Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q1CST1 (ALR_HELPH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:HPAG1_0924
OrganismHelicobacter pylori (strain HPAG1) [Complete proteome] [HAMAP]
Taxonomic identifier357544 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length377 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
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 – 377377Alanine racemase HAMAP-Rule MF_01201
PRO_1000065993

Sites

Active site371Proton acceptor; specific for D-alanine By similarity
Active site2711Proton acceptor; specific for L-alanine By similarity
Binding site1351Substrate By similarity
Binding site3191Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue371N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1CST1 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 2B87724DE32EA433

FASTA37741,730
        10         20         30         40         50         60 
MLKRASFVEV NSASLRHNFS AVKSIVPKDA HIMAVVKANA YGAGAIKASE IFLQEGANYL 

        70         80         90        100        110        120 
GVAALDEALE LRSHFPKTPI LILGYSPNAN ASMLIDNDLS AMVFSLEQAE VFSQMALKSQ 

       130        140        150        160        170        180 
KRLKVHLKID TGMHRLGLEP NFKSIETIKK IRALKGLEIE GIFTHLSNAD AKIKTHAKNQ 

       190        200        210        220        230        240 
MKAFNAFLEQ LLDQKIEFQY RHAYNSAGIL SLCNGNENRL LNLYRPGIML YGFYPSNGMK 

       250        260        270        280        290        300 
ESCPTILKNV ISLKAQIVQI RSVKKGEFIG YGEHFYTNEE TLVGVLALGY ADGLMRALGN 

       310        320        330        340        350        360 
RIQVAINNQL APLIGKVCMD QCFVKLNDIQ AKEGDEVILF GDKSARANDA SEIAALLNTI 

       370 
AYETISTLSK RLERVYI 

« Hide

References

[1]"The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression."
Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HPAG1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000241 Genomic DNA. Translation: ABF84991.1.
RefSeqYP_627665.1. NC_008086.1.

3D structure databases

ProteinModelPortalQ1CST1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357544.HPAG1_0924.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF84991; ABF84991; HPAG1_0924.
GeneID4098551.
KEGGhpa:HPAG1_0924.
PATRIC20603231. VBIHelPyl56048_0960.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAINNQLAP.
OrthoDBEOG6PP9NJ.
ProtClustDBCLSK496287.

Enzyme and pathway databases

BioCycHPYL357544:GH1F-938-MONOMER.
UniPathwayUPA00042; UER00497.

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. SSF50621. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR_HELPH
AccessionPrimary (citable) accession number: Q1CST1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 11, 2006
Last modified: February 19, 2014
This is version 59 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