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Entry version 115 (26 Feb 2020)
Sequence version 1 (01 Dec 2001)
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Protein

Bifunctional sugar-1-phosphate nucleotidylyltransferase/acetyltransferase

Gene

STK_04520

Organism
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
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

Bifunctional enzyme involved in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-N-acetylgalactosamine (UDP-GalNAc). It has multiple amino-sugar-1-phosphate acetyltransferase activities, including glucosamine-1-phosphate (GlcN-1-P) acetyltransferase and galactosamine-1-phosphate (GalN-1-P) acetyltransferase activities, and multiple sugar-1-phosphate nucleotidylyltransferase activities, including N-acetylglucosamine-1-phosphate (GlcNAc-1-P) uridyltransferase and N-acetylgalactosamine-1-phosphate (GalNAc-1-P) uridyltransferase activities (PubMed:15598657, PubMed:20400541, PubMed:25567746). Also catalyzes the formation of dTDP-glucose from dTTP and glucose-1-phosphate (Glc-1-P), and the reverse reaction, which produces dTTP from dTDP-glucose and diphosphate (PubMed:15598657). Can also catalyze the formation of UDP-glucose from UTP and glucose-1-phosphate (PubMed:27864169, PubMed:30291121).5 Publications

<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

Co2+1 Publication, Mn2+1 PublicationNote: Can also use Mg2+ and Zn2+, with lower efficiency. Important for nucleotidylyltransferase activity.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

GlcN-1-P acetyltransferase activity is inhibited by divalent cations. GalN-1-P acetyltransferase activity is enhanced by Co2+, Mg2+ and Ca2+, but inhibited by Zn2+ or Mn2+.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

kcat is 69.7 sec(-1) for GalN-1-P acetyltransferase activity. kcat is 123.2 sec(-1) for GlcN-1-P acetyltransferase activity.1 Publication
  1. KM=1.71 mM for GalN-1-P2 Publications
  2. KM=0.59 mM for GlcN-1-P2 Publications
  3. KM=0.63 mM for acetyl-CoA (in the presence of GalN-1-P or GlcN-1-P)2 Publications
  4. KM=0.068 mM for GlcNAc-1-P1 Publication
  5. KM=1.23 mM for Glc-1-P (in the presence of UTP)1 Publication
  6. KM=1.12 mM for Glc-1-P (in the presence of dTTP)1 Publication
  7. KM=0.02 mM for dTTP1 Publication
  8. KM=0.05 mM for dTDP-alpha-D-glucose for the reverse reaction of the glucose-1-phosphate thymidylyltransferase activity1 Publication
  9. KM=0.39 mM for diphosphate for the reverse reaction of the glucose-1-phosphate thymidylyltransferase activity1 Publication
  10. KM=0.056 mM for UDP-GalNAc for the reverse reaction of the GalNAc-1-P UTase activity1 Publication
  11. KM=0.016 mM for UDP-GlcNAc for the reverse reaction of the GlcNAc-1-P UTase activity1 Publication
  1. Vmax=1.46 µmol/min/mg enzyme for the forward reaction with alpha-D-glucose 1-phosphate as substrate1 Publication
  2. Vmax=13.65 µmol/min/mg enzyme for the reverse reaction with dTDP-alpha-D-glucose as substrate1 Publication

pH dependencei

Optimum pH is 8.5 for glucose-1-phosphate thymidylyltransferase activity.1 Publication

Temperature dependencei

Optimum temperature is 95 degrees Celsius for glucose-1-phosphate thymidylyltransferase activity.1 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: 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).1 Publication
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 sugar-1-phosphate nucleotidylyltransferase/acetyltransferase (STK_04520)
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.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional sugar-1-phosphate nucleotidylyltransferase/acetyltransferase (STK_04520)
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.

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 sitei73NTP2 Publications1
Binding sitei79NTP; via amide nitrogen2 Publications1
Binding sitei80GlcNAc1 Publication1
Binding sitei97GlcNAc1 Publication1
Binding sitei131GlcNAc; via amide nitrogen1 Publication1
Binding sitei146GlcNAc1 Publication1
Binding sitei157GlcNAc1 Publication1

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 bindingi8 – 13NTP2 Publications6

<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
LigandCobalt, Manganese, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:MONOMER-20592
STOK273063:G1G3D-538-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.1.157 6166
2.3.1.B28 6166
2.7.7.23 6166
2.7.7.24 6166
2.7.7.83 6166
2.7.7.9 6166
2.7.7.B18 6166
2.7.7.B19 6166
2.7.7.B20 6166
2.7.7.B21 6166

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

More...
UniPathwayi
UPA00113;UER00532
UPA00113;UER00533

<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 sugar-1-phosphate nucleotidylyltransferase/acetyltransferaseCurated
Including the following 2 domains:
Sugar-1-phosphate nucleotidylyltransferase1 Publication
Short name:
Sugar-1-P NTase1 Publication
Alternative name(s):
Glucose-1-phosphate thymidylyltransferase1 Publication (EC:2.7.7.241 Publication)
Glucose-1-phosphate uridylyltransferaseCurated (EC:2.7.7.92 Publications)
Short name:
Glc-1-P UTase1 Publication
N-acetylgalactosamine-1-phosphate uridyltransferase1 Publication (EC:2.7.7.831 Publication)
Short name:
GalNAc-1-P UTase1 Publication
N-acetylglucosamine-1-phosphate uridyltransferase1 Publication (EC:2.7.7.235 Publications)
Short name:
GlcNAc-1-P UTase1 Publication
Sugar-1-phosphate acetyltransferaseCurated
Alternative name(s):
Galactosamine-1-phosphate N-acetyltransferase1 Publication (EC:2.3.1.2762 Publications)
Short name:
GalN-1-P AcTase1 Publication
Short name:
GalN-1-P acetyltransferase1 Publication
Glucosamine-1-phosphate N-acetyltransferase1 Publication (EC:2.3.1.1572 Publications)
Short name:
GlcN-1-P AcTase1 Publication
Short name:
GlcN-1-P acetyltransferase1 Publication
<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
Ordered Locus Names:STK_04520Imported
ORF Names:ST04521 Publication
<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>OrganismiSulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
<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 identifieri273063 [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 lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfurisphaera
<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
  • UP000001015 <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 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>Mutagenesisi80T → A, G or Q: Increases both GlcNAc-1-P UTase and Glc-1-P UTase activities. 1 Publication1
Mutagenesisi80T → D or H: Decrease in GlcNAc-1-P UTase activity but increase in Glc-1-P UTase activity. 1 Publication1
Mutagenesisi80T → E, K, L, M, R, W or Y: Strong decrease in GlcNAc-1-P UTase activity and loss of Glc-1-P UTase activity. 1 Publication1
Mutagenesisi80T → F or I: Loss of both GlcNAc-1-P UTase and Glc-1-P UTase activities. 1 Publication1
Mutagenesisi80T → N or S: Strong increase in GlcNAc-1-P UTase activity and decrease in Glc-1-P UTase activity. 1 Publication1
Mutagenesisi80T → N: Loss of GlcNAc-1-P UTase activity; when associated with V-97. 1 Publication1
Mutagenesisi97Y → A, D, F, G, I, K, T or V: Increases GlcNAc-1-P UTase activity. Decreases Glc-1-P UTase activity. 1 Publication1
Mutagenesisi97Y → C, E, P, R or W: Decreases GlcNAc-1-P UTase and Glc-1-P UTase activities. 1 Publication1
Mutagenesisi97Y → H, L, M, N, Q or S: Increases GlcNAc-1-P UTase and Glc-1-P UTase activities. 1 Publication1
Mutagenesisi97Y → V: Loss of GlcNAc-1-P UTase activity; when associated with N-80. 1 Publication1
Mutagenesisi146E → A, C, F, G, I, K, L, M, P, Q, R, V, W or Y: Loss of both GlcNAc-1-P UTase and Glc-1-P UTase activities. 1 Publication1
Mutagenesisi146E → D or N: Decrease in GlcNAc-1-P UTase and Glc-1-P UTase activities. 1 Publication1
Mutagenesisi146E → H, S or T: Decrease in GlcNAc-1-P UTase activity and loss of Glc-1-P UTase activity. 1 Publication1
Mutagenesisi308H → A: Strong decrease in GalN-1-P AcTase activity and almost loss of GlcN-1-P AcTase activity. 1 Publication1
Mutagenesisi311Y → A: Strong decrease in GalN-1-P AcTase activity and increase in GlcN-1-P AcTase activity. 1 Publication1
Mutagenesisi331N → A: Strong decrease in GalN-1-P AcTase activity and decrease in GlcN-1-P AcTase activity. 1 Publication1
Mutagenesisi337K → A: Slight decrease in GalN-1-P AcTase activity and increase in GlcN-1-P AcTase activity. 1 Publication1
Mutagenesisi340K → A: Decrease in GalN-1-P AcTase activity and increase in GlcN-1-P AcTase activity. 1 Publication1
Mutagenesisi391 – 401Missing : No change in GlcNAc-1-P UTase activity. Shows 38% less GalN-1-P AcTase activity than the wild-type, but increases GlcN-1-P AcTase activity 16.8 times. Significantly affects the thermostability of the entire protein. 1 PublicationAdd BLAST11
Mutagenesisi397 – 401Missing : No change in GlcNAc-1-P UTase activity. Shows 20% less GalN-1-P AcTase activity than the wild-type, but increases GlcN-1-P AcTase activity 4.8 times. Does not affect thermostability. 1 Publication5

<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_00004480681 – 401Bifunctional sugar-1-phosphate nucleotidylyltransferase/acetyltransferaseAdd BLAST401

<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.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
273063.STK_04520

<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

1401
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

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SMRi
Q975F9

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q975F9

<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 – 220NucleotidylyltransferaseCuratedAdd BLAST220
Regioni236 – 401AcetyltransferaseCuratedAdd BLAST166

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal domain is essential for the formation of the trimer and the high thermostability of the entire protein. The C-terminal 11 residues are important for GalN-1-P AcTase activity, but they have an inhibitory effect on the GlcN-1-P AcTase activity.1 Publication

<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.Curated
In the C-terminal section; belongs to the transferase hexapeptide repeat family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
arCOG00666 Archaea
COG1208 LUCA

KEGG Orthology (KO)

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KOi
K23144

Identification of Orthologs from Complete Genome Data

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OMAi
QNAQKEY

Database of Orthologous Groups

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OrthoDBi
61185at2157

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.90.550.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR023915 Bifunctiontional_GlmU_arc-type
IPR001451 Hexapep
IPR005835 NTP_transferase_dom
IPR029044 Nucleotide-diphossugar_trans
IPR011004 Trimer_LpxA-like_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00132 Hexapep, 2 hits
PF00483 NTP_transferase, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51161 SSF51161, 1 hit
SSF53448 SSF53448, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR03992 Arch_glmU, 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.

Q975F9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKAFILAAGS GERLEPITHT RPKAFVPILS KPLIEYQIEY LRKCGIRDIT
60 70 80 90 100
VIVSSKNKEY FEKKLKEISI VTQKDDIKGT GAAILSAKFN DEALIIYGDL
110 120 130 140 150
FFSNEKEICN IITLKENAII GVKVSNPKDY GVLVLDNQNN LSKIIEKPEI
160 170 180 190 200
PPSNLINAGI YKLNSDIFTY LDKISISERG ELELTDAINL MAKDHRVKVI
210 220 230 240 250
EYEGYWMDIG KPWNIIDVNK WALDNLVFSQ NLGNVEDNVK IKGKVIIEED
260 270 280 290 300
AEIKSGTYIE GPVYIGKGSE IGPNSYLRPY TILVEKNKIG ASVEVKESVI
310 320 330 340 350
MEGSKIPHLS YVGDSVIAED VNFGAGTLIA NLRFDEKEVK VNVKGKRISS
360 370 380 390 400
GRRKLGAFIG GHVRTGINVT ILPGVKIGAY ARIYPGAVVN RDVGYGEFFK

V
Length:401
Mass (Da):44,516
Last modified:December 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:i5EF240CCDFFBF976
GO

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

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DDBJi
Links Updated
BA000023 Genomic DNA Translation: BAB65442.1

NCBI Reference Sequences

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RefSeqi
WP_010978425.1, NC_003106.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
BAB65442; BAB65442; STK_04520

Database of genes from NCBI RefSeq genomes

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GeneIDi
1458389

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sto:STK_04520

Pathosystems Resource Integration Center (PATRIC)

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PATRICi
fig|273063.9.peg.524

<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
BA000023 Genomic DNA Translation: BAB65442.1
RefSeqiWP_010978425.1, NC_003106.2

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
2GGOX-ray1.80A1-401[»]
2GGQX-ray2.00A1-401[»]
5Z09X-ray2.91A/B/C/D/E/F1-401[»]
5Z0AX-ray2.09A/B/C/D/E/F1-401[»]
SMRiQ975F9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi273063.STK_04520

Genome annotation databases

EnsemblBacteriaiBAB65442; BAB65442; STK_04520
GeneIDi1458389
KEGGisto:STK_04520
PATRICifig|273063.9.peg.524

Phylogenomic databases

eggNOGiarCOG00666 Archaea
COG1208 LUCA
KOiK23144
OMAiQNAQKEY
OrthoDBi61185at2157

Enzyme and pathway databases

UniPathwayiUPA00113;UER00532
UPA00113;UER00533
BioCyciMetaCyc:MONOMER-20592
STOK273063:G1G3D-538-MONOMER
BRENDAi2.3.1.157 6166
2.3.1.B28 6166
2.7.7.23 6166
2.7.7.24 6166
2.7.7.83 6166
2.7.7.9 6166
2.7.7.B18 6166
2.7.7.B19 6166
2.7.7.B20 6166
2.7.7.B21 6166

Miscellaneous databases

EvolutionaryTraceiQ975F9

Family and domain databases

Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR023915 Bifunctiontional_GlmU_arc-type
IPR001451 Hexapep
IPR005835 NTP_transferase_dom
IPR029044 Nucleotide-diphossugar_trans
IPR011004 Trimer_LpxA-like_sf
PfamiView protein in Pfam
PF00132 Hexapep, 2 hits
PF00483 NTP_transferase, 1 hit
SUPFAMiSSF51161 SSF51161, 1 hit
SSF53448 SSF53448, 1 hit
TIGRFAMsiTIGR03992 Arch_glmU, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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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 nameiS1PNA_SULTO
<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: Q975F9
<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: October 16, 2019
Last sequence update: December 1, 2001
Last modified: February 26, 2020
This is version 115 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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