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Q8EX97 (ALR_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 82. 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

EC=5.1.1.1
Gene names
Name:alr
Ordered Locus Names:LB_317
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) [Reference proteome] [HAMAP]
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids By similarity. HAMAP-Rule MF_01201

Catalytic activity

L-alanine = D-alanine. HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201

Pathway

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

Sequence similarities

Belongs to the alanine racemase family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processD-alanine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionalanine racemase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 389389Alanine racemase HAMAP-Rule MF_01201
PRO_0000114531

Sites

Active site481Proton acceptor; specific for D-alanine By similarity
Active site2811Proton acceptor; specific for L-alanine By similarity
Binding site1441Substrate By similarity
Binding site3291Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue481N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8EX97 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: B44569674B85B3BF

FASTA38943,278
        10         20         30         40         50         60 
MQDINSGSSS MKDTYSSWIE ISKRSLSNNL DNFRSILRPN STLTAILKSN AYGHGIEPMT 

        70         80         90        100        110        120 
RLCIEAGISR IGVNSIEEAL LIRNIDSKIP ILIMGEIQNP EKRKDVLSDP NFWIVFSRPE 

       130        140        150        160        170        180 
TARILSSFLP APKLHLKIDT GMGRLGSHGE TLKQTLSELK NVGITLGGIC THFASTEDVL 

       190        200        210        220        230        240 
EHKYSLMQTQ KFEEAIFLAK SFGYNHLIRH ACASASTMLF PNAHFDMVRI GISLYGLWPS 

       250        260        270        280        290        300 
IQTRLSLNLT GNKNFQLNPI LSWKSRIVHI QYHPADSYIG YGSTFQTSYP TKVAIVPVGY 

       310        320        330        340        350        360 
YEGLDRKLSS NGDMLVLGKK ARIIGRICMN MTMLDVTHIP GAEVGSIVTI IGQDGEESIT 

       370        380 
ADDLADRTHT INYEVMTRIS ESIPRIVVD 

« Hide

References

[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010301 Genomic DNA. Translation: AAN51876.1.
RefSeqNP_714861.1. NC_004343.2.

3D structure databases

ProteinModelPortalQ8EX97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189518.LB317.

Proteomic databases

PaxDbQ8EX97.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN51876; AAN51876; LB_317.
GeneID1153876.
KEGGlil:LB_317.
PATRIC22390170. VBILepInt91350_4636.

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMALWQLEAI.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycLINT189518:GJBB-3710-MONOMER.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
3.20.20.10. 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.
IPR029066. PLP-binding_barrel.
[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. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR_LEPIN
AccessionPrimary (citable) accession number: Q8EX97
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways