Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glucose-1-phosphate thymidylyltransferase

Gene

rmlA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Unreviewed-Annotation score:

Annotation score:3 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 formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.UniRule annotation

<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

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 sitei110TTPCombined sources1
Binding sitei111Glucose-1-phosphateCombined sources1
Binding sitei146Glucose-1-phosphate; via amide nitrogenCombined sources1
Binding sitei172Glucose-1-phosphate; via carbonyl oxygenCombined sources1
Binding sitei251TTP; via amide nitrogenCombined sources1
Binding sitei255TTPCombined sources1

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 bindingi10 – 15TTPCombined sources6
Nucleotide bindingi25 – 26TTPCombined sources2
Nucleotide bindingi82 – 87TTPCombined sources6
Nucleotide bindingi114 – 119TTPCombined sources6
Nucleotide bindingi219 – 220TTPCombined sources2

<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

  • glucose-1-phosphate thymidylyltransferase activity Source: PseudoCAP
  • metal ion binding Source: UniProtKB-KW
  • nucleotide binding Source: UniProtKB-KW

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 functionNucleotidyltransferaseUniRule annotation, Transferase
LigandMagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
PAER208964:G1FZ6-5280-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.24 5087

<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:
Glucose-1-phosphate thymidylyltransferaseUniRule annotation (EC:2.7.7.24UniRule annotation)
<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:rmlAImported
Ordered Locus Names:PA5163Imported
<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>OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)Imported
<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 identifieri208964 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002438 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

Organism-specific databases

Pseudomonas genome database

More...
PseudoCAPi
PA5163

<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

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03723 2'-Deoxy-Thymidine-Beta-L-Rhamnose
DB03751 2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose
DB02843 alpha-D-glucose-1-phosphate
DB04272 Citric Acid
DB04485 Deoxythymidine
DB01643 Thymidine-5'-Phosphate
DB02452 Thymidine-5'-Triphosphate

<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

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9HU22

PRoteomics IDEntifications database

More...
PRIDEi
Q9HU22

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
208964.PA5163

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q9HU22

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q9HU22

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

More...
SMRi
Q9HU22

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9HU22

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 240NTP_transferaseInterPro annotationAdd BLAST237

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>Regioni161 – 162Glucose-1-phosphate bindingCombined sources2

<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 glucose-1-phosphate thymidylyltransferase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4108I19 Bacteria
COG1209 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000283473

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9HU22

KEGG Orthology (KO)

More...
KOi
K00973

Identification of Orthologs from Complete Genome Data

More...
OMAi
GPYPMIY

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9HU22

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02538 G1P_TT_short, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.550.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005907 G1P_thy_trans_s
IPR005835 NTP_transferase_dom
IPR029044 Nucleotide-diphossugar_trans

The PANTHER Classification System

More...
PANTHERi
PTHR43532 PTHR43532, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00483 NTP_transferase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53448 SSF53448, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01207 rmlA, 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.

Q9HU22-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRKGIILAG GSGTRLHPAT LAISKQLLPV YDKPMIYYPL STLMLAGIRE
60 70 80 90 100
ILIISTPQDT PRFQQLLGDG SNWGLDLQYA VQPSPDGLAQ AFLIGESFIG
110 120 130 140 150
NDLSALVLGD NLYYGHDFHE LLGSASQRQT GASVFAYHVL DPERYGVVEF
160 170 180 190 200
DQGGKAISLE EKPLEPKSNY AVTGLYFYDQ QVVDIARDLK PSPRGELEIT
210 220 230 240 250
DVNRAYLERG QLSVEIMGRG YAWLDTGTHD SLLEAGQFIA TLENRQGLKV
260 270 280 290
ACPEEIAYRQ KWIDAAQLEK LAAPLAKNGY GQYLKRLLTE TVY
Length:293
Mass (Da):32,457
Last modified:March 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:i1E249F4359DC0553
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
AE004091 Genomic DNA Translation: AAG08548.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D83000

NCBI Reference Sequences

More...
RefSeqi
NP_253850.1, NC_002516.2
WP_003105518.1, NC_002516.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAG08548; AAG08548; PA5163

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
879990

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pae:PA5163

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|208964.12.peg.5411

<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
AE004091 Genomic DNA Translation: AAG08548.1
PIRiD83000
RefSeqiNP_253850.1, NC_002516.2
WP_003105518.1, NC_002516.2

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
1FXOX-ray1.66A/B/C/D/E/F/G/H1-293[»]
1FZWX-ray1.90A/B/C/D/E/F/G/H1-293[»]
1G0RX-ray1.87A/B/C/D/E/F/G/H1-293[»]
1G1LX-ray1.77A/B/C/D/E/F/G/H1-293[»]
1G23X-ray2.80A/B/C/D/E/F/G/H1-293[»]
1G2VX-ray2.60A/B/C/D/E/F/G/H1-293[»]
1G3LX-ray2.70A/B/C/D1-293[»]
3ZLKX-ray1.95A/B/C/D1-293[»]
3ZLLX-ray2.00A/B/C/D1-293[»]
4ARWX-ray2.20A/B/C/D1-293[»]
4ASJX-ray2.25A/B/C/D1-293[»]
4ASYX-ray2.30A/B/C/D1-293[»]
4B2WX-ray2.36A/B/C/D1-293[»]
4B2XX-ray1.70A/B/C/D1-293[»]
4B3UX-ray1.80A/B/C/D1-293[»]
4B42X-ray2.50A/B/C/D1-293[»]
4B4BX-ray2.10A/B/C/D1-293[»]
4B4GX-ray2.50A/B/C/D1-293[»]
4B4MX-ray2.35A/B/C/D1-293[»]
4B5BX-ray2.06A/B/C/D1-293[»]
5FTSX-ray2.20A/B/C/D1-293[»]
5FTVX-ray2.21A/B/C/D1-293[»]
5FU0X-ray1.90A/B/C/D1-293[»]
5FU8X-ray2.20A/B/C/D1-293[»]
5FUHX-ray1.60A/B/C/D1-293[»]
5FYEX-ray2.40A/B/C/D1-293[»]
ProteinModelPortaliQ9HU22
SMRiQ9HU22
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5163

Chemistry databases

BindingDBiQ9HU22
DrugBankiDB03723 2'-Deoxy-Thymidine-Beta-L-Rhamnose
DB03751 2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose
DB02843 alpha-D-glucose-1-phosphate
DB04272 Citric Acid
DB04485 Deoxythymidine
DB01643 Thymidine-5'-Phosphate
DB02452 Thymidine-5'-Triphosphate

Proteomic databases

PaxDbiQ9HU22
PRIDEiQ9HU22

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08548; AAG08548; PA5163
GeneIDi879990
KEGGipae:PA5163
PATRICifig|208964.12.peg.5411

Organism-specific databases

PseudoCAPiPA5163

Phylogenomic databases

eggNOGiENOG4108I19 Bacteria
COG1209 LUCA
HOGENOMiHOG000283473
InParanoidiQ9HU22
KOiK00973
OMAiGPYPMIY
PhylomeDBiQ9HU22

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-5280-MONOMER
BRENDAi2.7.7.24 5087

Miscellaneous databases

EvolutionaryTraceiQ9HU22

Family and domain databases

CDDicd02538 G1P_TT_short, 1 hit
Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR005907 G1P_thy_trans_s
IPR005835 NTP_transferase_dom
IPR029044 Nucleotide-diphossugar_trans
PANTHERiPTHR43532 PTHR43532, 1 hit
PfamiView protein in Pfam
PF00483 NTP_transferase, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit
TIGRFAMsiTIGR01207 rmlA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiQ9HU22_PSEAE
<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: Q9HU22
Secondary accession number(s): Q7AYQ9
<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/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: December 5, 2018
This is version 124 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 statusiUnreviewed (UniProtKB/TrEMBL)

<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-structureCombined sources, Complete proteome, Reference proteomeImported
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again