GMP reductase

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

<p>Describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the ‘Names and taxonomy’ section.</p><p><a href='../manual/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	181 – 181	1	Potassium; via carbonyl oxygenBy similarity
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	183 – 183	1	Potassium; via carbonyl oxygenBy similarity
<p>Is used for enzymes and indicates the residues directly involved in catalysis.</p><p><a href='../manual/act_site' target='_top'>More...</a></p>Active sitei	186 – 186	1	Thioimidate intermediateBy similarity

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>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><p><a href='../manual/np_bind' target='_top'>More...</a></p>Nucleotide bindingi	108 – 131	24	NADPBy similarity			Add BLAST
<p>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><p><a href='../manual/np_bind' target='_top'>More...</a></p>Nucleotide bindingi	216 – 239	24	NADPBy similarity			Add BLAST

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• GMP reductase activity Source: EcoCyc

  <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

  • 21298178

• identical protein binding Source: EcoCyc

  <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

  • 21298178

• metal ion binding Source: UniProtKB-KW

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

• purine ribonucleotide interconversion Source: EcoCyc

  <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

  • 14419794

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Ligandⁱ

Enzyme and pathway databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

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

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

• cytosol Source: EcoCyc

  <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

  • 15911532
  • 18304323

• GMP reductase complex Source: UniProtKB-EC

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

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 347	347	GMP reductase		PRO_0000093735	Add BLAST

Proteomic databases

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

<p>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="/help/function_section">‘Function’</a> section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>Provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.</p><p><a href='../manual/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• identical protein binding Source: EcoCyc

  <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

  • 21298178

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

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

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the <a href="/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQSWSGVPII 
        60         70         80         90        100
AANMDTVGTF SMASALASFD ILTAVHKHYS VEEWQAFINN SSADVLKHVM 
       110        120        130        140        150
VSTGTSDADF EKTKQILDLN PALNFVCIDV ANGYSEHFVQ FVAKAREAWP 
       160        170        180        190        200
TKTICAGNVV TGEMCEELIL SGADIVKVGI GPGSVCTTRV KTGVGYPQLS 
       210        220        230        240        250
AVIECADAAH GLGGMIVSDG GCTTPGDVAK AFGGGADFVM LGGMLAGHEE 
       260        270        280        290        300
SGGRIVEENG EKFMLFYGMS SESAMKRHVG GVAEYRAAEG KTVKLPLRGP 
       310        320        330        340 
VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNNL 

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	233 – 235	3	GGG → AR (PubMed:2904262).Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	233 – 235	3	GGG → AR (PubMed:8202364).Curated

Sequence databases

Genome annotation databases

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

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Technical termⁱ

Documents

1. Escherichia coli
   Escherichia coli (strain K12): entries and cross-references to EcoGene
2. SIMILARITY comments
   Index of protein domains and families

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ