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P0A6B4 (ALR1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alanine racemase, biosynthetic

EC=5.1.1.1
Gene names
Name:alr
Ordered Locus Names:b4053, JW4013
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. Ref.7

Catalytic activity

L-alanine = D-alanine. Ref.7

Cofactor

Pyridoxal phosphate. Ref.7

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_01201

Subunit structure

Homodimer. Ref.7

Sequence similarities

Belongs to the alanine racemase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.31 mM for D-alanine Ref.7

KM=1.00 mM for L-alanine

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Alanine racemase, biosynthetic HAMAP-Rule MF_01201
PRO_0000114514

Sites

Active site341Proton acceptor; specific for D-alanine
Active site2551Proton acceptor; specific for L-alanine By similarity
Binding site1291Substrate
Binding site3031Substrate; via amide nitrogen

Amino acid modifications

Modified residue341N6-(pyridoxal phosphate)lysine By similarity
Modified residue1221N6-carboxylysine HAMAP-Rule MF_01201

Experimental info

Mutagenesis1641D → A: Slightly reduces affinity for D-Ala and L-Ala. Ref.7
Mutagenesis1641D → K: Reduces catalytic activity. Slightly reduces affinity for D-Ala and L-Ala. Ref.7
Mutagenesis1651E → A: Slightly reduces affinity for D-Ala and L-Ala. Ref.7
Mutagenesis1651E → K: Reduces catalytic activity. Slightly reduces affinity for D-Ala and L-Ala. Ref.7
Mutagenesis2191P → A: No effect on catalytic activity. No effect on affinity for D-Ala and L-Ala. Ref.7
Mutagenesis2211E → A, K or P: Slightly increases catalytic activity. Slightly increases affinity for D-Ala and L-Ala. Ref.7

Secondary structure

....................................................................... 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6B4 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: FDE9B438115342C2

FASTA35939,153
        10         20         30         40         50         60 
MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP DADAFGVARL 

        70         80         90        100        110        120 
EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH NEEQLAALEE ASLDEPVTVW 

       130        140        150        160        170        180 
MKLDTGMHRL GVRPEQAEAF YHRLTQCKNV RQPVNIVSHF ARADEPKCGA TEKQLAIFNT 

       190        200        210        220        230        240 
FCEGKPGQRS IAASGGILLW PQSHFDWVRP GIILYGVSPL EDRSTGADFG CQPVMSLTSS 

       250        260        270        280        290        300 
LIAVREHKAG EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR 

       310        320        330        340        350 
VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT SRVAMKYVD 

« Hide

References

« Hide 'large scale' references
[1]"The 92-min region of the Escherichia coli chromosome: location and cloning of the ubiA and alr genes."
Lilley P.E., Stamford N.P., Vasudevan S.G., Dixon N.E.
Gene 129:9-16(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Nucleotide sequence of dnaB and the primary structure of the dnaB protein from Escherichia coli."
Nakayama N., Arai N., Bond M.W., Kaziro Y., Arai K.
J. Biol. Chem. 259:97-101(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[6]"Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene."
Kuramitsu S., Inoue K., Ogawa T., Ogawa H., Kagamiyama H.
Biochem. Biophys. Res. Commun. 133:134-139(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 320-359.
Strain: K12.
[7]"Residues Asp164 and Glu165 at the substrate entryway function potently in substrate orientation of alanine racemase from E. coli: Enzymatic characterization with crystal structure analysis."
Wu D., Hu T., Zhang L., Chen J., Du J., Ding J., Jiang H., Shen X.
Protein Sci. 17:1066-1076(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEXES WITH D-CYCLOSERINE AND PYRIDOXAL PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-34, MUTAGENESIS OF ASP-164; GLU-165; PRO-219 AND GLU-221, CARBOXYLATION AT LYS-122.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00006 Genomic DNA. Translation: AAC43147.1.
U00096 Genomic DNA. Translation: AAC77023.1.
AP009048 Genomic DNA. Translation: BAE78055.1.
K01174 Genomic DNA. No translation available.
M12047 Genomic DNA. No translation available.
PIRPC1296. D65213.
RefSeqNP_418477.1. NC_000913.2.
YP_492196.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RJGX-ray2.40A/B/C/D1-359[»]
2RJHX-ray2.40A/B/C/D1-359[»]
3B8TX-ray3.00A/B/C/D1-359[»]
3B8UX-ray3.00A/B/C/D1-359[»]
3B8VX-ray2.60A/B/C/D1-359[»]
3B8WX-ray2.70A/B/C/D1-359[»]
ProteinModelPortalP0A6B4.
SMRP0A6B4. Positions 1-359.
ModBaseSearch...

Protein-protein interaction databases

IntActP0A6B4. 6 interactions.
STRING511145.b4053.

Proteomic databases

PaxDbP0A6B4.
PRIDEP0A6B4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77023; AAC77023; b4053.
BAE78055; BAE78055; BAE78055.
GeneID12931829.
948564.
KEGGecj:Y75_p3940.
eco:b4053.
PATRIC32123645. VBIEscCol129921_4171.

Organism-specific databases

EchoBASEEB0001.
EcoGeneEG10001. alr.

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMAHQLETAV.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycEcoCyc:ALARACEBIOSYN-MONOMER.
ECOL316407:JW4013-MONOMER.
MetaCyc:ALARACEBIOSYN-MONOMER.
SABIO-RKP0A6B4.
UniPathwayUPA00042; UER00497.
UPA00219.

Gene expression databases

GenevestigatorP0A6B4.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
HAMAPMF_01201. Ala_racemase.
InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
[Graphical view]
PfamPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSPR00992. ALARACEMASE.
SMARTSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP0A6B4.
ChEMBLCHEMBL2833.
EvolutionaryTraceP0A6B4.

Entry information

Entry nameALR1_ECOLI
AccessionPrimary (citable) accession number: P0A6B4
Secondary accession number(s): P29743, P78136, Q2M6Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families