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Entry version 81 (12 Aug 2020)
Sequence version 1 (01 Jun 2001)
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Protein

Octopine dehydrogenase

Gene

odh1

Organism
Pecten maximus (King scallop) (Pilgrim's clam)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the reverse reaction of octopine dehydrogenation. Acts on L-arginine in preference to other substrates such as canavanine, cysteine, L-alanine, ornithine or norvaline, owing to the presence of the positively charged guanidium group.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Agmatine acts as a competitive inhibitor of the condensation reaction where the L-arginine and agmatine substrates compete for the same site.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

The kinetic constants are determined for the recombinant His5-tagged protein.2 Publications
  1. KM=0.8 mM for pyruvate for the reverse reaction of the octopine dehydrogenase activity2 Publications
  2. KM=0.5 mM for L-arginine for the reverse reaction of the octopine dehydrogenase activity2 Publications
  3. KM=0.0198 mM for NADH for the reverse reaction of the octopine dehydrogenase activity2 Publications
  4. KM=5.9 mM for ketobutyrate for the reverse reaction of the octopine dehydrogenase activity2 Publications
  5. KM=49.8 mM for ketovalerate for the reverse reaction of the octopine dehydrogenase activity2 Publications
  1. Vmax=1074 µmol/min/mg enzyme with pyruvate as substrate for the reverse reaction of the octopine dehydrogenase activity2 Publications
  2. Vmax=886 µmol/min/mg enzyme with L-arginine as substrate for the reverse reaction of the octopine dehydrogenase activity2 Publications
  3. Vmax=903 µmol/min/mg enzyme with NADH as substrate for the reverse reaction of the octopine dehydrogenase activity2 Publications
  4. Vmax=728 µmol/min/mg enzyme with ketobutyrate as substrate for the reverse reaction of the octopine dehydrogenase activity2 Publications
  5. Vmax=377 µmol/min/mg enzyme with ketovalerate as substrate for the reverse reaction of the octopine dehydrogenase activity2 Publications

pH dependencei

Optimum pH is 8.0-9.5 for the forward reaction and 6.5-7.5 for the reverse reaction.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei118Pyruvate1 Publication1
Binding sitei118Substrate1
Binding sitei143Pyruvate1 Publication1
Binding sitei148NAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei206L-arginine; via carbonyl oxygen1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei2121 Publication1
Binding sitei212Pyruvate1 Publication1
Binding sitei324NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi10 – 13NADH2 Publications4
Nucleotide bindingi35 – 38NADH2 Publications4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
LigandNAD, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:MONOMER-17683

BRENDA Comprehensive Enzyme Information System

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BRENDAi
1.5.1.11, 4573

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Octopine dehydrogenaseImported (EC:1.5.1.11Imported)
Short name:
OcDH1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:odh1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPecten maximus (King scallop) (Pilgrim's clam)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri6579 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaSpiraliaLophotrochozoaMolluscaBivalviaPteriomorphiaPectinoidaPectinoideaPectinidaePecten

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi118Q → A: Drastically reduced enzymatic activity. 1 Publication1
Mutagenesisi118Q → D: Drastically reduced enzymatic activity. Greater effect on catalytic efficiency for pyruvate than L-arginine or NADH. 1 Publication1
Mutagenesisi148C → A or S: Reduced catalytic efficiency but no change in the activity. 3-fold decrease in affinity for pyruvate, 3-fold decrease for L-arginine and 2-fold decrease for NADH. 1 Publication1
Mutagenesisi212H → A: 2 to 10-fold decrease in specific activity. 77-fold reduction in affinity for pyruvate, 6-fold decrease for L-arginine and 3-fold decrease for NADH. 1 Publication1
Mutagenesisi324R → A: 2 to 10-fold decrease in specific activity. 119-fold reduction in affinity for pyruvate, 200-fold reduction for L-arginine and 4-fold reduction for NADH. 1 Publication1
Mutagenesisi329D → A: 2 to 10-fold decrease in specific activity. 43-fold reduction in affinity for pyruvate and 18-fold reduction for L-arginine. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004146261 – 399Octopine dehydrogenaseAdd BLAST399

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1399
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9BHM6

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9BHM6

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

KEGG Orthology (KO)

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KOi
K23233

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1040.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR008927, 6-PGluconate_DH-like_C_sf
IPR013328, 6PGD_dom2
IPR036291, NAD(P)-bd_dom_sf
IPR003421, Opine_DH

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02317, Octopine_DH, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48179, SSF48179, 1 hit
SSF51735, SSF51735, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q9BHM6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTVKVCVCGG GNGAHTLSGL AASRDGVEVR VLTLFADEAE RWTKALGADE
60 70 80 90 100
LTVIVNEKDG TQTEVKSRPK VITKDPEIAI SGADVVILTV PAFAHEGYFQ
110 120 130 140 150
AMAPYVQDSA LIVGLPSQAG FEFQCRDILG DKAAAVSMMS FETLPWACRI
160 170 180 190 200
KEFGRKVEVL GTKSVLAASL IKGTAKTVDP LSTLQMLHGA EPVFRLAKHF
210 220 230 240 250
LEMLIMSYSF VHPAILFGRW GSWDGKPVPE APLFYQGIDQ ATADMLTACS
260 270 280 290 300
NECKDVANAI MAACPGNDLS DVKDIYQWYL EYYHEDIQDD HDLYHAITTN
310 320 330 340 350
KSYKGLVHPV KAVDGGVAPD FGNRYLTEDI PMGMIVFKGV AIAAGVAIPS
360 370 380 390
NDKLIMWAQE KIGKEYLVDG ALTGKDVATT RCPQRYGFNT LDAILTGKK
Length:399
Mass (Da):43,320
Last modified:June 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDA2DB070455B4C0F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AJ237916 mRNA Translation: CAC36305.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:CAC36305

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ237916 mRNA Translation: CAC36305.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C7AX-ray2.10A1-399[»]
3C7CX-ray3.10B1-399[»]
3C7DX-ray2.50B1-399[»]
3IQDX-ray2.80B1-399[»]
SMRiQ9BHM6
ModBaseiSearch...
PDBe-KBiSearch...

Genome annotation databases

KEGGiag:CAC36305

Phylogenomic databases

KOiK23233

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17683
BRENDAi1.5.1.11, 4573

Miscellaneous databases

EvolutionaryTraceiQ9BHM6

Family and domain databases

Gene3Di1.10.1040.10, 1 hit
InterProiView protein in InterPro
IPR008927, 6-PGluconate_DH-like_C_sf
IPR013328, 6PGD_dom2
IPR036291, NAD(P)-bd_dom_sf
IPR003421, Opine_DH
PfamiView protein in Pfam
PF02317, Octopine_DH, 1 hit
SUPFAMiSSF48179, SSF48179, 1 hit
SSF51735, SSF51735, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOCDH_PECMA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9BHM6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 14, 2011
Last sequence update: June 1, 2001
Last modified: August 12, 2020
This is version 81 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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