Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alanine racemase

Gene

alr

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
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-alanine and D-alanine. Also weakly active on serine.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

pyridoxal 5'-phosphateUniRule annotation6 Publications

<p>This subsection of the ‘Function’ 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

Inhibited by acetate and propionate. Irreversibly inhibited by cycloserine.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: D-alanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes D-alanine from L-alanine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Alanine racemase (GS458_0195), Alanine racemase (alr), Alanine racemase (GT94_03080), Alanine racemase (alr), Alanine racemase (AA904_04350)
This subpathway is part of the pathway D-alanine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-alanine from L-alanine, the pathway D-alanine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei39Proton acceptor; specific for D-alanine2 Publications1
<p>This subsection of the ‘Function’ 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 sitei136Substrate1 Publication1
Active sitei265Proton acceptor; specific for L-alanine2 Publications1
Binding sitei312Substrate; via amide nitrogen1 Publication1

<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
LigandPyridoxal phosphate

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.1.1.1 623

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P10724

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

More...
UniPathwayi
UPA00042;UER00497

<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:
Alanine racemaseUniRule annotation (EC:5.1.1.1UniRule annotation3 Publications)
<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:alr
Synonyms:dal
<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 stearothermophilus (Bacillus stearothermophilus)
<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 identifieri1422 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

<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>Mutagenesisi39K → A: Loss of activity. 1 Publication1
Mutagenesisi166H → A: 6.5-fold decrease in activity. 1 Publication1
Mutagenesisi219R → A: 100-fold decrease in activity. 1 Publication1
Mutagenesisi219R → E: 1000-fold decrease in activity. 1 Publication1
Mutagenesisi219R → K: 4-fold decrease in activity. 1 Publication1
Mutagenesisi265Y → A: 5000-fold decrease in activity. 1 Publication1
Mutagenesisi265Y → F: Loss of activity. 1 Publication1
Mutagenesisi265Y → S: 2000-fold decrease in activity. 1 Publication1
Mutagenesisi354Y → A: 54-fold increase in serine racemase activity. 1 Publication1
Mutagenesisi354Y → N: 81-fold increase in serine racemase activity. 1 Publication1
Mutagenesisi354Y → Q: 51-fold increase in serine racemase activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075086

Drug and drug target database

More...
DrugBanki
DB03801 Lysine Nz-Carboxylic Acid
DB01993 N-(5'-Phosphopyridoxyl)-D-Alanine
DB03766 Propanoic Acid
DB02142 Pyridoxamine-5'-Phosphate
DB04467 Pyridoxyl-Alanine-5-Phosphate
DB03327 {1-[(3-Hydroxy-Methyl-5-Phosphonooxy-Methyl-Pyridin-4-Ylmethyl)-Amino]-Ethyl}-Phosphonic Acid

<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_00001144991 – 388Alanine racemaseAdd BLAST388

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 residuei39N6-(pyridoxal phosphate)lysine3 Publications1
Modified residuei129N6-carboxylysine5 Publications1

<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.5 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

1388
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P10724

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

More...
SMRi
P10724

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P10724

<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

<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 alanine racemase family.UniRule annotation

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.37.10, 1 hit
3.20.20.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01201 Ala_racemase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000821 Ala_racemase
IPR009006 Ala_racemase/Decarboxylase_C
IPR011079 Ala_racemase_C
IPR001608 Ala_racemase_N
IPR020622 Ala_racemase_pyridoxalP-BS
IPR029066 PLP-binding_barrel

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00842 Ala_racemase_C, 1 hit
PF01168 Ala_racemase_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00992 ALARACEMASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01005 Ala_racemase_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50621 SSF50621, 1 hit
SSF51419 SSF51419, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00492 alr, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00395 ALANINE_RACEMASE, 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>.<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.

P10724-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNDFHRDTWA EVDLDAIYDN VENLRRLLPD DTHIMAVVKA NAYGHGDVQV
60 70 80 90 100
ARTALEAGAS RLAVAFLDEA LALREKGIEA PILVLGASRP ADAALAAQQR
110 120 130 140 150
IALTVFRSDW LEEASALYSG PFPIHFHLKM DTGMGRLGVK DEEETKRIVA
160 170 180 190 200
LIERHPHFVL EGLYTHFATA DEVNTDYFSY QYTRFLHMLE WLPSRPPLVH
210 220 230 240 250
CANSAASLRF PDRTFNMVRF GIAMYGLAPS PGIKPLLPYP LKEAFSLHSR
260 270 280 290 300
LVHVKKLQPG EKVSYGATYT AQTEEWIGTI PIGYADGWLR RLQHFHVLVD
310 320 330 340 350
GQKAPIVGRI CMDQCMIRLP GPLPVGTKVT LIGRQGDEVI SIDDVARHLE
360 370 380
TINYEVPCTI SYRVPRIFFR HKRIMEVRNA IGRGESSA
Length:388
Mass (Da):43,593
Last modified:November 1, 1997 - v2
<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:iF54AA581F135EA7A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti37 – 38VV → PP AA sequence (PubMed:3730360).Curated2
Sequence conflicti57 – 62AGASRL → RGPPP in AAA22220 (PubMed:2835089).Curated6
Sequence conflicti288 – 289WL → V in AAA22220 (PubMed:2835089).Curated2

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
M19142 Genomic DNA Translation: AAA22220.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A29984

<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
M19142 Genomic DNA Translation: AAA22220.1
PIRiA29984

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
1BD0X-ray1.60A/B1-388[»]
1EPVX-ray2.20A/B2-388[»]
1FTXX-ray2.20A/B2-388[»]
1L6FX-ray2.00A/B1-388[»]
1L6GX-ray2.00A/B1-388[»]
1NIUX-ray2.20A/B1-388[»]
1SFTX-ray1.90A/B1-388[»]
1XQKX-ray1.95A/B1-388[»]
1XQLX-ray1.80A/B1-388[»]
2SFPX-ray1.90A/B1-388[»]
3UW6X-ray2.30A/B/C1-388[»]
4ILSX-ray2.50A/B/C1-388[»]
ProteinModelPortaliP10724
SMRiP10724
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL1075086
DrugBankiDB03801 Lysine Nz-Carboxylic Acid
DB01993 N-(5'-Phosphopyridoxyl)-D-Alanine
DB03766 Propanoic Acid
DB02142 Pyridoxamine-5'-Phosphate
DB04467 Pyridoxyl-Alanine-5-Phosphate
DB03327 {1-[(3-Hydroxy-Methyl-5-Phosphonooxy-Methyl-Pyridin-4-Ylmethyl)-Amino]-Ethyl}-Phosphonic Acid

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00042;UER00497

BRENDAi5.1.1.1 623
SABIO-RKiP10724

Miscellaneous databases

EvolutionaryTraceiP10724

Family and domain databases

Gene3Di2.40.37.10, 1 hit
3.20.20.10, 1 hit
HAMAPiMF_01201 Ala_racemase, 1 hit
InterProiView protein in InterPro
IPR000821 Ala_racemase
IPR009006 Ala_racemase/Decarboxylase_C
IPR011079 Ala_racemase_C
IPR001608 Ala_racemase_N
IPR020622 Ala_racemase_pyridoxalP-BS
IPR029066 PLP-binding_barrel
PfamiView protein in Pfam
PF00842 Ala_racemase_C, 1 hit
PF01168 Ala_racemase_N, 1 hit
PRINTSiPR00992 ALARACEMASE
SMARTiView protein in SMART
SM01005 Ala_racemase_C, 1 hit
SUPFAMiSSF50621 SSF50621, 1 hit
SSF51419 SSF51419, 1 hit
TIGRFAMsiTIGR00492 alr, 1 hit
PROSITEiView protein in PROSITE
PS00395 ALANINE_RACEMASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiALR_GEOSE
<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: P10724
<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: July 1, 1989
Last sequence update: November 1, 1997
Last modified: December 5, 2018
This is version 134 of the entry and version 2 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again