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Q97DY9 (ALR2_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. 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 2

EC=5.1.1.1
Gene names
Name:alr2
Ordered Locus Names:CA_C3331
OrganismClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]
Taxonomic identifier272562 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length395 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 – 395395Alanine racemase 2 HAMAP-Rule MF_01201
PRO_0000114510

Sites

Active site601Proton acceptor; specific for D-alanine By similarity
Active site2881Proton acceptor; specific for L-alanine By similarity
Binding site1581Substrate By similarity
Binding site3321Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue601N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q97DY9 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 1A13F287C5C7CE43

FASTA39544,613
        10         20         30         40         50         60 
MEKKTVYNIT NSIAISEEEA VNCNIPEVNK AEINLSQLKR NFDIIQGFLK PNTKFMAVLK 

        70         80         90        100        110        120 
GDAYGHGIRP IAKELINLKC DVFGVVRLIE AFTLRKAGIK TPIMLLAPIS PSQAAWVIRY 

       130        140        150        160        170        180 
NIIPMVDSEE IVEALDQSAS QNDTIVKLHV KINTGLNRYG VNPENAVKFI REIHEKYLHV 

       190        200        210        220        230        240 
QVDGVYTHFQ DPDYNPDFTH KQIECFNNII FQLQKQKLRP RIIHAANSTG IIRYPEAHYD 

       250        260        270        280        290        300 
MVRCGTLLFG LEHEQGQRNM PKGIKTLMEL KGRIMKVRTI RAGEAGGYGS TFVAKKDSKV 

       310        320        330        340        350        360 
AIIAFGYGDG ISRGWKEVLV AGKRVPVVNY FMDGLMVDIS NIDETVKELD EAVIVGNQGD 

       370        380        390 
ESITWLEACK SLGSYVDEQI QCITERVPKK YFYEK 

« Hide

References

[1]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001437 Genomic DNA. Translation: AAK81263.1.
PIRD97309.
RefSeqNP_349923.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97DY9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272562.CA_C3331.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK81263; AAK81263; CA_C3331.
GeneID1119513.
KEGGcac:CA_C3331.
PATRIC32041093. VBICloAce74127_3511.

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAPVELWGQ.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycCACE272562:GJIH-3427-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 nameALR2_CLOAB
AccessionPrimary (citable) accession number: Q97DY9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: October 1, 2001
Last modified: June 11, 2014
This is version 95 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