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Entry version 81 (12 Aug 2020)
Sequence version 1 (06 Mar 2007)
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Protein

Dihydroorotate dehydrogenase A (fumarate)

Gene

pyrDA

Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
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 conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro, but cannot use NAD+ as an electron acceptor.1 Publication

<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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FMN2 PublicationsNote: Binds 1 FMN per subunit.2 Publications

<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=18 µM for dihydroorotate1 Publication
  2. KM=250 µM for fumarate1 Publication
  1. Vmax=18.6 µmol/min/mg enzyme1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in the pathway UMP biosynthesis via de novo pathway, which is part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

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 sitei19FMN2 Publications1
Binding sitei43Substrate1
Binding sitei127FMN2 Publications1
Binding sitei127Substrate1
<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 sitei130Nucleophile1
Binding sitei164FMN2 Publications1
Binding sitei192FMN; via carbonyl oxygen2 Publications1
Binding sitei221FMN; via amide nitrogen2 Publications1

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 bindingi43 – 44FMN2 Publications2
Nucleotide bindingi249 – 250FMN2 Publications2
Nucleotide bindingi271 – 272FMN2 Publications2

<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
Biological processPyrimidine biosynthesis
LigandFlavoprotein, FMN

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
LLAC416870:LLMG_RS04850-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.3.1.14, 2903

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00070

<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:
Dihydroorotate dehydrogenase A (fumarate) (EC:1.3.98.1)
Short name:
DHOD A
Short name:
DHODase A
Short name:
DHOdehase A
<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:pyrDA
Ordered Locus Names:llmg_0952
<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>OrganismiLactococcus lactis subsp. cremoris (strain MG1363)
<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 identifieri416870 [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 lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000364 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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

GO - Cellular componenti

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

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>Mutagenesisi43K → A: More than 500-fold reduction of enzymatic activity with oxygen or DCIP as electron acceptor. 1 Publication1
Mutagenesisi43K → E: 40-fold reduction of enzymatic activity with oxygen as electron acceptor; more than 120-fold reduction with DCIP as electron acceptor. 1 Publication1
Mutagenesisi50R → E: Steady state kinetics comparable to wild-type; 3-fold decrease in flavin bleaching rate. 1 Publication1
Mutagenesisi56P → A: More than 500-fold reduction of enzymatic activity. 1 Publication1
Mutagenesisi57R → A: More active than wild-type, especially with 2,6-dichloroindophenol as electron acceptor. 1 Publication1
Mutagenesisi67N → A: 100-fold lower affinity for dihydroorotate. 1 Publication1
Mutagenesisi127N → A: 70-fold lower affinity for dihydroorotate; inhibited by milimolar concentrations of fumarate. 1 Publication1
Mutagenesisi129S → A: 6-fold lower enzymatic activity with fumarate as electron acceptor. 1 Publication1
Mutagenesisi130C → A or S: Almost total loss of activity with oxygen or 2,6-dichloroindophenol as electron acceptor. 1 Publication1
Mutagenesisi131P → A: 4.5-fold lower enzymatic activity with fumarate and 2,6-dichloroindophenol as electron acceptor. 1 Publication1
Mutagenesisi132N → A: 54-fold reduction of enzymatic activity with oxygen as electron acceptor; more than 250-fold reduction with 2,6-dichloroindophenol as electron acceptor. 2 Publications1
Mutagenesisi136K → A: Slightly higher affinity to dihydroorotate; 2-fold decrease in flavin bleaching rate. 1 Publication1
Mutagenesisi164K → A: Almost total loss of activity with oxygen or 2,6-dichloroindophenol as electron acceptor. 1 Publication1
Mutagenesisi193N → A: 500-fold lower affinity for dihydroorotate; inhibited by milimolar concentrations of fumarate. 1 Publication1
Mutagenesisi213K → A: 7-fold decrease in enzymatic activity; 50-fold decrease in flavin bleaching rate. 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_00002852391 – 311Dihydroorotate dehydrogenase A (fumarate)Add BLAST311

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
416870.llmg_0952

<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

1311
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

More...
SMRi
A2RJT9

Database of comparative protein structure models

More...
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
A2RJT9

<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>Regioni67 – 71Substrate binding5
Regioni193 – 194Substrate binding2

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0167, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_042042_3_0_9

KEGG Orthology (KO)

More...
KOi
K00226

Identification of Orthologs from Complete Genome Data

More...
OMAi
TNTLGSC

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04741, DHOD_1A_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.26.10, 1 hit
3.20.20.70, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00224, DHO_dh_type1, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785, Aldolase_TIM
IPR033886, DHOD_1A
IPR023359, Dihydro_DH_chainA_dom2
IPR005720, Dihydroorotate_DH
IPR024920, Dihydroorotate_DH_1
IPR012135, Dihydroorotate_DH_1_2
IPR001295, Dihydroorotate_DH_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01180, DHO_dh, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000164, DHO_oxidase, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01037, pyrD_sub1_fam, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00911, DHODEHASE_1, 1 hit
PS00912, DHODEHASE_2, 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.

A2RJT9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLNTTFANAK FANPFMNASG VHCMTIEDLE ELKASQAGAY ITKSSTLEKR
60 70 80 90 100
EGNPLPRYVD LELGSINSMG LPNLGFDYYL DYVLKNQKEN AQEGPIFFSI
110 120 130 140 150
AGMSAAENIA MLKKIQESDF SGITELNLSC PNVPGKPQLA YDFEATEKLL
160 170 180 190 200
KEVFTFFTKP LGVKLPPYFD LVHFDIMAEI LNQFPLTYVN SVNSIGNGLF
210 220 230 240 250
IDPEAESVVI KPKDGFGGIG GAYIKPTALA NVRAFYTRLK PEIQIIGTGG
260 270 280 290 300
IETGQDAFEH LLCGATMLQI GTALHKEGPA IFDRIIKELE EIMNQKGYQS
310
IADFHGKLKS L
Length:311
Mass (Da):34,210
Last modified:March 6, 2007 - 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:i30157E3C2791CDD7
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X74206 Genomic DNA Translation: CAA52279.1
AM406671 Genomic DNA Translation: CAL97544.1

NCBI Reference Sequences

More...
RefSeqi
WP_011834894.1, NZ_WJVF01000006.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAL97544; CAL97544; llmg_0952

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
llm:llmg_0952

<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
X74206 Genomic DNA Translation: CAA52279.1
AM406671 Genomic DNA Translation: CAL97544.1
RefSeqiWP_011834894.1, NZ_WJVF01000006.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DORX-ray2.00A/B1-311[»]
1JQVX-ray2.10A/B1-311[»]
1JQXX-ray1.70A/B1-311[»]
1JRBX-ray1.90A/B1-311[»]
1JRCX-ray1.80A/B1-311[»]
1JUBX-ray1.40A/B1-311[»]
1JUEX-ray1.80A/B1-311[»]
1NFCmodel-A1-311[»]
1OVDX-ray2.25A/B1-311[»]
2BSLX-ray2.30A/B1-311[»]
2BX7X-ray2.04A/B1-311[»]
2DORX-ray2.00A/B1-311[»]
SMRiA2RJT9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi416870.llmg_0952

Genome annotation databases

EnsemblBacteriaiCAL97544; CAL97544; llmg_0952
KEGGillm:llmg_0952

Phylogenomic databases

eggNOGiCOG0167, Bacteria
HOGENOMiCLU_042042_3_0_9
KOiK00226
OMAiTNTLGSC

Enzyme and pathway databases

UniPathwayiUPA00070
BioCyciLLAC416870:LLMG_RS04850-MONOMER
BRENDAi1.3.1.14, 2903

Miscellaneous databases

EvolutionaryTraceiA2RJT9

Family and domain databases

CDDicd04741, DHOD_1A_like, 1 hit
Gene3Di2.30.26.10, 1 hit
3.20.20.70, 1 hit
HAMAPiMF_00224, DHO_dh_type1, 1 hit
InterProiView protein in InterPro
IPR013785, Aldolase_TIM
IPR033886, DHOD_1A
IPR023359, Dihydro_DH_chainA_dom2
IPR005720, Dihydroorotate_DH
IPR024920, Dihydroorotate_DH_1
IPR012135, Dihydroorotate_DH_1_2
IPR001295, Dihydroorotate_DH_CS
PfamiView protein in Pfam
PF01180, DHO_dh, 1 hit
PIRSFiPIRSF000164, DHO_oxidase, 1 hit
TIGRFAMsiTIGR01037, pyrD_sub1_fam, 1 hit
PROSITEiView protein in PROSITE
PS00911, DHODEHASE_1, 1 hit
PS00912, DHODEHASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
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 nameiPYRDA_LACLM
<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: A2RJT9
Secondary accession number(s): P54321
<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: May 1, 2007
Last sequence update: March 6, 2007
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)
Annotation programProkaryotic 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

Documents

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