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UniProtKB/Swiss-Prot entry Q89A37

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

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Entry information
Entry name MTLD_BUCBP
Primary accession number Q89A37
Secondary accession numbers None
Integrated into Swiss-Prot on May 23, 2003
Sequence was last modified on May 23, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 30)
Name and origin of the protein
Protein name Mannitol-1-phosphate 5-dehydrogenase
Synonym EC 1.1.1.17
Gene name
Name: mtlD
OrderedLocusNames: bbp_516
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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
AE016826; AAO27219.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_778114.1; -.
3D structure databases
ModBase Q89A37.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_516-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; FALSE_NEG.
BLOCKS Q89A37.
Genome annotation databases
GeneID 1058182; -.
GenomeReviews AE016826_GR; bbp_516.
KEGG bab:bbp516; -.
Phylogenomic databases
HOGENOM Q89A37; -.
Genome annotation databases
CMR Q89A37; bbp_516.
Other
ProtoNet Q89A37.
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   390  390     Mannitol-1-phosphate 5-dehydrogenase. PRO_0000170701
NP_BIND   3    14  12     NAD (By similarity). 
Sequence information
Length: 390 AA [This is the length of the unprocessed precursor] Molecular weight: 44567 Da [This is the MW of the unprocessed precursor] CRC64: B1037CA82DC02E8D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNALHFGAGN IGRGFIGPLL LKSGFNLTFV DNNQAIVDAI NRHQKYDITV VGNNFSYITT 

        70         80         90        100        110        120 
VKKVKAIYIN DPNIYFKIAK INVITISVGV HAINSLVVFF EKLIRYKIET NDFVFLTIIA 

       130        140        150        160        170        180 
CENVFRCASK LKENIKILLP GIYHKYLDKN ISFVDSVVDK IVCPNDKNNS DDINLSVKVE 

       190        200        210        220        230        240 
KFSEWIVDCT QFKHDRPNII GMIYSNHLDA FFERKLFTLN TGHAIAAYLG LLIGYKNIYQ 

       250        260        270        280        290        300 
AILDPLIFNI VYGAMKESGM VLIRKYNFFT DSEHKNYILK ILSRFKNIYL TDSLKRVGRN 

       310        320        330        340        350        360 
PLQKLKKDDR LISPLIDTIK YNLPNANLMK GIAAALCYID EKDIEAKKLR NMIINKGIKY 

       370        380        390 
VLSKISSLDS SLLIISEISI YFNIFMKVNI
Q89A37 in FASTA format

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