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Entry version 83 (11 Dec 2019)
Sequence version 1 (01 Feb 2005)
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Protein

Fused isobutyryl-CoA mutase

Gene

icmF

Organism
Geobacillus kaustophilus (strain HTA426)
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 reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, and to a lesser extent, of pivalyl-CoA and isovaleryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly. Also displays ATPase activity. Is not able to convert 3-hydroxybutyryl-CoA to 2-hydroxyisobutyryl-CoA. Does not exhibit methylmalonyl-CoA mutase (MCM) activity.2 Publications

<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

<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

Protein has several cofactor binding sites:

<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 3.1 sec(-1) for ICM activity in the absence of nucleotides, at pH 7.5 and 37 degrees Celsius. Activity might be 4-fold higher at 60 degrees Celsius, the optimal growth temperature for this organism. kcat is 1.96 sec(-1) for ICM activity in the presence of GDP, at pH 7.5 and 37 degrees Celsius. kcat is 1.88 sec(-1) for ICM activity in the presence of GTP, at pH 7.5 and 37 degrees Celsius (PubMed:19864421). kcat is 10 min(-1) for GTPase activity and 19 min(-1) for ATPase activity (at 37 degrees Celsius) (PubMed:22167181).2 Publications
  1. KM=20.1 µM for isobutyryl-CoA (in the absence of nucleotides, at pH 7.5 and 37 degrees Celsius)1 Publication
  2. KM=45.3 µM for isobutyryl-CoA (in the presence of GDP, at pH 7.5 and 37 degrees Celsius)1 Publication
  3. KM=50.8 µM for isobutyryl-CoA (in the presence of GTP, at pH 7.5 and 37 degrees Celsius)1 Publication
  4. KM=51 µM for GTP (at 37 degrees Celsius)2 Publications
  5. KM=62 µM for isovaleryl-CoA (at 37 degrees Celsius)1 Publication
  6. KM=1290 µM for ATP (at 37 degrees Celsius)1 Publication
  1. Vmax=0.021 µmol/min/mg enzyme for isovaleryl-CoA isomerization (at 37 degrees Celsius)1 Publication
  2. Vmax=1.2 µmol/min/mg enzyme for isobutyryl-CoA isomerization (at 37 degrees Celsius)1 Publication
  3. Vmax=3.3 µmol/min/mg enzyme for n-butyryl-CoA isomerization (at 37 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi23Cobalt (adenosylcobalamin axial ligand)UniRule annotation1
Metal bindingi214Magnesium 1; catalyticUniRule annotation1
Metal bindingi238Magnesium 2; via carbonyl oxygenUniRule annotation1
Metal bindingi239Magnesium 2UniRule annotation1
Metal bindingi252Magnesium 1; catalyticUniRule annotation1
Metal bindingi252Magnesium 2UniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei255GTPUniRule annotation1
Metal bindingi300Magnesium 1; catalyticUniRule annotation1
Metal bindingi300Magnesium 2UniRule annotation1
Metal bindingi301Magnesium 2; via carbonyl oxygenUniRule annotation1
Binding sitei578Substrate; via carbonyl oxygenUniRule annotation1
Binding sitei613SubstrateUniRule annotation1
Binding sitei719SubstrateUniRule annotation1
Binding sitei763SubstrateUniRule annotation1
Binding sitei812SubstrateUniRule annotation1
Binding sitei847SubstrateUniRule annotation1
Binding sitei852SubstrateUniRule annotation1
Binding sitei964GTPUniRule annotation1
Binding sitei1085GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi210 – 215GTPUniRule annotation6
Nucleotide bindingi347 – 350GTPUniRule annotation4

<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 functionChaperone, Hydrolase, Isomerase, Multifunctional enzyme
LigandCobalamin, Cobalt, GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

<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:
Fused isobutyryl-CoA mutase1 PublicationUniRule annotation
Including the following 2 domains:
Isobutyryl-CoA mutase1 PublicationUniRule annotation (EC:5.4.99.13UniRule annotation2 Publications)
Short name:
ICM1 PublicationUniRule annotation
P-loop GTPase1 PublicationUniRule annotation (EC:3.6.5.-UniRule annotation2 Publications)
Alternative name(s):
G-protein chaperone1 PublicationUniRule 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:icmF1 PublicationUniRule annotation
Ordered Locus Names:GK3391Imported
<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>OrganismiGeobacillus kaustophilus (strain HTA426)
<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 identifieri235909 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillusGeobacillus thermoleovorans group
<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
  • UP000001172 <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

<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_and_biotech_section">'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>Mutagenesisi213K → A: Loss of GTPase and ATPase activities. No effect on the mutase activity. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004341271 – 1086Fused isobutyryl-CoA mutaseAdd BLAST1086

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

Homodimer.

UniRule annotation1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
235909.GK3391

<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

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

More...
SMRi
Q5KUG0

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Domaini10 – 140B12-bindingUniRule annotationAdd BLAST131

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>Regioni153 – 407GTPase chaperone MeaIUniRule annotationAdd BLAST255
Regioni408 – 570LinkerUniRule annotationAdd BLAST163

<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

Is composed of four functional domains: the N-terminal 5'-deoxyadenosylcobalamin binding region that is homologous to the small subunit of ICM (IcmB), a middle P-loop GTPase domain (MeaI) that likely acts as a chaperone for ICM, a structured linker region involved in dimer formation, and a C-terminal part that is homologous to the large substrate-binding subunit of ICM (IcmA).UniRule annotation1 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

Belongs to the IcmF family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105D5P Bacteria
COG1703 LUCA
COG1884 LUCA
COG2185 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000024525

KEGG Orthology (KO)

More...
KOi
K11942

Identification of Orthologs from Complete Genome Data

More...
OMAi
YYLSRGM

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_02050 IcmF, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006159 Acid_CoA_mut_C
IPR016176 Cbl-dep_enz_cat
IPR006158 Cobalamin-bd
IPR036724 Cobalamin-bd_sf
IPR033669 IcmF
IPR006099 MeMalonylCoA_mutase_a/b_cat
IPR027417 P-loop_NTPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02310 B12-binding, 1 hit
PF01642 MM_CoA_mutase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51703 SSF51703, 1 hit
SSF52242 SSF52242, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00640 acid_CoA_mut_C, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51332 B12_BINDING, 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>. 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_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.

Q5KUG0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAHIYRPKHH VRFVTASSLF DGHDASINIM RRILQASGAE VIHLGHNRSV
60 70 80 90 100
EEIVNAAIQE DVQGIAVSSY QGGHMEFFKY MYDLLQERGA SHIRIYGGGG
110 120 130 140 150
GVIIPREIKE LHEYGIARIF SPEDGRRLGL QGMINVMLEE CDFPTVTVVT
160 170 180 190 200
DELERLPSGD VQAIARLITL CEYRAEGENK EAAAAAEAAI EQVKALEKRV
210 220 230 240 250
PVLGITGTGG AGKSSLTDEL VRRFLNEIPD IKIAILSVDP TKQKTGGALL
260 270 280 290 300
GDRIRMNSIN SPRVYMRSLA TRHSRTELSP AIRDAISVVK AAGFDLVIIE
310 320 330 340 350
TSGIGQGDAA ITEVCDVSMY VMTSEFGAPT QLEKIDMIDY ADLIVINKFE
360 370 380 390 400
RKGSEDAKRQ VQKQYQRSHQ LFDRDVSEMP VYGTIASQFN DPGTNTLFVA
410 420 430 440 450
LVDTINKKAG TNWKTSLKTV ANVEKHNVII PNERRYYLRE IAETVRSYHR
460 470 480 490 500
RAEQQVEVAR RLFQIEGAIE AAKERGEAED VIRALETLKA DYEAKLTPES
510 520 530 540 550
KRILATWEET KAKYAAKQFV TKVRDKEIVT ELTTKTLSGL DIPKVVLPKF
560 570 580 590 600
KDYGEILRWV YKENVPGSFP YTAGVFPFKR QGEDPKRQFA GEGTPERTNR
610 620 630 640 650
RFHYLCKEDK AKRLSTAFDS VTLYGEDPDY RPDIFGKVGE SGVSVCTLDD
660 670 680 690 700
MKKLYKGFDL CDPLTSVSMT INGPAPILLA MFMNTAIDQQ VEKKEAELGR
710 720 730 740 750
PLTPEEYEQV KEWTLQTVRG TVQADILKED QGQNTCIFST DFALKMMGDI
760 770 780 790 800
QEYFIKHRVR NYYSVSISGY HIAEAGANPI TQLAFTLANG FTYVEYYLSR
810 820 830 840 850
GMHIDDFAPN LSFFFSNGLD PEYSVIGRVA RRIWAIVMRE KYGANERSQK
860 870 880 890 900
LKYHIQTSGR SLHAQEIDFN DIRTTLQALL AIYDNCNSLH TNAYDEAITT
910 920 930 940 950
PTEESVRRAM AIQLIITKEF GLTKNENPLQ GSFIIEELTD LVEEAVLQEF
960 970 980 990 1000
ERLNDRGGVL GAMEMQYQRG KIQDESLYYE TKKHTGELPI IGVNTFLNPN
1010 1020 1030 1040 1050
PPSEDELNNI QLARATYEEK ETQIRNLREF QERNKDKAGP ALERLKQVAT
1060 1070 1080
SGGNIFEELM ETVKVASLGQ ITRALYEVGG QYRRNM
Length:1,086
Mass (Da):122,429
Last modified:February 1, 2005 - 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:i073D27235443416F
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
BA000043 Genomic DNA Translation: BAD77676.1

NCBI Reference Sequences

More...
RefSeqi
WP_011232858.1, NC_006510.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAD77676; BAD77676; GK3391

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gka:GK3391

<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
BA000043 Genomic DNA Translation: BAD77676.1
RefSeqiWP_011232858.1, NC_006510.1

3D structure databases

SMRiQ5KUG0
ModBaseiSearch...

Protein-protein interaction databases

STRINGi235909.GK3391

Genome annotation databases

EnsemblBacteriaiBAD77676; BAD77676; GK3391
KEGGigka:GK3391

Phylogenomic databases

eggNOGiENOG4105D5P Bacteria
COG1703 LUCA
COG1884 LUCA
COG2185 LUCA
HOGENOMiHOG000024525
KOiK11942
OMAiYYLSRGM

Family and domain databases

HAMAPiMF_02050 IcmF, 1 hit
InterProiView protein in InterPro
IPR006159 Acid_CoA_mut_C
IPR016176 Cbl-dep_enz_cat
IPR006158 Cobalamin-bd
IPR036724 Cobalamin-bd_sf
IPR033669 IcmF
IPR006099 MeMalonylCoA_mutase_a/b_cat
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF02310 B12-binding, 1 hit
PF01642 MM_CoA_mutase, 1 hit
SUPFAMiSSF51703 SSF51703, 1 hit
SSF52242 SSF52242, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00640 acid_CoA_mut_C, 1 hit
PROSITEiView protein in PROSITE
PS51332 B12_BINDING, 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 nameiICMF_GEOKA
<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: Q5KUG0
<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/Swiss-Prot: October 14, 2015
Last sequence update: February 1, 2005
Last modified: December 11, 2019
This is version 83 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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