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Entry version 89 (11 Dec 2019)
Sequence version 1 (30 May 2006)
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Protein

Fused isobutyryl-CoA mutase

Gene

icmF

Organism
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
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 much lesser extent, of pivalyl-CoA and isovaleryl-CoA, using radical chemistry (PubMed:22167181). 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 (PubMed:22167181, PubMed:25675500). The G-domain of IcmF has also a role in its cofactor repair (PubMed:28130442). Does not display ATPase activity.3 Publications

Miscellaneous

In many AdoCbl-dependent isomerases, e.g. methylmalonyl-CoA mutase (MCM), its G-protein chaperone is a separate protein.Curated

<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 <a href="http://www.uniprot.org/help/function_section">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

Is prone to inactivation during catalytic turnover due to the occasional loss of the 5'-deoxyadenosine moiety and formation of the inactive cob(II)alamin cofactor in its active site. The GTPase activity of IcmF powers the ejection of the inactive cofactor and requires the presence of an acceptor protein, adenosyltransferase (ATR), for receiving it. ATR, in turn, catalyzes an adenosylation reaction converting cob(II)alamin in the presence of ATP and a reductant to the active AdoCbl cofactor. The repaired cofactor is then reloaded onto IcmF in a GTPase-gated step, regenerating active enzyme. The GTPase activity of IcmF is significantly decreased in the presence of excess of AdoCbl or cob(II)alamin and is higher in the apoenzyme state, indicating that the G-domain senses the presence and identity of the cofactor in the mutase active site.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 18 min(-1) for GTPase activity (at 37 degrees Celsius).1 Publication
  1. KM=40 µM for GTP (at 37 degrees Celsius)1 Publication
  1. Vmax=0.015 µmol/min/mg enzyme for isovaleryl-CoA isomerization (at 37 degrees Celsius)1 Publication
  2. Vmax=13.8 µmol/min/mg enzyme for isobutyryl-CoA isomerization (at 37 degrees Celsius)1 Publication
  3. Vmax=33.0 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 bindingi39Cobalt (adenosylcobalamin axial ligand)UniRule annotationCombined sources1 Publication1
Metal bindingi223Magnesium 1; catalyticUniRule annotationCombined sources1 Publication1
Metal bindingi248Magnesium 2; via carbonyl oxygenUniRule annotationCombined sources1 Publication1
Metal bindingi249Magnesium 2UniRule annotationCombined sources1 Publication1
Metal bindingi262Magnesium 1; catalyticUniRule annotationCombined sources1 Publication1
Metal bindingi262Magnesium 2UniRule annotationCombined sources1 Publication1
<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 sitei265GTPUniRule annotationCombined sources1 Publication1
Metal bindingi310Magnesium 1; catalyticUniRule annotationCombined sources1 Publication1
Metal bindingi310Magnesium 2UniRule annotationCombined sources1 Publication1
Metal bindingi311Magnesium 2; via carbonyl oxygenUniRule annotationCombined sources1 Publication1
Binding sitei587Substrate; via carbonyl oxygenUniRule annotation1 Publication1
Binding sitei622SubstrateUniRule annotation1 Publication1
Binding sitei728SubstrateUniRule annotation1 Publication1
Binding sitei772SubstrateUniRule annotation1 Publication1
Binding sitei821SubstrateUniRule annotation1 Publication1
Binding sitei856SubstrateUniRule annotation1 Publication1
Binding sitei861SubstrateUniRule annotation1 Publication1
Binding sitei973GTPUniRule annotationCombined sources1 Publication1
Binding sitei1092GTPUniRule annotationCombined sources1 Publication1

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 bindingi219 – 224GTPUniRule annotationCombined sources1 Publication6
Nucleotide bindingi357 – 360GTPUniRule annotationCombined sources1 Publication4

<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

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q1LRY0

<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 annotation1 Publication)
Short name:
ICM1 PublicationUniRule annotation
P-loop GTPase1 PublicationUniRule annotation (EC:3.6.5.-UniRule annotation1 Publication)
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
Synonyms:sbmImported
Ordered Locus Names:Rmet_0210Imported
<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>OrganismiCupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
<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 identifieri266264 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
<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
  • UP000002429 <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>Mutagenesisi598F → A: Switches the substrate specificity and enhances the catalytic efficiency of the isovaleryl-CoA mutase over the native isobutyryl-CoA mutase activity about 4000-fold. Is even more susceptible to inactivation than wild-type during turnover. 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_00004341251 – 1093Fused isobutyryl-CoA mutaseAdd BLAST1093

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
266264.Rmet_0210

<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

11093
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
Q1LRY0

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Domaini26 – 156B12-bindingUniRule annotation1 PublicationAdd 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>Regioni169 – 417GTPase chaperone MeaIUniRule annotation1 PublicationAdd BLAST249
Regioni418 – 579LinkerUniRule annotation1 PublicationAdd BLAST162

<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 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).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

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

Database of Orthologous Groups

More...
OrthoDBi
154460at2

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
IPR006098 MMCoA_mutase_a_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
TIGR00641 acid_CoA_mut_N, 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.

Q1LRY0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTDLSDVSRT AAAKPPAVPG RGPANKVRFV TAASLFDGHD ASINIMRRIL
60 70 80 90 100
QSQGCEVIHL GHNRSVQEVV TAALQEDVQG IAISSYQGGH VEYFKYMIDL
110 120 130 140 150
LREHGGEHIQ VFGGGGGVIV PDEIRELQAY GVARIYSPED GQRMGLAGMI
160 170 180 190 200
TDMAQRCDID LTRYAPTTLD TVVAGDRRAL AQLITALENG KADPELVSAL
210 220 230 240 250
HAQAKAAAVP VLGITGTGGA GKSSLTDELI RRFRLDQDDA LSIAVISIDP
260 270 280 290 300
SRRKSGGALL GDRIRMNAIN HPNIFMRSLA TREAGSEISQ ALPDVIAACK
310 320 330 340 350
AARFDLVIVE TSGIGQGDAA IVPHVDLSLY VMTPEFGAAS QLEKIDMLDF
360 370 380 390 400
ADFVAINKFD RKGAQDAWRD VAKQVQRNRE QWHSRAEDMP VYGTQASRFN
410 420 430 440 450
DDGVTMLYQG LVGALGARGM SLKPGTLPNL EGRISTGQNV IVPPARSRYL
460 470 480 490 500
AELADTVRAY HRRVVAQSKL ARERQQLRAA HDMLQGAGHE SAALETLASE
510 520 530 540 550
RDVSLGAVER KLLAMWPQMQ QAYSGDEYVV KIRDKEIRTG LISTTLSGTK
560 570 580 590 600
IRKVVLPRFE DEGEILKWLM RENVPGSFPY TAGVFAFKRE GEDPTRMFAG
610 620 630 640 650
EGDAFRTNRR FKLVSEGMEA KRLSTAFDSV TLYGEDPHER PDIYGKVGNS
660 670 680 690 700
GVSIATLEDM KVLYDGFDLT NPSTSVSMTI NGPAPTILAM FMNTAIDQQI
710 720 730 740 750
DRFRADNGRD PTADEEAKIR AWVLQNVRGT VQADILKEDQ GQNTCIFSTE
760 770 780 790 800
FSLKVMGDIQ EYFVHHQVRN FYSVSISGYH IAEAGANPIS QLAFTLANGF
810 820 830 840 850
TYVEAYLARG MHIDDFAPNL SFFFSNGMDP EYSVLGRVAR RIWAVTMRDK
860 870 880 890 900
YGANDRSQKL KYHIQTSGRS LHAQEIDFND IRTTLQALIA IYDNCNSLHT
910 920 930 940 950
NAYDEAITTP TAESVRRALA IQLIINREWG VAKCENPNQG SFLIEELTDL
960 970 980 990 1000
VEEAVLQEFE RIAERGGVLG AMETGYQRGK IQEESLYYEQ LKHDGTLPII
1010 1020 1030 1040 1050
GVNTFRNPNG DPTPQTLELA RSSEDEKQSQ LHRLTEFHGA HQADAEAMLA
1060 1070 1080 1090
RLRQAVIDNR NVFAVLMDAV RVCSLGQITH ALFEVGGQYR RNM
Length:1,093
Mass (Da):120,612
Last modified:May 30, 2006 - 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:i42ABCE6FD4B22E82
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
CP000352 Genomic DNA Translation: ABF07096.1

NCBI Reference Sequences

More...
RefSeqi
WP_011515115.1, NC_007973.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABF07096; ABF07096; Rmet_0210

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24150756

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rme:Rmet_0210

<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
CP000352 Genomic DNA Translation: ABF07096.1
RefSeqiWP_011515115.1, NC_007973.1

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
4XC6X-ray3.35A/B1-1093[»]
4XC7X-ray3.45A/B1-1093[»]
4XC8X-ray3.25A/B1-1093[»]
5CJTX-ray3.40A/B1-1093[»]
5CJUX-ray3.50A/B1-1093[»]
5CJVX-ray3.45A/B1-1093[»]
5CJWX-ray3.40A/B1-1093[»]
SMRiQ1LRY0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi266264.Rmet_0210

Genome annotation databases

EnsemblBacteriaiABF07096; ABF07096; Rmet_0210
GeneIDi24150756
KEGGirme:Rmet_0210

Phylogenomic databases

eggNOGiENOG4105D5P Bacteria
COG1703 LUCA
COG1884 LUCA
COG2185 LUCA
HOGENOMiHOG000024525
KOiK11942
OMAiYYLSRGM
OrthoDBi154460at2

Enzyme and pathway databases

SABIO-RKiQ1LRY0

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
IPR006098 MMCoA_mutase_a_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
TIGR00641 acid_CoA_mut_N, 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_CUPMC
<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: Q1LRY0
<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: May 30, 2006
Last modified: December 11, 2019
This is version 89 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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