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P0A6B5 (ALR1_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:SF4152, S3578
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

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

General annotation (Comments)

Function

Provides the D-alanine required for cell wall biosynthesis. HAMAP MF_01201

Catalytic activity

L-alanine = D-alanine. HAMAP MF_01201

Cofactor

Pyridoxal phosphate.

Pathway

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

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_01201

Subunit structure

Monomer but homodimer in the presence of the substrate.

Sequence similarities

Belongs to the alanine racemase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8-10. HAMAP MF_01201

Temperature dependence:

Optimum temperature is 50 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Alanine racemase, biosynthetic HAMAP MF_01201
PRO_0000114565

Sites

Active site341Proton acceptor; specific for D-alanine By similarity
Active site2551Proton acceptor; specific for L-alanine By similarity

Amino acid modifications

Modified residue341N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict1381E → G in BAB71772. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0A6B5 [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]"Gene cloning and characterization of alanine racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei."
Yokoigawa K., Hirasawa R., Ueno H., Okubo Y., Umesako S., Soda K.
Biochem. Biophys. Res. Commun. 288:676-684(2001) [PubMed: 11676496] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, CHARACTERIZATION.
[2]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[3]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB070927 Genomic DNA. Translation: BAB71772.1.
AE005674 Genomic DNA. Translation: AAN45574.1.
AE014073 Genomic DNA. Translation: AAP18624.1.
RefSeqNP_709867.1. NC_004337.2.
NP_838813.1. NC_004741.1.

3D structure databases

ProteinModelPortalP0A6B5.
SMRP0A6B5. Positions 1-359.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000087995; EBESCP00000084817; EBESCG00000087040.
EBESCT00000092946; EBESCP00000089582; EBESCG00000091990.
GeneID1025471.
1079800.
GenomeReviewsGene locus SF4152 in contig AE005674_GR.
Gene locus S3578 in contig AE014073_GR.
KEGGsfl:SF4152.
sfx:S3578.
PATRIC18708936. VBIShiFle31049_3906.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009862.
HOGENOMHBG712172.
OMAEGTPVWV.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycSFLE198214:AAN45574.1-MONOMER.
BRENDA5.1.1.1. 5712.

Family and domain databases

HAMAPMF_01201. Ala_racemase.
[Tree]
InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
[Graphical view]
Gene3DG3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 1 hit.
KOK01775.
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...

Entry information

Entry nameALR1_SHIFL
AccessionPrimary (citable) accession number: P0A6B5
Secondary accession number(s): P29743, P78136
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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