA443CEA443
Show »

FASTA

493

54,498

        10         20         30         40         50         60 
MKLNKQNLTQ LAPEVKLPAY TLADTRQGIA HIGVGGFHRA HQAYYTDALM NTGEGLDWSI 

        70         80         90        100        110        120 
CGVGLRSEDR KARDDLAGQD YLFTLYELGD TDDTEVRVIG SISDMLLAED SAQALIDKLA 

       130        140        150        160        170        180 
SPEIRIVSLT ITEGGYCIDD SNGEFMAHLP QIQHDLAHPS SPKTVFGFIC AALTQRRAAG 

       190        200        210        220        230        240 
IPAFTVMSCD NLPHNGAVTR KALLAFAALH NAELHDWIKA HVSFPNAMVD RITPMTSTAH 

       250        260        270        280        290        300 
RLQLHDEHGI DDAWPVVCEP FVQWVLEDKF VNGRPAWEKV GVQFTDDVTP YEEMKIGLLN 

       310        320        330        340        350        360 
GSHLALTYLG FLKGYRFVHE TMNDPLFVAY MRAYMDLDVT PNLAPVPGID LTDYKQTLVD 

       370        380        390        400        410        420 
RFSNQAIADQ LERVCSDGSS KFPKFTVPTI NRLIADGRET ERAALVVAAW ALYLKGVDEN 

       430        440        450        460        470        480 
GVSYTIPDPR AEFCQGLVSD DALISQRLLA VEEIFGTAIP NSPEFVAAFE RCYGSLRDNG 

       490 
VTTTLKHLLK KPV

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References

[1]	"Cloning, nucleotide sequence and expression of a mannitol dehydrogenase gene from Pseudomonas fluorescens DSM 50106 in Escherichia coli." Brunker P., Altenbuchner J., Kulbe K.D., Mattes R. Biochim. Biophys. Acta 1351:157-167(1997) [PubMed: 9116029] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: DSM50106 EMBL AAC04472.1.
[2]	"Structure and function of the genes involved in mannitol, arabitol and glucitol utilization from Pseudomonas fluorescens DSM50106." Brunker P., Altenbuchner J., Mattes R. Gene 206:117-126(1998) [PubMed: 9461423] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: DSM50106 EMBL AAC04472.1.
[3]	Bruenker P., Altenbuchner J., Mattes R. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: DSM50106 EMBL AAC04472.1.
[4]	"Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism." Kavanagh K.L., Klimacek M., Nidetzky B., Wilson D.K. J. Biol. Chem. 277:43433-43442(2002) [PubMed: 12196534] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH NAD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF007800 Genomic DNA. Translation: AAC04472.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LJ8	X-ray	1.70	A	1-493	[»]
1M2W	X-ray	1.80	A/B	1-493	[»]

ProteinModelPortal

O08355.

SMR

O08355. Positions 1-492.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR000669. Mannitol_DH.
IPR013118. Mannitol_DH_C.
IPR023027. Mannitol_DH_CS.
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.

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. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

O08355_PSEFL

Accession

Primary (citable) accession number: O08355

Entry history

Integrated into UniProtKB/TrEMBL:	July 1, 1997
Last sequence update:	July 1, 1997
Last modified:	October 19, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)