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P06191 (ALR2_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine racemase, catabolic

EC=5.1.1.1
Gene names
Name:dadX
Synonyms:dadB
Ordered Locus Names:STM1802
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. 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

Subunit structure

Monomer.

Induction

By alanine. HAMAP MF_01201

Sequence similarities

Belongs to the alanine racemase family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processalanine metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionalanine racemase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Alanine racemase, catabolic HAMAP MF_01201
PRO_0000114561

Sites

Active site351Proton acceptor; specific for D-alanine By similarity
Active site2531Proton acceptor; specific for L-alanine By similarity

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine HAMAP MF_01201

Sequences

Sequence LengthMass (Da)Tools
P06191 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 43DF23205EF25C69

FASTA35638,804
        10         20         30         40         50         60 
MTRPIQASLD LQVMKQNLAI VRRAAPEARV WSVVKANAYG HGIERVWSAL GATDGFAMLN 

        70         80         90        100        110        120 
LEEAITLRER GWKGPILMLE GFFHAQDLEA YDTYRLTTCI HSNWQLKALQ NARLNAPLDI 

       130        140        150        160        170        180 
YVKVNSGMNR LGFQPERAQT VWQQLRAMRN VGEMTLMSHF AQADHPEGIG EAMRRIALAT 

       190        200        210        220        230        240 
EGLQCAYSLS NSAATLWHPQ AHYDWVRPGI ILYGASPSGQ WRDIADTGLK PVMTLSSEII 

       250        260        270        280        290        300 
GVQTLSAGER VGYGGGYSVT QEQRIGIVAA GYADGYPRHA PTGTPVLVDG IRTRTVGTVS 

       310        320        330        340        350 
MDMLAVDLTP CPQAGIGTPV ELWGKEIKVD DVASAAGTLG YELLCAVAPR VPFVTT 

« Hide

References

« Hide 'large scale' references
[1]"Catabolic alanine racemase from Salmonella typhimurium: DNA sequence, enzyme purification, and characterization."
Wasserman S.A., Daub E., Grisafi P., Botstein D., Walsh C.T.
Biochemistry 23:5182-5187(1984) [PubMed: 6391537] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Inactivation of the dadB Salmonella typhimurium alanine racemase by D and L isomers of beta-substituted alanines: kinetics, stoichiometry, active site peptide sequencing, and reaction mechanism."
Badet B., Roise D., Walsh C.T.
Biochemistry 23:5188-5194(1984) [PubMed: 6439236] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-44.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02119 Genomic DNA. Translation: AAA27054.1.
AE006468 Genomic DNA. Translation: AAL20717.1.
PIRA29519.
RefSeqNP_460758.1. NC_003197.1.

3D structure databases

ProteinModelPortalP06191.
ModBaseSearch...

Proteomic databases

PRIDEP06191.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1253321.
GenomeReviewsGene locus STM1802 in contig AE006468_GR.
KEGGstm:STM1802.
PATRIC32382125. VBISalEnt20916_1901.

Phylogenomic databases

HOGENOMHBG712172.
OMASVELWGD.
ProtClustDBPRK03646.

Enzyme and pathway databases

BioCycSTYP99287:STM1802-MONOMER.

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 nameALR2_SALTY
AccessionPrimary (citable) accession number: P06191
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: January 25, 2012
This is version 92 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