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Entry version 142 (07 Oct 2020)
Sequence version 1 (01 Nov 1995)
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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
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 last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.UniRule annotation1 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

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

<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: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Bifunctional protein GlmU (glmU)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional protein GlmU (glmU)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate, the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: LPS lipid A biosynthesis

This protein is involved in the pathway LPS lipid A biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway LPS lipid A biosynthesis and in Bacterial outer membrane biogenesis.

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 sitei25UDP-GlcNAcUniRule annotation1
Binding sitei76UDP-GlcNAcUniRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi105MagnesiumUniRule annotation1
Binding sitei140UDP-GlcNAc; via amide nitrogenUniRule annotation1 Publication1
Binding sitei154UDP-GlcNAcUniRule annotation1 Publication1
Binding sitei169UDP-GlcNAcUniRule annotation1 Publication1
Metal bindingi227MagnesiumUniRule annotation1
Binding sitei227UDP-GlcNAcUniRule annotation1
Binding sitei333UDP-GlcNAcUniRule annotation1
Binding sitei351UDP-GlcNAcUniRule annotation1
<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 sitei363Proton acceptorUniRule annotation1
Binding sitei366UDP-GlcNAcUniRule annotation1
Binding sitei377UDP-GlcNAcUniRule annotation1
Binding sitei380Acetyl-CoA; via amide nitrogenUniRule annotationBy similarity1
Binding sitei405Acetyl-CoAUniRule annotation1
Binding sitei423Acetyl-CoA; via amide nitrogenUniRule annotation1
Binding sitei440Acetyl-CoAUniRule annotation1

<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 functionAcyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Transferase
Biological processCell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
HINF71421:G1GJ1-673-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.23, 2529

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

More...
UniPathwayi
UPA00113;UER00532
UPA00113;UER00533
UPA00973

<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:
Bifunctional protein GlmUUniRule annotation
Including the following 2 domains:
UDP-N-acetylglucosamine pyrophosphorylaseUniRule annotation (EC:2.7.7.23UniRule annotation)
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation
Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation (EC:2.3.1.157UniRule annotation)
<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:glmUUniRule annotation
Ordered Locus Names:HI_0642
<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>OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
<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 identifieri71421 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
<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
  • UP000000579 <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>Mutagenesisi25K → A: No pyrophosphorylase activity. 1 Publication1
Mutagenesisi76Q → A: No pyrophosphorylase activity. 1 Publication1
Mutagenesisi103Y → A: Reduces the pyrophosphorylase activity. 1 Publication1
Mutagenesisi105D → A: No pyrophosphorylase activity. 1 Publication1
Mutagenesisi223V → A: Reduces slightly the pyrophosphorylase activity. 1 Publication1
Mutagenesisi224E → A: Reduces the pyrophosphorylase activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB08344, 4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide

<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_00000687031 – 456Bifunctional protein GlmUAdd BLAST456

<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

Homotrimer.

UniRule annotation3 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
71421.HI_0642

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P43889

<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

1456
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
P43889

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
P43889

<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>Regioni1 – 229PyrophosphorylaseUniRule annotationAdd BLAST229
Regioni11 – 14UDP-GlcNAc bindingUniRule annotation3 Publications4
Regioni81 – 82UDP-GlcNAc bindingUniRule annotation2 Publications2
Regioni103 – 105UDP-GlcNAc bindingUniRule annotation3 Publications3
Regioni230 – 250LinkerUniRule annotationAdd BLAST21
Regioni251 – 456N-acetyltransferaseUniRule annotationAdd BLAST206
Regioni386 – 387Acetyl-CoA bindingUniRule annotation2

<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

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.UniRule annotationCurated
In the C-terminal section; belongs to the transferase hexapeptide repeat family.UniRule annotationCurated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1207, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_029499_15_2_6

KEGG Orthology (KO)

More...
KOi
K04042

Identification of Orthologs from Complete Genome Data

More...
OMAi
TAIVEHK

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P43889

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03353, LbH_GlmU_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.550.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01631, GlmU, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005882, Bifunctional_GlmU
IPR038009, GlmU_C_LbH
IPR001451, Hexapep
IPR018357, Hexapep_transf_CS
IPR025877, MobA-like_NTP_Trfase
IPR029044, Nucleotide-diphossugar_trans
IPR011004, Trimer_LpxA-like_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00132, Hexapep, 3 hits
PF12804, NTP_transf_3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51161, SSF51161, 1 hit
SSF53448, SSF53448, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01173, glmU, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00101, HEXAPEP_TRANSFERASES, 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.

P43889-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTKKALSAVI LAAGKGTRMY SDLPKVLHTI AGKPMVKHVI DTAHQLGSEN
60 70 80 90 100
IHLIYGHGGD LMRTHLANEQ VNWVLQTEQL GTAHAVQQAA PFFKDNENIV
110 120 130 140 150
VLYGDAPLIT KETLEKLIEA KPENGIALLT VNLDNPTGYG RIIRENGNVV
160 170 180 190 200
AIVEQKDANA EQLNIKEVNT GVMVSDGASF KKWLARVGNN NAQGEYYLTD
210 220 230 240 250
LIALANQDNC QVVAVQATDV MEVEGANNRL QLAALERYFQ NKQASKLLLE
260 270 280 290 300
GVMIYDPARF DLRGTLEHGK DVEIDVNVII EGNVKLGDRV KIGTGCVLKN
310 320 330 340 350
VVIGNDVEIK PYSVLEDSIV GEKAAIGPFS RLRPGAELAA ETHVGNFVEI
360 370 380 390 400
KKSTVGKGSK VNHLTYVGDS EIGSNCNIGA GVITCNYDGA NKFKTIIGDD
410 420 430 440 450
VFVGSDTQLV APVKVANGAT IGAGTTITRD VGENELVITR VAQRHIQGWQ

RPIKKK
Length:456
Mass (Da):49,287
Last modified:November 1, 1995 - 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:i93B76552A8F9BD36
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
L42023 Genomic DNA Translation: AAC22302.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G64083

NCBI Reference Sequences

More...
RefSeqi
NP_438802.1, NC_000907.1
WP_005694502.1, NC_000907.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC22302; AAC22302; HI_0642

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hin:HI0642

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|71421.8.peg.670

<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
L42023 Genomic DNA Translation: AAC22302.1
PIRiG64083
RefSeqiNP_438802.1, NC_000907.1
WP_005694502.1, NC_000907.1

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
2V0HX-ray1.79A1-456[»]
2V0IX-ray1.89A1-456[»]
2V0JX-ray2.00A1-456[»]
2V0KX-ray2.30A1-456[»]
2V0LX-ray2.20A1-456[»]
2VD4X-ray1.90A1-456[»]
2W0VX-ray1.99A1-456[»]
2W0WX-ray2.59A1-456[»]
4E1KX-ray2.00A1-456[»]
4KNRX-ray2.10A1-456[»]
4KNXX-ray1.90A1-456[»]
4KPXX-ray2.21A1-456[»]
4KPZX-ray2.09A1-456[»]
4KQLX-ray2.31A1-456[»]
SMRiP43889
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi71421.HI_0642

Chemistry databases

BindingDBiP43889
DrugBankiDB08344, 4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide

Genome annotation databases

EnsemblBacteriaiAAC22302; AAC22302; HI_0642
KEGGihin:HI0642
PATRICifig|71421.8.peg.670

Phylogenomic databases

eggNOGiCOG1207, Bacteria
HOGENOMiCLU_029499_15_2_6
KOiK04042
OMAiTAIVEHK
PhylomeDBiP43889

Enzyme and pathway databases

UniPathwayiUPA00113;UER00532
UPA00113;UER00533
UPA00973
BioCyciHINF71421:G1GJ1-673-MONOMER
BRENDAi2.7.7.23, 2529

Miscellaneous databases

EvolutionaryTraceiP43889

Protein Ontology

More...
PROi
PR:P43889

Family and domain databases

CDDicd03353, LbH_GlmU_C, 1 hit
Gene3Di3.90.550.10, 1 hit
HAMAPiMF_01631, GlmU, 1 hit
InterProiView protein in InterPro
IPR005882, Bifunctional_GlmU
IPR038009, GlmU_C_LbH
IPR001451, Hexapep
IPR018357, Hexapep_transf_CS
IPR025877, MobA-like_NTP_Trfase
IPR029044, Nucleotide-diphossugar_trans
IPR011004, Trimer_LpxA-like_sf
PfamiView protein in Pfam
PF00132, Hexapep, 3 hits
PF12804, NTP_transf_3, 1 hit
SUPFAMiSSF51161, SSF51161, 1 hit
SSF53448, SSF53448, 1 hit
TIGRFAMsiTIGR01173, glmU, 1 hit
PROSITEiView protein in PROSITE
PS00101, HEXAPEP_TRANSFERASES, 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 nameiGLMU_HAEIN
<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: P43889
<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: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 7, 2020
This is version 142 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, Reference proteome

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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