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Entry version 81 (17 Jun 2020)
Sequence version 1 (01 Nov 1999)
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Protein

L-lysine 2,3-aminomutase

Gene

kamA

Organism
Clostridium subterminale
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 interconversion of L-alpha-lysine and L-beta-lysine.3 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

Protein has several cofactor binding sites:

<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

The enzyme is activated by S-adenosyl-methionine. Activity is dependent on the levels of Fe2+, S2- and Co2+. Activity is stimulated by addition of EDTA. S-adenosylhomocysteine competitively inhibits the activity whereas 5'-methylthioadenosine is not inhibitory in the presence of S-adenosylmethionine. Competitively inhibited by 4-thialysine. Inhibited by sodium borohydride (1 mM) when added with 2 mM dithionate. Moderately inhibited by beta-mercaptoethanol (30 mM) along with dithionate. Higher concentrations of Fe2+ partially inhibit the activity and Co2+ at 1 mM is a strong inhibitor. Hydroxylamine, isonicotinic acid hydrazide inhibit effectively, in addition, hydrazine, D-penicillamine and D-cycloserine are also inhibitory at high concentrations.3 Publications

Redox potential

E0 is between -336 and -370 mV for 4Fe-4S cluster.3 Publications

<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

  1. KM=6.6 µM for L-lysine3 Publications
  2. KM=28 nM for adenosylmethionine3 Publications
  3. KM=1.4 mM for 4-thialysine3 Publications
  1. Vmax=0.19 µmol/min/mg enzyme with 4-thialysine as substrate (at 37 degrees Celsius and pH 8)3 Publications

pH dependencei

Optimum pH is 8.0. Displays half maximal activity between pH 6.0 and 9.8.3 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius. It has strong activity at 37 degrees Celsius but is reversibly inactivated in temperatures between 37 and 65 degrees Celsius. Minimal loss of activity is observed in enzyme stored at -10 degrees Celsius in the presence of 15% glycerol.3 Publications

<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: L-lysine degradation via acetate pathway

This protein is involved in the pathway L-lysine degradation via acetate pathway, which is part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the pathway L-lysine degradation via acetate pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi125Iron-sulfur (4Fe-4S-S-AdoMet)1
Metal bindingi129Iron-sulfur (4Fe-4S-S-AdoMet)1
Metal bindingi132Iron-sulfur (4Fe-4S-S-AdoMet)1
Metal bindingi268Zinc1
Metal bindingi375Zinc1
Metal bindingi377Zinc1
Metal bindingi380Zinc1

<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 functionIsomerase
Ligand4Fe-4S, Cobalt, Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-12270

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.4.3.2, 1523

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

More...
UniPathwayi
UPA00870

<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:
L-lysine 2,3-aminomutase (EC:5.4.3.2)
Short name:
LAM
Alternative name(s):
KAM
<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:kamA
<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>OrganismiClostridium subterminale
<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 identifieri1550 [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 lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

<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>Mutagenesisi86E → Q: Reduction in activity. Decrease in iron and sulfide and PLP content. 1 Publication1
Mutagenesisi96D → N: Reduction in activity. Decrease in iron and sulfide and PLP content. 1 Publication1
Mutagenesisi130R → Q or K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers. 1 Publication1
Mutagenesisi134R → K: Complete loss of activity. Significant decrease in iron and sulfide and PLP content. 1 Publication1
Mutagenesisi134R → Q: Complete loss of activity. Slight decrease in iron and sulfide and PLP content. 1 Publication1
Mutagenesisi135R → K: Reduction in activity. Decrease in iron and sulfide and PLP content. 1 Publication1
Mutagenesisi135R → Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content. 1 Publication1
Mutagenesisi136R → Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content. 1 Publication1
Mutagenesisi165D → N: Significant reduction in activity. Decrease in iron and sulfide and PLP content. 1 Publication1
Mutagenesisi172D → N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers. 1 Publication1
Mutagenesisi236E → Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content. 1 Publication1
Mutagenesisi293D → N: Complete loss of activity. Decrease in iron and sulfide and PLP content. 1 Publication1
Mutagenesisi330D → A or N: Complete loss of activity. Decrease in iron and sulfide and PLP content. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001722871 – 416L-lysine 2,3-aminomutaseAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei337N6-(pyridoxal phosphate)lysine1

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9XBQ8

<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

Homohexamer; trimer of dimers.

Forms a homotetramer in crystal.

2 Publications

<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

1416
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
Q9XBQ8

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
Q9XBQ8

<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%5Fand%5Fdomains%5Fsection">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>Domaini111 – 322Radical SAM corePROSITE-ProRule annotationAdd BLAST212

<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 radical SAM superfamily. KamA family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785, Aldolase_TIM
IPR025895, LAM_C_dom
IPR003739, Lys_aminomutase/Glu_NH3_mut
IPR022459, Lysine_aminomutase
IPR007197, rSAM

The PANTHER Classification System

More...
PANTHERi
PTHR30538, PTHR30538, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12544, LAM_C, 1 hit
PF04055, Radical_SAM, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF004911, DUF160, 1 hit

Structure-Function Linkage Database

More...
SFLDi
SFLDF00283, L-lysine_2_3-aminomutase_(LAM, 1 hit
SFLDG01070, PLP-dependent, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03820, lys_2_3_AblA, 1 hit
TIGR00238, TIGR00238, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51918, RADICAL_SAM, 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.

Q9XBQ8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MINRRYELFK DVSDADWNDW RWQVRNRIET VEELKKYIPL TKEEEEGVAQ
60 70 80 90 100
CVKSLRMAIT PYYLSLIDPN DPNDPVRKQA IPTALELNKA AADLEDPLHE
110 120 130 140 150
DTDSPVPGLT HRYPDRVLLL ITDMCSMYCR HCTRRRFAGQ SDDSMPMERI
160 170 180 190 200
DKAIDYIRNT PQVRDVLLSG GDALLVSDET LEYIIAKLRE IPHVEIVRIG
210 220 230 240 250
SRTPVVLPQR ITPELVNMLK KYHPVWLNTH FNHPNEITEE STRACQLLAD
260 270 280 290 300
AGVPLGNQSV LLRGVNDCVH VMKELVNKLV KIRVRPYYIY QCDLSLGLEH
310 320 330 340 350
FRTPVSKGIE IIEGLRGHTS GYCVPTFVVD APGGGGKTPV MPNYVISQSH
360 370 380 390 400
DKVILRNFEG VITTYSEPIN YTPGCNCDVC TGKKKVHKVG VAGLLNGEGM
410
ALEPVGLERN KRHVQE
Length:416
Mass (Da):47,102
Last modified:November 1, 1999 - 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:i6C3602E5B87E25A1
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
AF159146 Genomic DNA Translation: AAD43134.1

<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
AF159146 Genomic DNA Translation: AAD43134.1

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
2A5HX-ray2.10A/B/C/D1-416[»]
SMRiQ9XBQ8
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PRIDEiQ9XBQ8

Enzyme and pathway databases

UniPathwayiUPA00870
BioCyciMetaCyc:MONOMER-12270
BRENDAi5.4.3.2, 1523

Miscellaneous databases

EvolutionaryTraceiQ9XBQ8

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785, Aldolase_TIM
IPR025895, LAM_C_dom
IPR003739, Lys_aminomutase/Glu_NH3_mut
IPR022459, Lysine_aminomutase
IPR007197, rSAM
PANTHERiPTHR30538, PTHR30538, 1 hit
PfamiView protein in Pfam
PF12544, LAM_C, 1 hit
PF04055, Radical_SAM, 1 hit
PIRSFiPIRSF004911, DUF160, 1 hit
SFLDiSFLDF00283, L-lysine_2_3-aminomutase_(LAM, 1 hit
SFLDG01070, PLP-dependent, 1 hit
TIGRFAMsiTIGR03820, lys_2_3_AblA, 1 hit
TIGR00238, TIGR00238, 1 hit
PROSITEiView protein in PROSITE
PS51918, RADICAL_SAM, 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 nameiKAMA_CLOSU
<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: Q9XBQ8
<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: January 24, 2006
Last sequence update: November 1, 1999
Last modified: June 17, 2020
This is version 81 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, Direct protein sequencing

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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