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UniProtKB/Swiss-Prot entry Q8RCS0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MTLD_THETN
Primary accession number Q8RCS0
Secondary accession numbers None
Integrated into Swiss-Prot on October 19, 2002
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 34)
Name and origin of the protein
Protein name Mannitol-1-phosphate 5-dehydrogenase
Synonym EC 1.1.1.17
Gene name
Name: mtlD
OrderedLocusNames: TTE0342
From
Thermoanaerobacter tengcongensis [TaxID: 119072] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; Thermoanaerobacteraceae; Thermoanaerobacter.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
DOI=10.1101/gr.219302; PubMed=11997336 [NCBI, ExPASy, EBI, Israel, Japan]
Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R., Wang J., Yu J., Yang H.;
"A complete sequence of the T. tengcongensis genome.";
Genome Res. 12:689-700(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE013006; AAM23634.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_622030.1; -.
3D structure databases
ModBase Q8RCS0.
Enzyme and pathway databases
BioCyc TTEN273068:TTE0342-MON; -.
Ontologies
GO
GO:0008926; Molecular function: mannitol-1-phosphate 5-dehydrogenase activity (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00196; -; 1.
PBIL [Tree]
InterPro IPR013328; DHase_multihelical.
IPR013118; Mannitol_DHase_C.
IPR000669; Mannitol_DHase_core.
IPR013131; Mannitol_DHase_N.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
Pfam PF01232; Mannitol_dh; 1.
PF08125; Mannitol_dh_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00084; MTLDHDRGNASE.
PROSITE PS00974; MANNITOL_DHGENASE; 1.
BLOCKS Q8RCS0.
Genome annotation databases
GeneID 996309; -.
GenomeReviews AE008691_GR; TTE0342.
KEGG tte:TTE0342; -.
NMPDR fig|273068.3.peg.188; -.
Phylogenomic databases
HOGENOM Q8RCS0; -.
Genome annotation databases
CMR Q8RCS0; TTE0342.
Other
ProtoNet Q8RCS0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   386  386     Mannitol-1-phosphate 5-dehydrogenase. PRO_0000170728
NP_BIND   4    15  12     NAD (By similarity). 
Sequence information
Length: 386 AA [This is the length of the unprocessed precursor] Molecular weight: 44022 Da [This is the MW of the unprocessed precursor] CRC64: 251DDC8448736BEC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLKALHFGAG NIGRGFIGYL LNKSGYEVTF VDISKEIVDN INKYKKYNVI ILKEPVEKEE 

        70         80         90        100        110        120 
VKEVKALHLE EEDKVLDAFL EADMVTTSVG VSNLSSIGGR LKKYLKARKE KNEKPLDIMA 

       130        140        150        160        170        180 
CENALFATDV LRERVVKEED DDFITYLNLK VGFPNTAVDR IVPAVKIDKK LPVDVAVEEF 

       190        200        210        220        230        240 
FEWDIEKNKI KGNLQIEGVE LVDDLKPYIE RKLFLLNGAH ATTAYLGYLR GYTYIHQAIK 

       250        260        270        280        290        300 
DDNIRAIVKG MQEEISTALS KKYDVDKESL MAYAEKVIKR FENPYLQDEV TRVGREPLRK 

       310        320        330        340        350        360 
LSSEDRLIAP LKLCSEVGIT PNFILYGIAA GLLFDYKEDA QAVKMREYVE QFGIKKAVNV 

       370        380 
ITGLEEESDL VEEIEKRYFE LKGKLI 

Q8RCS0 in FASTA format

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