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Reviewed, UniProtKB/Swiss-Prot P0A6B6 (ALR1_SHIBO)

Last modified February 9, 2010. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alanine racemase, biosynthetic
    EC=5.1.1.1
Gene names
Name: alr
OrganismShigella boydii
Taxonomic identifier621 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

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. HAMAP MF_01201

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. HAMAP MF_01201

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_0000114563

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

Sequences

Sequence LengthMass (Da)Tools
P0A6B6-1 [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

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB070926 Genomic DNA. Translation: BAB71771.1.

3D structure databases

SMRP0A6B6. Positions 1-359.
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.1.1.1. 96885.

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]
PfamPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSPR00992. ALARACEMASE.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR1_SHIBO
AccessionPrimary (citable) accession number: P0A6B6
Secondary accession number(s): P29743, P78136
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: February 9, 2010
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents