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Entry version 93 (16 Jan 2019)
Sequence version 1 (01 Jan 1998)
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Protein

Formate dehydrogenase

Gene

FDH1

Organism
Candida boidinii (Yeast)
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 NAD+-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.UniRule annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 ‘Function’ 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

Cu2+, Hg and p-chloromercuribenzoate are strong inhibitors of enzyme activity and Ca2+, Mg2+, Zn2+, Mn2+, Cd2+ and Sn2+ have no effect on activity indicating a cysteine residue in the protein is essential for enzyme activity or to maintain the proper structure of the enzyme. Nitrite and nitrate inhibit some enzyme activity, however cyanide, azide, thiocyanate and cyanate are strong inhibitors of the enzymic reaction. The inhibition of cyanide is competitive with formate and reversible.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

  1. KM=13 mM for formate (at 30 degrees Celsius and at pH 7.5)1 Publication
  2. KM=0.09 mM for NAD (at 30 degrees Celsius and at pH 7.5)1 Publication
  3. KM=5.6 mM for formate (at 30 degrees Celsius and at pH 7.5)1 Publication
  4. KM=0.045 mM for NAD (at 30 degrees Celsius and at pH 7.5)1 Publication
  5. KM=2.42 mM for formate (at 25 degrees Celsius and at pH 7.5)1 Publication
  6. KM=0.04 mM for NAD (at 25 degrees Celsius and at pH 7.5)1 Publication
  7. KM=2.4 mM for formate (at 25 degrees Celsius and at pH 7.6)1 Publication
  8. KM=0.04 mM for NAD (at 25 degrees Celsius and at pH 7.6)1 Publication
  9. KM=20.0 mM for formate (at 20 degrees Celsius, at pH 7.5 and after 2 weeks of storage at 4 degrees Celsius in GF buffer)1 Publication
  10. KM=0.05 mM for NAD (at 20 degrees Celsius, at pH 7.5 and after 2 weeks of storage at 4 degrees Celsius in GF buffer)1 Publication
  11. KM=35.0 mM for formate (at 20 degrees Celsius, at pH 7.5 and after 4 months of storage at 4 degrees Celsius in GF buffer)1 Publication
  12. KM=0.09 mM for NAD (at 20 degrees Celsius, at pH 7.5 and after 4 months of storage at 4 degrees Celsius in GF buffer)1 Publication
  1. Vmax=6 µM/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7.5-8.5.5 Publications

Temperature dependencei

Broad temperature optima between 45 and 55 degrees Celsius. Reaction rate increases steeply up to 55 degrees Celsius. 50% of activity lost after incubation for 20 minutes at 57 degrees Celsius. Thermal stability increases in the presence of glycerol.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei93Substrate; via amide nitrogenUniRule annotation1
Binding sitei119SubstrateUniRule annotation1
Binding sitei195NADUniRule annotation1
Binding sitei256NAD; via carbonyl oxygenUniRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei258Important for catalytic activityUniRule annotation1 Publication1
Binding sitei282NADUniRule annotation1
Sitei311Important for catalytic activityUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi174 – 175NADUniRule annotation2
Nucleotide bindingi230 – 234NADUniRule annotation5
Nucleotide bindingi311 – 314NADUniRule annotation4

<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

GO - Biological processi

<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
LigandATP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-17206

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.2.1.2 1100

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O13437

<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_and_taxonomy_section">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:
Formate dehydrogenaseUniRule annotationImported (EC:1.17.1.9UniRule annotation5 Publications)
Short name:
FDHUniRule annotation
Alternative name(s):
NAD-dependent formate dehydrogenaseUniRule annotationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:FDH11 PublicationImported
Synonyms:FDHImported, FDH3Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiCandida boidinii (Yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri5477 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPichiaceaeOgataeaOgataea/Candida clade

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Ideal catalyst for synthesizing chiral compounds of high enantiomeric purity from prochiral precursors due to a favorable thermodynamic equilibrium, the oxidation of formate to carbon dioxide while also reducing NAD to NADH. However, the necessesity for the presence of large quantities of the enzyme and its rapid inactivation under biotransformation conditions results in higher costs for the biocatalyst industry. In order to make this enzymatic reduction viable and to perform it on a larger scale a more efficient and cost effective process has been established. Site-directed mutagenesis has been effective in stabilizing this commercially important enzyme for its application in the biotransformation of trimethyl pyruvate to L-tert leucine.2 Publications

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Is able to grow on methanol in a batch culture experiment, but its growth is greatly inhibited and a toxic level of formate accumulates in the medium. Formate is not detected in the medium in a methanol-limited chemostat culture but deletion mutant shows only one-fourth of the growth yield of the wild-type.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi23C → S: Slight increase in substrate affinity for formate but no change in affinity for NAD, 9 degrees Celsius decrease in thermal stability compared to the wild-type, significantly higher stability compared to wild-type under biotransformation conditions, significantly more stable in the presence of CuCl(2); when associated with A-262. Large increase in substrate affinity for formate but no significant change in affinity for NAD, 13 degrees Celsius decrease in thermal stability compared to the wild-type, significantly more stable in the presence of CuCl(2); when associated with V-262. No significant change in affinity for formate or NAD, 5 degrees Celsius decrease in thermal stability compared to the wild-type, significantly higher stability compared to wild-type under biotransformation conditions, and significantly more stable in the presence of CuCl(2). 1 Publication1
Mutagenesisi47K → E: Slight increase in substrate affinity for formate and also affinity for NAD increases by half after 2 weeks. Also after 4 months affinity for formate increases by more than half and affinity for NAD increases by more than half. Retains 84% of residual activity after incubation for 20 minutes at a thermal inactivation temperature of 55 degrees Celsius in samples stored for 2 weeks compared to wild-type which loses 50% of its activity at 55 degrees Celsius. 1 Publication1
Mutagenesisi69F → A: 2-fold decrease in substrate affinity for formate, but no significant change in affinity for NAD. A significant reduction in catalytic activity compared to the wild-type. 1 Publication1
Mutagenesisi119N → A: 94-fold decrease in substrate affinity for formate and 2700-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type; when associated with A-311. 1 Publication1
Mutagenesisi119N → H: 80-fold decrease in substrate affinity for formate and a 1250-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type. 1 Publication1
Mutagenesisi175I → A: 2-fold decrease in substrate affinity for formate and a 12-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type. 1 Publication1
Mutagenesisi197Q → L: 4-fold decrease in substrate affinity for formate but no significant change in affinity for NAD compared to the wild-type. 1 Publication1
Mutagenesisi258R → A: No catalytic activity. 1 Publication1
Mutagenesisi262C → A: Slight increase in substrate affinity for formate but no change in affinity for NAD, 9 degrees Celsius decrease in thermal stability compared to the wild-type, greater stability at a higher pH compared to the wild-type; when associated with S-23. 1 Publication1
Mutagenesisi262C → V: Large increase in substrate affinity for formate but no significant change in affinity for NAD, 13 degrees Celsius decrease in thermal stability compared to the wild-type; when associated with S-23. Great increase in substrate affinity for formate and NAD and 8 degrees Celsius decrease in thermal stability compared to the wild-type. 1 Publication1
Mutagenesisi287Q → A: 2-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with A-311. 1 Publication1
Mutagenesisi287Q → E: 380-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with T-288. No significant decrease in substrate affinity for formate but a 4-fold decrease in substrate affinity for NAD and a significant reduction in catalytic activity compared to the wild-type, a more acidic pH is seen than in the wild-type, preventing formate binding by a single ionization of a group compared to that of the wild-type. 1 Publication1
Mutagenesisi288P → T: 380-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with E-287. 1 Publication1
Mutagenesisi311H → A: 2-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with A-287. 93-fold decrease in substrate affinity for formate and 2700-fold decrease in substrate affinity for NAD, and a significant reduction in catalytic activity compared to the wild-type; when associated with A-119. 1 Publication1
Mutagenesisi311H → Q: 10-fold decrease in substrate affinity for formate and significant reduction in the catalytic activity compared to the wild-type. 1 Publication1
Mutagenesisi328K → V: A 75% increase in substrate affinity for formate after 2 weeks and a 50% increase in affinity for NAD. However, after 4 months the affinity for formate increases 7-fold and affinity for NAD increases by 2 thirds. Retains 70% of residual activity after incubation for 20 minutes at a thermal inactivation temperature of 55 degrees Celsius in samples stored for 2 weeks compared to wild-type which loses 50% of its activity at 55 degrees Celsius. 1 Publication1
Mutagenesisi360K → A: Exhibits no change in substrate affinity for formate, but shows a 4-fold decrease in substrate affinity for NAD implying that L-360 side chain forms strong interactions with the cofactor. A higher reaction rate is observed at an acidic and basic pH values. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003939491 – 364Formate dehydrogenaseAdd BLAST364

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
O13437

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is strongly induced by methanol, but is completely repressed in the presence of glucose. However, methanol induced expression is equally strong in cells grown on glucose when formate, methylamine or choline is added. No expression is detected in cells grown on glycerol. When formate, methylamine or choline is added to the culture medium of glycerol- or glucose-grown cells, they exhibit an induction of FDH1 expression.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.UniRule annotation2 Publications

GO - Molecular functioni

<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

1364
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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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
2FSSX-ray1.70A/B/C/D2-364[»]
2J6IX-ray1.55A/B/C/D2-364[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O13437

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

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SMRi
O13437

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O13437

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 119CatalyticUniRule annotation1 PublicationAdd BLAST118
Regioni120 – 312Coenzyme-bindingUniRule annotation1 PublicationAdd BLAST193
Regioni313 – 358CatalyticUniRule annotation1 PublicationAdd BLAST46

<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

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.UniRule annotation

Phylogenomic databases

Database of Orthologous Groups

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OrthoDBi
700058at2759

Family and domain databases

Conserved Domains Database

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CDDi
cd05302 FDH, 1 hit

HAMAP database of protein families

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HAMAPi
MF_03210 Formate_dehydrogenase, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR006139 D-isomer_2_OHA_DH_cat_dom
IPR029753 D-isomer_DH_CS
IPR029752 D-isomer_DH_CS1
IPR006140 D-isomer_DH_NAD-bd
IPR033689 FDH_NAD-dep
IPR036291 NAD(P)-bd_dom_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF00389 2-Hacid_dh, 1 hit
PF02826 2-Hacid_dh_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51735 SSF51735, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00065 D_2_HYDROXYACID_DH_1, 1 hit
PS00670 D_2_HYDROXYACID_DH_2, 1 hit
PS00671 D_2_HYDROXYACID_DH_3, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

O13437-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKIVLVLYDA GKHAADEEKL YGCTENKLGI ANWLKDQGHE LITTSDKEGE
60 70 80 90 100
TSELDKHIPD ADIIITTPFH PAYITKERLD KAKNLKLVVV AGVGSDHIDL
110 120 130 140 150
DYINQTGKKI SVLEVTGSNV VSVAEHVVMT MLVLVRNFVP AHEQIINHDW
160 170 180 190 200
EVAAIAKDAY DIEGKTIATI GAGRIGYRVL ERLLPFNPKE LLYYDYQALP
210 220 230 240 250
KEAEEKVGAR RVENIEELVA QADIVTVNAP LHAGTKGLIN KELLSKFKKG
260 270 280 290 300
AWLVNTARGA ICVAEDVAAA LESGQLRGYG GDVWFPQPAP KDHPWRDMRN
310 320 330 340 350
KYGAGNAMTP HYSGTTLDAQ TRYAEGTKNI LESFFTGKFD YRPQDIILLN
360
GEYVTKAYGK HDKK
Length:364
Mass (Da):40,370
Last modified:January 1, 1998 - 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:i1B30982E0D5B77E8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti19 – 23KLYGC → EKLYG AA sequence (PubMed:11171126).Curated5
Sequence conflicti23C → T AA sequence (PubMed:7557425).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti9D → G in strain: 2.2159. CuratedImported1
Natural varianti50 – 51ET → GN in strain: 2.2159 and NCYC 1513. 1 Publication2
Natural varianti53E → V in strain: 2.2159 and NCYC 1513. 1 Publication1
Natural varianti56K → Q in strain: 2.2159 and NCYC 1513. 1 Publication1
Natural varianti79L → I in strain: 2.2159 and NCYC 1513. 1 Publication1
Natural varianti84N → K in strain: 2.2159 and NCYC 1513. 1 Publication1
Natural varianti87L → S in strain ATCC 56294 / CBS 8030 / CCRC 21757 / NRRL Y-17325. 1 Publication1
Natural varianti108K → R in strain: 2.2159. CuratedImported1
Natural varianti145I → N in strain: 2.2159. CuratedImported1
Natural varianti184L → V in strain: 2.2159 and NCYC 1513. 1 Publication1
Natural varianti202E → D in strain: 2.2159 and NCYC 1513. 1 Publication1
Natural varianti308M → T in strain: 2.2159. CuratedImported1
Natural varianti325E → Q in strain: 2.2159 and NCYC 1513. 1 Publication1

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

More...
DDBJi
Links Updated
X81129 Genomic DNA Translation: CAA57036.1
AF004096 Genomic DNA Translation: AAC49766.1
AJ245934 Genomic DNA Translation: CAB54834.1
AJ011046 Genomic DNA Translation: CAA09466.2
DQ458777 Genomic DNA Translation: ABE69165.2

Protein sequence database of the Protein Information Resource

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PIRi
JC4252

<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
X81129 Genomic DNA Translation: CAA57036.1
AF004096 Genomic DNA Translation: AAC49766.1
AJ245934 Genomic DNA Translation: CAB54834.1
AJ011046 Genomic DNA Translation: CAA09466.2
DQ458777 Genomic DNA Translation: ABE69165.2
PIRiJC4252

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FSSX-ray1.70A/B/C/D2-364[»]
2J6IX-ray1.55A/B/C/D2-364[»]
ProteinModelPortaliO13437
SMRiO13437
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO13437

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBi700058at2759

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17206
BRENDAi1.2.1.2 1100
SABIO-RKiO13437

Miscellaneous databases

EvolutionaryTraceiO13437

Family and domain databases

CDDicd05302 FDH, 1 hit
HAMAPiMF_03210 Formate_dehydrogenase, 1 hit
InterProiView protein in InterPro
IPR006139 D-isomer_2_OHA_DH_cat_dom
IPR029753 D-isomer_DH_CS
IPR029752 D-isomer_DH_CS1
IPR006140 D-isomer_DH_NAD-bd
IPR033689 FDH_NAD-dep
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF00389 2-Hacid_dh, 1 hit
PF02826 2-Hacid_dh_C, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00065 D_2_HYDROXYACID_DH_1, 1 hit
PS00670 D_2_HYDROXYACID_DH_2, 1 hit
PS00671 D_2_HYDROXYACID_DH_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiFDH_CANBO
<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: O13437
Secondary accession number(s): O93968, Q00498, Q1PAH3
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 1, 1998
Last modified: January 16, 2019
This is version 93 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)
Annotation programFungal Protein Annotation Program

<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, Direct protein sequencing

Documents

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