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UniProtKB/Swiss-Prot entry Q44297


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

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Entry information
Entry name ODH_ARTSC
Primary accession number Q44297
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 54)
Name and origin of the protein
Protein name Opine dehydrogenase
Synonyms EC 1.5.1.28
N-(1-D-carboxyethyl)-L-norvaline dehydrogenase
Gene name
Name: odh
From
Arthrobacter sp. (strain 1C) [TaxID: 79670] 
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Micrococcineae; Micrococcaceae; Arthrobacter.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7487048 [NCBI, ExPASy, EBI, Israel, Japan]
Dairi T., Asano Y.;
"Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C.";
Appl. Environ. Microbiol. 61:3169-3171(1995).
[2]
CHARACTERIZATION.
PubMed=2753861 [NCBI, ExPASy, EBI, Israel, Japan]
Asano Y., Yamaguchi K., Kondo K.;
"A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C.";
J. Bacteriol. 171:4466-4471(1989).
[3]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1038/854; PubMed=9665174 [NCBI, ExPASy, EBI, Israel, Japan]
Britton K.L., Asano Y., Rice D.W.;
"Crystal structure and active site location of N-(1-D-carboxylethyl)-L-norvaline dehydrogenase.";
Nat. Struct. Biol. 5:593-601(1998).
Comments
  • FUNCTION: In the forward direction acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. In the reverse direction, the enzyme also acts on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine.
  • CATALYTIC ACTIVITY: (2S)-2-((1-(R)-carboxyethyl)amino)pentanoate + NAD+ + H2O = L-2-aminopentanoic acid + pyruvate + NADH.
  • SUBUNIT: Homodimer.
  • SIMILARITY: Belongs to the lysopine/nopaline/octopine/opine/vitopine dehydrogenases family.
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
D45211; BAA08145.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I39664; I39664.
3D structure databases
PDB
1BG6; X-ray; 1.80 A; A=1-359.[ExPASy / RCSB / EBI]
PDBsum 1BG6; -.
ModBase Q44297.
Family and domain databases
InterPro IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR006168; NAD-dep_Gly3P_DHase.
IPR011128; NAD-dep_Gly3P_DHase_N.
IPR003421; Opine_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR11728; NAD_Gly3P_DH; 1.
Pfam PF01210; NAD_Gly3P_dh_N; 1.
PF02317; Octopine_DH; 1.
Pfam graphical view of domain structure.
BLOCKS Q44297.
Other
ProtoNet Q44297.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   359  359     Opine dehydrogenase. PRO_0000179982
STRAND   6    10  5      
HELIX   14    25  12      
STRAND   29    33  5      
HELIX   37    46  10      
STRAND   48    55  8      
STRAND   58    60  3      
STRAND   63    67  5      
HELIX   69    73  5      
STRAND   77    81  5      
HELIX   85    87  3      
HELIX   88    95  8      
HELIX   96    98  3      
STRAND   104   109  6      
HELIX   114   124  11      
STRAND   131   137  7      
STRAND   139   143  5      
STRAND   149   155  7      
STRAND   159   165  7      
HELIX   166   168  3      
HELIX   169   176  8      
TURN   177   179  3      
STRAND   183   185  3      
HELIX   189   194  6      
HELIX   197   201  5      
HELIX   203   207  5      
HELIX   210   214  5      
HELIX   221   225  5      
HELIX   228   246  19      
TURN   247   249  3      
HELIX   255   258  4      
HELIX   270   275  6      
HELIX   278   280  3      
STRAND   287   289  3      
HELIX   292   299  8      
HELIX   302   311  10      
HELIX   317   329  13      
HELIX   334   337  4      
TURN   341   345  5      
HELIX   351   358  8      
Sequence information
Length: 359 AA [This is the length of the unprocessed precursor] Molecular weight: 37937 Da [This is the MW of the unprocessed precursor] CRC64: 7542D8A44D859028 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIESKTYAVL GLGNGGHAFA AYLALKGQSV LAWDIDAQRI KEIQDRGAII AEGPGLAGTA 

        70         80         90        100        110        120 
HPDLLTSDIG LAVKDADVIL IVVPAIHHAS IAANIASYIS EGQLIILNPG ATGGALEFRK 

       130        140        150        160        170        180 
ILRENGAPEV TIGETSSMLF TCRSERPGQV TVNAIKGAMD FACLPAAKAG WALEQIGSVL 

       190        200        210        220        230        240 
PQYVAVENVL HTSLTNVNAV MHPLPTLLNA ARCESGTPFQ YYLEGITPSV GSLAEKVDAE 

       250        260        270        280        290        300 
RIAIAKAFDL NVPSVCEWYK ESYGQSPATI YEAVQGNPAY RGIAGPINLN TRYFFEDVST 

       310        320        330        340        350 
GLVPLSELGR AVNVPTPLID AVLDLISSLI DTDFRKEGRT LEKLGLSGLT AAGIRSAVE 

Q44297 in FASTA format

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